KR20230003072A - 조작된 효소 및 이의 이용 및 제조 방법 - Google Patents

조작된 효소 및 이의 이용 및 제조 방법 Download PDF

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KR20230003072A
KR20230003072A KR1020227041382A KR20227041382A KR20230003072A KR 20230003072 A KR20230003072 A KR 20230003072A KR 1020227041382 A KR1020227041382 A KR 1020227041382A KR 20227041382 A KR20227041382 A KR 20227041382A KR 20230003072 A KR20230003072 A KR 20230003072A
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naturally occurring
microbial organism
occurring microbial
amino acid
hmd
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아밋 마헨드라 샤
더챵 장
조셉 로이 워너
벤자민 매튜 그리핀
러셀 스콧 코모르
하리시 나가라잔
상카 가탁
토비 하워드 리처드슨
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Abstract

본 발명은 조작된 카르복시산 리덕타제 (CAR) 효소, CAR 효소를 코딩하는 핵산, 및 CAR, 조작된 트랜스아미나제 (TA) 효소 및/또는 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소를 코딩하는 외인성 핵산을 포함하는 비-천연성 미생물 유기체를 제공한다. 본 발명은 6-아미노카프로에이트 세미알데하이드, HDO 또는 이 둘다를 생산하기 위해 충분한 양으로 발현되는 1,6-헥산다이올 (HDO) 경로 효소를 가진 HDO 경로를 포함하는 비-천연성 미생물 유기체를 제공한다. 본 발명은 6-아미노카프로에이트 세미알데하이드, HMD 또는 이 둘다를 생산하기 위해 충분한 양으로 발현되는 HMD 경로 효소를 가진 HMD 경로를 포함하는 비-천연성 미생물 유기체를 제공한다. 또한, 본 발명은 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO, 및 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 생산하는 방법을 제공한다.

Description

조작된 효소 및 이의 이용 및 제조 방법
관련 출원에 대한 교차 -참조
본 출원은 2020년 4월 24일자 미국 가출원 번호 63/015,428에 대해 우선권을 주장하며, 이의 내용은 그 전체가 원용에 의해 본 명세서에 포함된다.
서열목록
본 출원은 2021년 4월 20일에 생성된 파일명 12956-492-228_SEQ_LISTING.txt의 1,773,544 바이트 크기의 ASCII 텍스트 파일로서 본 출원과 함께 제출된 서열목록을 원용에 의해 포함한다.
나일론은 다이아민과 다이카르복시산의 축합 중합 또는 락탐의 축합 중합에 의해 합성할 수 있는 폴리아미드이다. 나일론 6,6은 헥사메틸렌다이아민 (HMD) 및 아디프산의 반응을 통해 제조되는 반면, 나일론 6는 카프로락탐의 개환 중합을 통해 만들어진다. 즉, 아디프산, 헥사메틸렌다이아민 및 카프로락탐은 나일론 생산에 중요한 중간산물이다.
미생물은 나일론 중간산물들 중 일부를 생산하기 위해 조작되어 왔다. 그러나, 조작된 미생물은 경로 중간산물 및 최종 산물에 대한 부적절한 효소 활성의 결과로서 부적절한 부산물을 만들 수 있다. 이러한 부산물 및 불순물은 따라서 생합성 효소의 비용 및 복잡성을 높이며, 원하는 산물의 효율 및 수율을 떨어뜨릴 수 있다.
본 발명은 (a) 6-아미노카프로익산 물질로부터 6-아미노카프로에이트 세미알데하이드를, (b) 6-아미노카프로익산 물질로부터 6-아미노카프로에이트 세미알데하이드를 야생형 CAR과 비교해 더 높은 비율로 생성할 수 있으며, (c) 야생형 CAR과 비교해 6-아미노카프로익산 물질에 대해 더 높은 친화성을 가진, 또는 (a), (b), 및 (c) 중 임의 조합을 가진, 조작된 카르복시산 리덕타제 (CAR) 효소를 제공한다. 조작된 CAR 효소는 본원에 개시된 하나 이상의 잔기 위치에 하나 이상의 아미노산 변이를, 예를 들어 서열번호 152, 153 또는 254의 하나 이상의 아미노산 변이를 포함할 수 있다. 본 발명은 서열번호 152, 153 또는 254의 CAR 활성에 비해 적어도 20% 높은 활성을 가진 조작된 CAR을 제공한다.
또한, 본 발명은 프로모터에 작동가능하게 연결될 수 있으며, 벡터일 수 있는, 본원에 개시된 조작된 CAR을 코딩하는 핵산을 제공한다.
본 발명은 또한 본원에 개시된 조작된 CAR 또는 본원에 개시된 TA2에 대해 적어도 50%의 서열 동일성을 가진 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소를 코딩하는 외인성 핵산을 포함하는 비-천연성 미생물 유기체를 제공하며, 상기한 CAR은 본원에 개시된 CAR에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 가진다. 일부 측면에서, 비-천연성 미생물 유기체는 본원에 개시된 서열을 가진 조작된 트랜스아미나제 (TA) 효소, 예를 들어, 본원에 개시된 잔기들로부터 선택되는 하나 이상의 위치에 하나 이상의 아미노산 변이를 가지거나 또는 본원에 개시된 임의의 TA 서열의 적어도 25개 이상의 연속 아미노산들에 대해 적어도 50%의 서열 동일성을 가진 TA 효소를 코딩하는 외인성 핵산을 추가로 포함한다. 외인성 핵산은 이종이거나 또는 동종일 수 있다. 비-천연성 미생물 유기체는 CAR 변이체, TA2 변이체 및/또는 본원에 개시된 TA 변이체를 포함할 수 있다.
본 발명은 HMD를 생산하기 위해 충분한 양으로 발현되는 HMD 경로 효소를 가진 헥사메틸렌다이아민 (HMD) 경로를 포함하는, 본원에서 청구되는 임의의 하나의 비-천연성 미생물 유기체를 제공한다. HMD 경로는 (1) 3-옥소아디필-CoA 티올라제, (2) 하이드록시아디필-CoA 데하이드로게나제 (HBD), (3) 크로토나제, (4) 트랜스-에노일CoA 리덕타제 (TER), (5) 6ACA-알데하이드 데하이드로게나제 (6ACA-ALD), (6) 6ACA-트랜스아미나제 (TA), (7) 카르복시산 리덕타제 (CAR), 및 (8) HMD-트랜스아미나제 (TA2)를 포함한다. 비-천연성 미생물 유기체는 포스포판테테이닐 트랜스퍼라제 HMD 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 더 포함할 수 있다. 외인성 핵산은 이종의 핵산일 수 있다. 일부 측면에서, 비-천연성 미생물 유기체는 실질적인 혐기성 배양 배지 중에 존재한다. 미생물 유기체는 박테리아, 효모 또는 진균 종일 수 있다. 일부 측면에서, 비-천연성 미생물 유기체는 외인성 핵산을 가지지 않은 대조군 미생물 유기체와 비교해 6-아미노카프로에이트 세미알데하이드, HMD 또는 이 둘다를 적어도 10% 많이 생산할 수 있다. 본 발명은 외인성 핵산을 가지지 않은 대조군 미생물 유기체와 비교해 (a) 아디페이트 세미알데하이드에서 6-아미노카프로익산으로; (b) 6-아미노카프로익산에서 6-아미노카프로에이트 세미알데하이드로, 및/또는 (c) 6-아미노카프로에이트 세미알데하이드에서 HMD로 더 많이 변환하는 비-천연성 미생물 유기체를 제공한다.
본 발명은 본원에 개시된 조작된 CAR, 또는 본원에 개시된 CAR 서열의 적어도 25개 이상의 연속 아미노산들에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는 CAR을 코딩하는 외인성 핵산을 가진 비-천연성 미생물 유기체를 제공한다. 비-천연성 미생물 유기체는 (a) 서열번호 1, 13 또는 31의 아미노산의 하나 이상의 변이를 포함하는 조작된 트랜스아미나제 (TA) 효소; (b) 본원에 개시된 잔기들로부터 선택되는 하나 이상의 위치에 하나 이상의 아미노산 변이를 포함하는 조작된 TA 효소; (c) 서열번호 1의 본원에 개시된 변이로부터 선택되는 조작된 단백질의 하나 이상의 아미노산 변이 및 이들의 조합을 포함하는 조작된 TA 효소, 또는 (d) 본원에 개시된 서열의 적어도 25개 이상의 연속 아미노산들에 대해 적어도 50%의 서열 동일성을 가진 트랜스아미나제를 코딩하는 외인성 핵산을 추가로 포함할 수 있다. 외인성 핵산은 이종적이거나 또는 동종일 수 있다. 비-천연성 미생물 유기체는 본원에 개시된 CAR 변이체, 및/또는 본원에 개시된 TA 변이체의 아미노산 서열을 가진 조작된 TA로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 CAR을 포함할 수 있다. 일부 측면에서, 비-천연성 미생물 유기체는 HDO를 생산하기 위해 충분한 양으로 발현되는 HDO 경로 효소를 가진 1,6-헥산다이올 (HDO) 경로를 포함하며, 여기서 HDO 경로는 (1) 티올라제, (2) 하이드록시아디필-CoA 데하이드로게나제 (HBD), (3) 크로토나제, (4) 트랜스-에노일CoA 리덕타제 (TER), (5) 6ACA-알데하이드 데하이드로게나제 (6ACA-ALD), (6) 6ACA-트랜스아미나제 (TA), (7) 카르복시산 리덕타제 (CAR), (8) 6-아미노카프로에이트 세미알데하이드 리덕타제, (9) 6-아미노헥사놀 아미노트랜스퍼라제 또는 옥시도리덕타제, 및 (10) 6-하이드록시헥사날 리덕타제를 포함한다. 비-천연성 미생물 유기체는 포스포판테테이닐 트랜스퍼라제 HDO 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 추가로 포함할 수 있다. 외인성 핵산은 이종의 핵산일 수 있다. 일부 측면에서, 비-천연성 미생물 유기체는 실질적으로 혐기성 배양 배지에 존재한다. 미생물 유기체는 박테리아, 효모 또는 진균 종일 수 있다. 일부 측면에서, 비-천연성 미생물 유기체는 본원에 개시된 외인성 핵산을 포함하지 않는 대조군 미생물 유기체와 비교해 6-아미노카프로에이트 세미알데하이드, HDO 또는 이 둘다를 적어도 10% 많이 생산할 수 있다. 본원에 제공되는 비-천연성 미생물 유기체는 본원에 개시된 외인성 핵산을 포함하지 않는 대조군 미생물 유기체와 비교해 (a) 아디페이트 세미알데하이드를 6-아미노카프로익산으로, 및/또는 (b) 6-아미노카프로익산을 6-아미노카프로에이트 세미알데하이드로 더 많이 변환한다.
본 발명은 본원에 개시된 비-천연성 미생물 유기체를 HMD를 생산하기 위해 충분한 기간 동안 조건 하에 배양하는 것을 포함하는, 헥사메틸렌다이아민 (HMD) 생산 방법을 추가로 제공한다. 또한, 본 발명은 본원에 개시된 비-천연성 미생물 유기체를 HDO를 생산하기 위해 충분한 기간 동안 조건 하에 배양하는 것을 포함하는, 1,6-헥산다이올 (HDO) 생산 방법을 제공한다. 일부 측면에서, 본 방법은 배양물에서 다른 성분들로부터 HMD 또는 HDO를 분리하는 단계를 추가로 포함한다. 분리는 추출, 연속 액체-액체 추출, 투과 증발, 막 여과, 막 분리, 역 삼투압, 전기투석, 증류, 결정화, 원심분리, 추출 여과, 이온 교환 크로마토그래피, 흡착 크로마토그래피 또는 한외여과를 포함할 수 있다.
본 발명은 생물유래 (bioderived) HMD, 6-아미노카프로에이트 세미알데하이드, 및/또는 대기 CO2 흡수 소스를 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진 HDO를 포함하는 배양물 배지 (culture medium)를 제공한다. 일부 측면에서, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드, 및/또는 HDO는 본원에 개시된 비-천연성 미생물 유기체 또는 본원에 개시된 방법에 의해 생산된다. 일부 측면에서, 배양물 배지는 본원에 개시된 조작된 CAR, 조작된 TA 효소, 조작된 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소, 및/또는 알데하이드 데하이드로게나제 (ALD) 효소를 포함한다. 일부 측면에서, 배양 배지는 본원에 개시된 조작된 CAR, 조작된 TA 효소, 조작된 TA2 효소, 및/또는 알데하이드 데하이드로게나제 (ALD) 효소를 코딩하는 핵산을 함유한다. 일부 측면에서, 배양 배지는 본원에 개시된 비-천연성 미생물 유기체를 함유한다. 배양 배지는 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 생산하는 비-천연성 미생물 유기체로부터 분리될 수 있다.
본 발명은 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 대기 CO2 흡수 소스를 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진 HDO를 추가로 제공한다. 일부 측면에서, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO는 본원에 개시된 비-천연성 미생물 유기체 및/또는 방법에 의해 생산된다. 일부 측면에서, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO는 Fm 값이 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95% 또는 적어도 98%이다. 본 발명은 또한 본원에 개시된 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO, 및 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO 이외의 다른 화합물을 포함하는 조성물을 제공한다. 조성물은 본원에 개시된 비-천연성 미생물 유기체 또는 세포 용해물 또는 배양 상층액의 일부를 함유할 수 있다.
도 1은 숙시닐-CoA 및 아세틸-CoA로부터 6-아미노카프로에이트, 헥사메틸렌다이아민 (HMD) 및 카프로락탐까지의 예시적인 경로를 도시한다. 효소는 다음과 같이 명명된다: A) 3-옥소아디필-CoA 티올라제, B) 3-옥소아디필-CoA 리덕타제, C) 3-하이드록시아디필-CoA 데하이드라타제, D) 5-카르복시-2-펜테노일-CoA 리덕타제, E) 3-옥소아디필-CoA/아실-CoA 트랜스퍼라제, F) 3-옥소아디필-CoA 신타제, G) 3-옥소아디필-CoA 하이드롤라제, H) 3-옥소아디페이트 리덕타제, I) 3-하이드록시아디페이트 데하이드라타제, J) 5-카르복시-2-펜테노에이트 리덕타제, K) 아디필-CoA/아실-CoA 트랜스퍼라제, L) 아디필-CoA 신타제, M) 아디필-CoA 하이드롤라제, N) 아디필-CoA 리덕타제 (알데하이드 생성), O) 6-아미노카프로에이트 트랜스아미나제, P) 6-아미노카프로에이트 데하이드로게나제, Q) 6-아미노카프로일-CoA/아실-CoA 트랜스퍼라제, R) 6-아미노카프로일-CoA 신타제, S) 아미도하이드롤라제, T) 자발적인 고리화, U) 6-아미노카프로일-CoA 리덕타제 (알데하이드 생성), V) HMD 트랜스아미나제, W) HMD 데하이드로게나제, X) 아디페이트 리덕타제, Y) 아디페이트 키나제, Z) 아디필포스페이트 리덕타제.
도 2는 서열번호 1에서 돌연변이되는 아미노산 위치를 나타낸 도표이다.
도 3은 야생형 서열번호 1 대조군 (서열번호 1)과 비교해 변이체의 활성을 나타낸 도표이다.
도 4는 출발 지점으로서 라이신을 이용한 6-아미노 카프로익산 및 아디페이트 합성 경로의 예를 도시한다.
도 5는 출발 지점으로서 아디필-CoA를 이용한 카프로락탐 합성 경로의 예를 도시한다.
도 6은 피루베이트 및 숙시닉 세미알데하이드로부터 6-아미노카프로에이트 합성 경로의 예를 도시한다. 효소는 다음과 같다: A) HODH 알돌라제, B) OHED 하이드라타제, C) OHED 리덕타제, D) 2-OHD 데카르복실라제, E) 아디페이트 세미알데하이드 아미노트랜스퍼라제 및/또는 아디페이트 세미알데하이드 옥시도리덕타제 (아민화), F) OHED 데카르복실라제, G) 6-OHE 리덕타제, H) 2-OHD 아미노트랜스퍼라제 및/또는 2-OHD 옥시도리덕타제 (아민화), I) 2-AHD 데카르복실라제, J) OHED 아미노트랜스퍼라제 및/또는 OHED 옥시도리덕타제 (아민화), K) 2-AHE 리덕타제, L) HODH 포르메이트-리아제 및/또는 HODH 데하이드로게나제, M) 3-하이드록시아디필-CoA 데하이드라타제, N) 2,3-데하이드로아디필-CoA 리덕타제, O) 아디필-CoA 데하이드로게나제, P) OHED 포르메이트-리아제 및/또는 OHED 데하이드로게나제, Q) 2-OHD 포르메이트-리아제 및/또는 2-OHD 데하이드로게나제. 약어는 다음과 같다: HODH = 4-하이드록시-2-옥소헵탄-1,7-다이오에이트, OHED = 2-옥소헵트-4-엔-1,7-다이오에이트, 2-OHD = 2-옥소헵탄-1,7-다이오에이트, 2-AHE = 2-아미노헵트-4-엔-1,7-다이오에이트, 2-AHD = 2-아미노헵탄-1,7-다이오에이트, 및 6-OHE = 6-옥소헥스-4-에노에이트.
도 7은 6-아미노카프로페이트로부터 헥사메틸렌다이아민 합성 경로의 예를 도시한다. 효소는 다음과 같다: A) 6-아미노카프로에이트 키나제, B) 6-AHOP 옥시도리덕타제, C) 6-아미노카프로익 세미알데하이드 아미노트랜스퍼라제 및/또는 6-아미노카프로익 세미알데하이드 옥시도리덕타제 (아민화), D) 6-아미노카프로에이트 N-아세틸트랜스퍼라제, E) 6-아세트아미도헥사노에이트 키나제, F) 6-AAHOP 옥시도리덕타제, G) 6-아세트아미도헥사날 아미노트랜스퍼라제 및/또는 6-아세트아미도헥사날 옥시도리덕타제 (아민화), H) 6-아세트아미도헥산아민 N-아세틸트랜스퍼라제 및/또는 6-아세트아미도헥산아민 하이드롤라제 (아미드), I) 6-아세트아미도헥사노에이트 CoA 트랜스퍼라제 및/또는 6-아세트아미도헥사노에이트 CoA 리가제, J) 6-아세트아미도헥사노일-CoA 옥시도리덕타제, K) 6-AAHOP 아실트랜스퍼라제, L) 6-AHOP 아실트랜스퍼라제, M) 6-아미노카프로에이트 CoA 트랜스퍼라제 및/또는 6-아미노카프로에이트 CoA 리가제, N) 6-아미노카프로일-CoA 옥시도리덕타제. 약어는 다음과 같다: 6-AAHOP = [(6-아세트아미도헥사노일)옥시]포스포네이트 및 6-AHOP = [(6-아미노헥사노일)옥시]포스포네이트.
도 8은 1.6-헥산다이올 생합성 경로의 예를 도시한다. A)는 6ACA → 6-아미노카프로일-CoA 변환을 촉매하는 6-아미노카프로일-CoA 트랜스퍼라제 또는 신테타제이고; B) 6-아미노카프로일-CoA → 6-아미노카프로에이트 세미알데하이드 변환을 촉매하는 6-아미노카프로일-CoA 리덕타제이고; C) 6-아미노카프로에이트 세미알데하이드 → 6-아미노헥사놀 변환을 촉매하는 6-아미노카프로에이트 세미알데하이드 리덕타제이고; D) 6ACA → 6-아미노카프로에이트 세미알데하이드 변환을 촉매하는 6-아미노카프로에이트 리덕타제이고; E) 아디필-CoA → 아디페이트 세미알데하이드 변환을 촉매하는 아디필-CoA 리덕타제이고; F) 아디페이트 세미알데하이드 → 6-하이드록시헥사노에이트 변환을 촉매하는 아디페이트 세미알데하이드 리덕타제이고; G) 6-하이드록시헥사노에이트 → 6-하이드록시헥사노일-CoA 변환을 촉매하는 6-하이드록시헥사노일-CoA 트랜스퍼라제 또는 신테타제이고; H) 6-하이드록시헥사노일-CoA → 6-하이드록시헥사날 변환을 촉매하는 6-하이드록시헥사노일-CoA 리덕타제이고; I) 6-하이드록시헥사날 → HDO 변환을 촉매하는 6-하이드록시헥사날 리덕타제이고; J) 6-아미노헥사놀 → 6-하이드록시헥사날 변환을 촉매하는 6-아미노헥사놀 아미노트랜스퍼라제 또는 옥시도리덕타제이고; K) 6-하이드록시헥사노에이트 → 6-하이드록시헥사날 변환을 촉매하는 6-하이드록시헥사노에이트 리덕타제이고; L) ADA → 아디페이트 세미알데하이드 변환을 촉매하는 아디페이트 리덕타제이고; M) 아디필-CoA → ADA 변환을 촉매하는 아디필-CoA 트랜스퍼라제, 하이드롤라제 또는 신타제이다.
도 9는 아디페이트 또는 아디필-CoA에서 카프로락톤 합성 경로의 예를 도시한다. 효소는 다음과 같다: A. 아디필-CoA 리덕타제, B. 아디페이트 세미알데하이드 리덕타제, C. 6-하이드록시헥사노일-CoA 트랜스퍼라제 또는 신테타제, D. 6-하이드록시헥사노일-CoA 사이클라제 또는 자발적인 고리화, E. 아디페이트 리덕타제, F. 아디필-CoA 트랜스퍼라제, 신테타제 또는 하이드롤라제, G. 6-하이드록시헥사노에이트 사이클라제, H. 6-하이드록시헥사노에이트 키나제, I. 6-하이드록시헥사노일 포스페이트 사이클라제 또는 자발적인 고리화, J. 포스포트랜스-6-하이드록시헥사노일라제.
도 10은 헥사메틸렌다이아민 (HMD) 생합성 경로의 예를 도시한다. 숙시닐-CoA 및 아세틸-CoA에서 시작하며, 효소들은 다음과 같이 언급된다: (A) 티올라제; (B) 하이드록시아디필-CoA 데하이드로게나제 (HBD); (C) 크로토나제; (D) 트랜스-에노일-CoA 리덕타제 (Ter); (E) 6ACA-알데하이드 데하이드로게나제 (ALD); (F) 6ACA-트랜스아미나제 (TA); (G) CoA 트랜스퍼라제/CoA 리가제; (H) HMD-알데하이드 데하이드로게나제 (ALD); (I) 카르복시산 리덕타제 (CAR), 및 (J) HMD-트랜스아미나제 (TA2). PPTase는 포스포판테테이닐 트랜스퍼라제이다.
도 11은 4 탄소 기질 (부티레이트, 4-하이드록시부티레이트 (4-HB, 숙시네이트 및 4-아미노부티르산 (GABA)) 및 6 탄소 기질 (헥사노에이트, 6-하이드록시카프로익산, 아디페이트 및 6ACA)에 대한 마이코박테리움 아비움 유래 CAR 상동체 (서열번호 153)에 대한 효소 활성을 나타낸 것이다.
도 12는 표 9에 나타낸 변이체 1과 비교해 마이코박테리움 아비움 유래 CAR 상동체 (서열번호 153; 모 균주)의 효소 활성을 나타낸 것이다.
달리 정의되지 않은 한, 본원에서 사용되는 모든 기술 용어 및 과학 용어들은 본 발명의 구현예들이 속하는 기술 분야의 당업자들에게 통상적으로 이해되는 의미와 동일한 의미를 가진다. 본원에 기술된 것과 비슷하거나 또는 균등한 임의의 방법, 기구 및 물질은 본 발명의 구현예를 실시하는데 이용할 수 있다. 아래 정의들은 본원에 빈번하게 사용되는 일부 용어들을 이해하는데 도움을 주기 위해 제공되나, 본 발명의 범위를 제한하는 것으로 의도되는 것은 아니다. 본원에서 참조되는 모든 문헌들 (예, 특허 출원 또는 특허)은 그 전체가 원용에 의해 본 명세서에 포함된다.
아미노 도너 물질의 1차 아민으로부터 아미노 어셉터 분자의 카르보닐 기로 아미노 기, 전자 한쌍 및 프로톤을 전달하는 과정을 촉매하는 트랜스아미나제 (E.C. 2.6.1)로도 알려져 있는 아미노트랜스퍼라제를 기술한다. 트랜스아미나제의 바람직한 반응은 글루타메이트 또는 알라닌의 아미노 기를 아디페이트 세미알데하이드로 전달하여 6-아미노카프로익산 (6ACA)을 생성하는 것으로, 다음과 같이 표시된다:
아디페이트 세미알데하이드 + 글루타메이트 → 6ACA + α-케토글루타르산
그러나, 트랜스아미나제는 또한 다음과 같이 표시되는 바와 같이 숙시네이트 세미알데하이드 또는 피루베이트에 특이성을 가진다:
숙시네이트 세미알데하이드 + 글루타메이트 → γ-아미노부티르산 + α-케토글루타르산
피루베이트 + 글루타메이트 → 알라닌 + α-케토글루타르산
알라닌이 아민 도너로서 글루타메이트를 대신할 수 있다.
언급된 트랜스아미나제 (TA) 효소는 아디페이트 세미알데하이드 기질에 활성을 나타내어 6-아미노카프로익산을 합성하는 것으로 동정되었다. 이 효소는 아마 나일론 중간산물로 이어지는 다양한 경로들에 이용가능할 수 있다.
언급된 트랜스아미나제는 상동성 연구뿐 아니라 이 경로에서 6ACA를 합성하는 원하는 반응을 수행할 수 있는 효소에 대한 메타게놈 발견으로 동정되었다. 트랜스아미나제의 아디페이트 세미알데하이드 이용성을 조사하기 위해, 일부 구현예에서, 분석은 본원에 예시된 바와 같이 6ACA 또는 다른 후보 물질을 이용해 정방향 또는 역방향으로 수행할 수 있다. 분석은 당해 기술 분야에 잘 알려진 방법을 이용해 효소학적 산물을 직접 또는 간접적으로 측정함으로써 수행될 수 있다. 한가지 예시적인 방법은 아래에, 그리고 실시예에 예시된 간접적인 방법이다.
일부 구현예에서, 서열번호 1에 의해 코딩되는 트랜스아미나제 효소를 아크로모박터 크실로스옥시단스 (Achromobacter xylosoxidans)로부터 동정하였다. 다른 TA 효소를 동정하기 위해, 서열번호 1을 이용하였다. 상동성 효소들이 표 6에 기재된 바와 같이 동정되었다. 일부 구현예에서, 트랜스아미나제 효소 또는 서열은 BLAST에 의해 동정한다. 일부 구현예에서, 트랜스아미나제는 표 6의 트랜스아미나제의 아미노산 서열들의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, 표 6에 동정된 트랜스아미나제는 서열번호 1, 13 또는 31의 트랜스아미나제 아미노산 서열들의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, 트랜스아미나제 효소는 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116 중 임의의 서열에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50%의 아미노산 서열 동일성을 가진다. 일부 구현예에서, 아디페이트 세미알데하이드와 반응하여 6ACA를 합성하는 트랜스아미나제 효소의 아미노산 서열은 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116의 아미노산 서열들로부터 선택된다.
일부 구현예에서, TA 효소의 촉매 효율 및/또는 기질로서 아디페이트 세미알데하이드의 대사회전수 (turnover number)는 숙시네이트 세미알데하이드를 기질로 사용할 경우와 비슷하다. 일부 구현예에서, 기질로서 숙시네이트 세미알데하이드를 이용한 경우와 유사하게, 기질로서 아디페이트 세미알데하이드에 대한 대사회전수 및/또는 촉매 효율을 가진 효소는, 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116의 트랜스아미나제의 아미노산 서열들의 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상의 연속 아미노산에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
본원에 언급된 임의 효소와 관련하여 사용되는 바와 같이, 용어 대사회전수 (kcat으로도 지칭됨)는 주어진 효소 농도 [ET]에 대해 단일 촉매 부위에서 이루어지는 분당 기질 분자의 최대 화학적 변환 횟수로서 정의된다. 이는 아래와 같이 최대 반응 속도 Vmax 및 촉매 부위 농도 [ET]로부터 계산할 수 있다:
Kcat = Vmax/[ET]. 단위는 s-1이다.
본원에 언급된 임의 효소와 관련하여 사용되는 바와 같이, 용어 "촉매 효율"은 효소가 기질을 생산물로 변환하는 효율의 척도이다. 촉매 효율의 비교는 또한 여러가지 기질들에 대한 효소의 선호성 (예, 기질 특이성) 척도로도 이용할 수 있다. 촉매 효율이 높을수록, 효소는 그 기질을 더 "선호"하는 것이다. 이는 식: kcat/KM로부터 계산할 수 있는데, 여기서 kcat는 대사회전수이고, KM은 미카엘 상수이고, KM은 반응 속도가 Vmax의 1/2일 때의 기질 농도이다. 촉매 효율의 단위는 s-1M- 1으로 나타낼 수 있다.
동정되는 트랜스아미나제 효소는 유전학적으로 매우 다양한 유기체들로부터 유래한다. 일부 예시적인 트랜스아미나제에 대한 쌍별 서열 정렬을 아래 표 1에 나타낸다.
표 1.
서열번호 1 서열번호 13 서열번호 31
서열번호 1 44% 87%
서열번호 13 44% 43%
서열번호 31 87% 43%
트랜스아미나제 효소들은 보존된 도메인을 가진다. 다중 서열 정렬 및 HMM (hidden Markov models)에 기반하여, 트랜스아미나제 효소는 유럽 생물정보학 위원회의 Pfam 데이터베이스 (pfam.xfam.org)에서 Pfam PF00202로 분류된다.
일부 구현예에서, 단백질의 결정 구조 연구를 통해 서열번호 1에서 아미노산의 돌연변이 위치를 동정하였으며, 서열번호 1을 코딩하는 유전자에 대해 선택된 아미노산 위치에서 포화 돌연변이 유발을 수행하였다. 야생형 (비-변형된) 서열번호 1보다 활성이 우수한 변이체 아미노산을 제공할 기회를 얻기 위해 촉매학적으로 관련있는 잔기들을 동정하였다.
일부 구현예에서, 트랜스아미나제 효소는 대응되는 야생형에 비해 아디페이트 세미알데하이드 기질에 대해 더 높은 특이성을 가지도록 조작된다.
본원에서 사용되는 바와 같이 "조작된" 또는 "변이체"는 본원에 언급된 임의의 폴리펩타이드 또는 핵산을 참조하여 사용되는 경우, 이는 모 서열과 비교해 아미노산 위치 또는 핵산 위치에 하나 이상의 변이 또는 변형을 가진 서열을 지칭한다. 모 서열은, 예를 들어, 비-변형된, 야생형 서열, 이의 상동체 또는 예를 들어 야생형 서열 또는 이의 상동체에 대해 변형된 변이체일 수 있다.
일부 구현예에서, 조작된 트랜스아미나제는 서열번호 1, 서열번호 13 또는 서열번호 31의 아미노산의 하나 이상의 변이를 가진다. 일부 구현예에서 조작된 트랜스아미나제는 서열번호 1 서열번호 13 또는 서열번호 31에 대하여, 적어도 1개, 적어도 2개, 적어도 3개, 적어도 4개, 적어도 5개, 적어도 6개, 적어도 7개 또는 적어도 8개의 아미노산 변이를 가진 아미노산 서열 변이를 가진다.
일부 구현예에서, 조작된 TA는 잔기 V114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265 및 L386, G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416, A421에 대응되는 하나 이상의 위치, 또는 이들의 하나 이상의 조합 및 서열번호 1의 아미노산 잔기 위치들로부터 선택되는 위치에서 하나 이상의 아미노산 변이를 가진다.
일부 구현예에서, 조작된 단백질의 하나 이상의 아미노산 변이는 잔기 V114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265 및 L386, G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416 및 A421에 대응되는 하나 이상의 위치, 또는 이들의 하나 이상의 조합 및 서열번호 1의 아미노산 잔기 위치들에 보존적인 또는 비-보존적인 아미노산 치환을 가진다.
일부 구현예에서, 조작된 TA는 표 7에 나타낸 잔기들에 대응되는 위치에서의 변이로서, 조작된 단백질의 하나 이상의 아미노산 변이를 가진다.
일부 구현예에서, 조작된 TA 효소는 적어도 아디페이트 세미알데하이드 기질에 대한 촉매 효율이 서열번호 1, 13 또는 31을 가진 대응되는 야생형 효소와 비교해 적어도 1.5X, 적어도 2 X, 적어도 5X, 적어도 10X, 적어도 25X 또는 1.5-25X이다.
일부 구현예에서, 공지된 표준 조건에서 조작된 트랜스아미나제 효소에 의한 아디페이트 세미알데하이드의 효소적 변환은 서열번호 1, 13 또는 31을 가진 대응되는 야생형 효소의 효소 활성에 비해 적어도 10%, 적어도 20%, 적어도 30%, 적어도 40%, 적어도 50%, 적어도 60%, 적어도 70%, 적어도 80% 또는 적어도 90% 높다.
일부 구현예에서, TA 변이체를 제공하기 위해 본 발명의 서열번호 1로 표시되는 아크로모박터 크실로스옥시단스 TA를 주형 또는 모 서열로 선택한다. 변이체는, 본원에 기술된 바와 같이, 하나 이상의 아미노산 변이 (예, 치환)를 주형에 도입함으로써 생성할 수 있다. 변이체는 활성 증가 및/또는 이의 기질 특이성 증가를 나타낸 것을 동정하기 위해 스크리닝할 수 있다. 예를 들어, TA 변이체는 아디페이트 세미알데하이드 또는 이의 유사체에 대해 활성 및/또는 특이성을 증가시키는 변이를 동정하기 위해 스크리닝한다. 본원에 기술된 다른 변이체도 마찬가지로 스크리닝하여, 모 효소의 기질 또는 기질들에 대한 활성 및/또는 특이성 증가를 동정한다.
아미노산 위치의 번호를 지정하기 위해, 일부 구현예에서, 서열번호 1을 기준 서열로 이용한다. 즉, 예를 들어, 서열번호 1을 참조하여 아미노산 위치 79번을 언급하지만, 다른 TA 서열 (표적 서열 또는 기타 주형 서열) 맥락에서, 변이체 생성시 대응되는 아미노산 위치는 위치 번호가 동일하거나 또는 상이할 수 있다 (예, 78, 79 또는 80). 일부 경우에, 서열번호 1에서 오리지널 아미노산 및 그 위치는 표적 TA 서열에서의 오리지널 서열 및 위치와 엄밀한 상관관계가 존재할 것이다. 다른 경우에, 서열번호 1 기준 주형에서 오리지널 아미노산 및 그 위치는 오리지널 아미노산과 상관관계가 존재할 것이나, 표적에서의 그 위치는 대응되는 주형 위치에 존재하지 않을 것이다. 그러나, 표적 상의 대응되는 아미노산은 기준 주형 위치로부터 아미노산 10, 9, 8, 7, 6, 5, 4, 3, 2 또는 1개 이내와 같이, 주형 상의 위치로부터 미리 결정된 거리일 수 있다. 다른 경우에, 서열번호 1 기준 주형 상의 오리지널 아미노산은 표적 상의 오리지널 아미노산과 엄밀한 상관관계가 존재하지 않을 것이다. 그러나, 표적 서열 상의 대응되는 어떤 아미노산이 표적 아미노산 근처에서의 아미노산 서열 및 주형 상의 아미노산의 일반적인 위치에 기반하는지를 파악할 수 있다. 본원에 구체적으로 기술되지 않은 TA 서열과의 서열 정렬을 생성할 수 있으며, 이러한 정렬을 이용해 본원의 교시 내용 및 지침을 감안하여 새로운 TA 변이체를 파악하고 구축할 수 있는 것으로 이해된다. 일부 구현예에서, 서열 정렬은 표적 아미노산 주위의 일반적인 또는 유사한 아미노산을 파악할 수 있게 하며, 이들 아미노산은 주형과 표적 서열 간에 특정한 동일성 또는 유사성 수준을 가진 "서열 모티프"로서 검토할 수 있다. 이들 서열 모티프를 이용해, 변이체 아미노산이 위치한 TA 서열의 영역 및 모티프에 존재할 수 있는 변이체(들) 타입을 파악할 수 있다.
또한, 카르복시산을 이의 대응되는 알데하이드로 ATP 및 NADPH 의존적으로 환원하는 반응을 촉매하는 카르복시산 리덕타제 (CAR)가 언급된 바 있다 (Venkitasubramanian et al., J. Biol . Chem . 282:478-485 (2007)). 본원에 언급되는 CAR은 중간산물 6ACA를 6-아미노카프로에이트 세미알데하이드로 변환하는데 이용할 수 있으며, 이의 E.C. 번호는 E.C. 1.2.1.30이다. 본원에 기술된 헥사메틸렌다이아민 (HMD) 및 헥산다이올 (HDO) 경로에서, 6ACA와 6-아미노카프로에이트 세미알데하이드는 중간산물이며, 6ACA에서 6-아미노카프로에이트 세미알데하이드로의 변환은 효소학적 단계이다. 즉, CAR은 예를 들어 본원에 언급된 HMD 및 HDO 경로 등의 나일론 중간산물을 합성하는 다양한 경로들에 이용할 수 있다.
요망한 CAR은 6-아미노카프로에이트 세미알데하이드 합성 경로에서 원하는 반응을 수행할 수 있는 효소에 대한 메타게놈 발굴뿐 아니라 상동성 연구에 의해 동정되었다. CAR을 6ACA 이용성에 대해 평가하기 위해, 일부 구현예에서, 분석은 6ACA 또는 본원에 예시된 바와 같은 다른 후보 기질을 이용해 정방향으로 수행될 수 있다. 마찬가지로, 분석은 또한 6-아미노카프로에이트 세미알데하이드 또는 다른 후보 기질을 이용해 역방향으로도 수행될 수 있다. 분석은 당해 기술 분야에 잘 알려진 방법을 이용해 효소학적 생산물에 대한 직접 또는 간접적인 측정에 의해 수행될 수 있다. 방법의 일 예는 실시예와 아래에 예시된 간접적인 방법이다.
일부 구현예에서, 마이콜리시박테리움 스메그마티스 (Mycolicibacterium smegmatis) MC2 155로부터 유래한 서열번호 150에 의해 암호화된 CAR 효소가 동정되었다. 일부 구현예에서, 서열번호 153에 의해 암호화된 마이코박테리움 아비움 유래 CAR 효소가 동정되었다. 다른 CAR 효소를 동정하기 위해, 서열번호 150 및 서열번호 153을 이용하였다. 상동성 효소들이 표 8에 기재된 바와 같이 동정되었다. 일부 구현예에서, CAR 효소 또는 서열을 BLAST에 의해 동정한다. 일부 구현예에서, CAR은 표 8의 CAR 아미노산 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, 표 8에서 동정된 CAR은 서열번호 152, 153 또는 254의 CAR 아미노산 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, CAR 효소는 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264 중 임의 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50%의 아미노산 서열 동일성을 가진다. 일부 구현예에서, 6ACA와 반응하여 6-아미노카프로에이트 세미알데하이드를 합성하는 CAR 효소의 아미노산 서열은 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264의 아미노산 서열들로부터 선택된다.
일부 구현예에서, 기질로서 6ACA에 대한 CAR 효소의 촉매 효율, 및/또는 대사회전수는 기질이 숙시네이트일 경우와 비슷하다. 일부 구현예에서, 기질로서 6ACA에 대한 CAR 효소의 촉매 효율 및/또는 대사회전수는 기질이 헥사노에이트일 경우와 비슷하다. 다른 구현예들에서, 기질로서 6ACA에 대한 촉매 효율 및/또는 대사회전수가 기질이 숙시네이트일 경우와 비슷한 CAR 효소는, 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264의 CAR 아미노산 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다. 또 다른 구현예에서, 기질로서 6ACA에 대한 촉매 효율 및/또는 대사회전수가 기질이 헥사노에이트일 경우 비슷한 CAR 효소는, 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264의 CAR 아미노산 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
동정한 CAR 효소들은 유전학적으로 매우 다양한 유기체들로부터 유래한 것이다. 이하 일부 예시적인 CAR들에 대한 쌍별 서열 정렬을 표 2에 나타낸다.
표 2. 예시적인 CAR들에 대한 쌍별 서열 정렬에서의 동일성 %
서열번호 152 서열번호 153 서열번호 159 서열번호 254
서열번호 152 99% 34% 74%
서열번호 153 99% 34% 75%
서열번호 159 34% 34% 36%
서열번호 254 74% 75% 36%
CAR 효소는 보존된 도메인을 가지고 있다. 다중 서열 정렬 및 HMM (hidden Markov models)에 기반하여, CAR 효소들은 유럽 생물정보학 위원회의 Pfam 데이터베이스 (pfam.xfam.org)의 하기 도메인들을 포함할 수 있다: AMP-결합 도메인 (Pfam PF00501), NAD-결합 도메인 (Pfam PF07993) 및 포스포판테테인 (PP)-결합 도메인 (Pfam PF00550).
일부 구현예에서, 단백질의 결정 구조 연구를 통해 서열번호 152에서 아미노산의 돌연변이 위치를 동정하였으며, 서열번호 152를 코딩하는 유전자 또는 이의 상동체를 선택된 아미노산 위치에서 포화 돌연변이 유발을 수행하였다. 야생형 (비-변형된) 서열번호 152 또는 이의 상동체보다 활성이 우수한 변이체 아미노산을 제공할 기회를 얻기 위해 촉매학적으로 관련있는 잔기들을 동정하였다. 일부 구현예에서, 서열번호 153에서 아미노산의 돌연변이 위치들을 동정하였으며, 서열번호 153을 암호화하는 유전자 또는 이의 상동체를 단백질 조작용 주형으로서 사용하였다 (예를 들어, 선택 아미노산 위치에서 돌연변이 유발). 일부 구현예에서, 서열번호 254에서 아미노산의 돌연변이 위치를 동정하였으며, 서열번호 254를 암호화하는 유전자 또는 이의 상동체는 단백질 조작용 주형으로서 사용하였다 (예를 들어, 선택 아미노산 위치들에서 돌연변이 유발).
일부 구현예에서, CAR 효소는 이의 대응되는 야생형에 비해 6ACA 기질 특이성이 더 높도록 조작된다.
일부 구현예에서, 조작된 CAR은 서열번호 152, 서열번호 153 또는 서열번호 254의 아미노산의 하나 이상의 변이를 가진다. 일부 구현예에서 조작된 CAR은 서열번호 152, 서열번호 153 또는 서열번호 254에 대해, 적어도 1개, 적어도 2개, 적어도 3개, 적어도 4개, 적어도 5개, 적어도 6개, 적어도 7개 또는 적어도 8개의 아미노산 변이를 가진 아미노산 서열에 변이를 가진다. 일부 구현예에서, 조작된 CAR은 잔기 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929에 대응하는 하나 이상의 위치, 또는 이들의 조합 및 서열번호 152, 153 또는 254의 아미노산 잔기 위치들로부터 선택되는 위치에 하나 이상의 아미노산 변이를 가진다.
일부 구현예에서, 조작된 CAR은 하기로 이루어진 군으로부터 선택되는 하나 이상의 잔기 위치에 하나 이상의 아미노산 변이를 포함한다: N335E; N335D; S274D; S274E; K275D; K275E; S299D; S299E; M389D; M389E; G414D; G414E; G421D; G421E; M422D; M422E; F425D; F425E; N335D 및 A282P; N335D 및 A282V; N335D 및 A283C; N335D, A283C 및 F929L; N335D, A283C 및 G636D; N335D 및 A283G; N335D 및 F278A; N335D 및 F278C; N335D 및 F278S; N335D 및 F278V; N335D 및 G279V; N335D 및 I247M; N335D 및 I247Q; N335D 및 I247T; N335D 및 I247V; N335D 및 I300C; N335D 및 I300G; N335D 및 I300M; N335D 및 I300M; N335D 및 I300Y; N335D 및 K275A; N335D 및 K275D; N335D 및 K275D; N335D 및 K275E; N335D 및 K275M; N335D 및 K275N; N335D 및 K275S; N335D 및 K275T; N335D 및 K275V; N335D 및 K275W; N335D 및 L245C; N335D 및 L245G; N335D 및 L245S; N335D 및 L245T; N335D 및 L245V; N335D 및 M389I; N335D 및 M389W; N335D 및 M422D; N335D 및 N276S; N335D 및 N279 INSERT; N335D 및 P141G; N335D 및 S299D; N335D 및 S299E; N335D 및 S391G; N335D 및 W270M; K275D, N276S, F278S, A283C 및 N335D; L245V, K275D, N276S, F278S, A283C 및 N335D; I247M, K275D, N276S, F278A, A283C 및 N335D; L245V, K275T, N276S, F278S, A283C 및 N335D; I247M, K275T, N276S, F278S, A283C 및 N335D; K275D, N276S, F278S, A283C, I300G 및 N335D; L245T, K275D, N276S, F278A, A283C 및 N335D; K275N, F278S, A283C, S299D 및 N335D; I247M, K275N, N276S, F278S, A283C 및 N335D; K275N, F278S, A283C, I300G 및 N335D; K275N, N276S, F278S, A283C, I300G 및 N335D; I247M, K275T, F278S, A283C 및 N335D; L245V, K275D, N276S, F278A, A283C 및 N335D; K275N, F278S, A283C, I300G 및 N335D; K275N, F278A, A283C, S299D 및 N335D; K275N, N276S, F278A, A283C 및 N335D; L245V, K275N, N276S, F278S, A283C, I300G 및 N335D; L245T, K275N, N276S, F278S, A283C, I300G 및 N335D; K275N, F278A, S299D 및 N335D; I247M, K275N, F278A, A283C, I300Y 및 N335D; I247M, K275N, F278A, A283C 및 N335D; K275D, N276S, F278A 및 N335D; K275T, F278A, A283C, S299D 및 N335D; F278A, A282P 및 N335D; F278A, A283C 및 N335D; K275N, S299D 및 N335D; L245T, S299D 및 N335D; K275D, S299D 및 N335D; K275N, F278S 및 N335D; S299D, M389W 및 N335D; G279V, S299D 및 N335D; F278A, S283C 및 N335D; K275D, N276S 및 N335D; G279V, S299E 및 N335D; I247M, S299D 및 N335D; P141G, A282P 및 N335D; L245T, A282P 및 N335D; F278S, A283C 및 N335D; K275D, S284I, S299D 및 N335D; I247M, I282P 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D; K275D, S274A, N276S, F278S, A283C, I300G 및 N335D; K275D, S274P, N276S, F278S, A283C, I300G 및 N335D; K275D, N276S, F278S, A282F, A283C, I300G 및 N335D; K275D, N276S, F278S, A282P, A283C, I300G 및 N335D; K275D, N276S, F278S, A283C, S299I, I300G 및 N335D; K275D, N276S, F278S, A283C, I300G, N335D 및 M389C; K275D, N276S, F278S, A283C, I300G, N335D 및 M389Y; 및 K275D, N276S, F278S, A283C, I300G, N335D 및 M389S.
일부 구현예에서, 조작된 단백질의 하나 이상의 아미노산 변이는 잔기 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929에 대응하는 하나 이상의 위치, 또는 이들의 하나 이상의 조합 및 서열번호 152, 153 또는 254의 아미노산 잔기 위치들에서의 보존적인 또는 비-보존적인 아미노산 치환이다.
일부 구현예에서, 조작된 단백질의 하나 이상의 아미노산 변이는 표 9에 나타낸 잔기들에 대응되는 위치에 변이를 가진다.
일부 구현예에서, 조작된 CAR 효소는 적어도 6ACA 기질에 대한 촉매 효율이 서열번호 152, 153 또는 254를 가진 대응되는 야생형 또는 모 효소와 대해 적어도 1.5X, 적어도 2X, 적어도 5X, 적어도 10X, 적어도 25X 또는 1.5-25X이다.
일부 구현예에서, 공지된 표준 조건에서 조작된 CAR 효소에 의한 6ACA의 효소적 변환은, 서열번호 152, 153 또는 254를 가진 대응되는 야생형 또는 모 효소에 비해, 효소 활성이 적어도 10%, 적어도 20%, 적어도 30%, 적어도 40%, 적어도 50%, 적어도 60%, 적어도 70%, 적어도 80% 또는 적어도 90% 우수하다.
일부 구현예에서, CAR 변이체를 제공하기 위해, 마이코박테리움 아비움 또는 이의 상동체 CAR은 본원의 서열번호 152 및 153으로 표시되며, 주형 또는 모 서열로서 선택된다. 일부 구현예에서, CAR 변이체를 제공하기 위해, 마이코박테리움 sp . JS623 또는 이의 상동체 CAR은 본원의 서열번호 254에 의해 표시되며, 주형 또는 모 서열로서 선택된다. 본원에 언급된 CAR 변이체를 스크리닝하여, 6ACA 또는 본원에 예시된 바와 같이 다른 후보 기질에 대해 활성 및/또는 특이성을 높이는 변이를 동정할 수 있다.
본원에 언급된 CAR들에 대해 아미노산 위치 번호를 지정하기 위해, 일부 구현예에서, 서열번호 152를 기준 서열로 이용한다. 즉, 예를 들어, 서열번호 152에 대해서는 아미노산 위치 89번을 언급하지만, 다른 CAR 서열 (표적 서열 또는 기타 주형 서열) 맥락에서, 변이체 생성에서 대응되는 아미노산 위치는 위치 번호가 동일하거나 또는 상이할 수 있다 (예, 88, 89 또는 90). 일부 경우에, 서열번호 152에서 오리지널 아미노산과 그 위치는 표적 CAR 서열에서의 오리지널 서열 및 위치와 정확한 상관관계가 존재할 것이다. 다른 경우에, 서열번호 152 기준 주형에서 오리지널 아미노산 및 그 위치는 오리지널 아미노산과 상관관계가 존재할 것이나, 표적에서의 그 위치는 대응되는 주형 위치에 존재하진 않을 것이다. 그러나, 표적 상의 대응되는 아미노산은 기준 주형 위치로부터 아미노산 10, 9, 8, 7, 6, 5, 4, 3, 2 또는 1개 이내와 같이, 주형 상의 위치로부터 미리 결정된 거리일 수 있다. 다른 경우에, 서열번호 152 기준 주형 상의 오리지널 아미노산은 표적 상의 오리지널 아미노산과 정확한 상관관계가 존재하지 않을 것이다. 그러나, 표적 서열 상의 대응되는 어떤 아미노산이 표적 아미노산 근처 아미노산 서열 및 주형 상의 아미노산의 일반적인 위치에 기반하는 지를 파악할 수 있다. 본원에 구체적으로 기술되지 않은 CAR 서열과 서열 정렬할 수 있으며, 이러한 정렬을 이용해 본원의 교시 내용 및 지침을 감안하여 새로운 CAR 변이체를 파악하고 구축할 수 있는 것으로 이해된다. 일부 구현예에서, 서열 정렬은 표적 아미노산 근처 일반적인 또는 유사한 아미노산을 이해할 수 있게 하며, 이들 아미노산은 주형과 표적 서열 간에 특정한 동일성 또는 유사성 수준을 가진 "서열 모티프"로서 검토할 수 있다. 이들 서열 모티프를 이용해, 변이체 아미노산이 위치한 CAR 서열의 영역 및 모티프에 존재할 수 있는 변이체(들) 타입을 파악할 수 있다.
일부 구현예에서, 조작된 CAR은 조작된 단백질의 하나 이상의 아미노산 변이를 가지며, 하나 이상의 변이는 표 10에 나타낸 잔기에 대응되는 위치에서의 변이이다. 일부 구현예에서, 조작된 CAR은 표 10에 나타낸 바와 같이 서열번호 153에 대해 아미노산 변이를 적어도 1개, 적어도 2개, 적어도 3개, 적어도 4개, 적어도 5개, 적어도 6개, 적어도 7개 또는 적어도 8개 가진 아미노산 서열 변이이다. 일부 구현예에서, 조작된 CAR은 아미노산 변이 N335D와 더불어 표 10에 나타낸 하나 이상의 아미노산 변이를 가진다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 L245, I247, S274, K275, N276, F278, A282, A283, S299, I300 및 M389 잔기에 대응되는 하나 이상의 위치로부터 선택되는 하나 이상의 아미노산 변이를 가진다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 245번 위치에서 L, T 또는 V을 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 247번 위치에 I, M 또는 T를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 274번 위치에 S, C, A 또는 P를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 275번 위치에 K, D, N 또는 T를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 276번 위치에 N 또는 S를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 278번 위치에 F, S 또는 A를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 282번 위치에서 A, F 또는 P를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 283번 위치에 A 또는 C를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 299번 위치에 S 또는 D를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 300번 위치에 I, G 또는 Y를 포함할 수 있다. 일부 구현예에서, 조작된 CAR은 서열번호 153의 389번 위치에 M, C, Y 또는 S를 포함할 수 있다. 돌연변이는 단독으로 발생할 수 있으며, 표 10에 나타낸 다른 아미노산 위치에서의 돌연변이와 조합하여 발생할 수 있다.
아울러, 본 발명은 전술한 TA 트랜스아미나제와는 다른 트랜스아미나제 (E.C.2.6.1)를 기술한다. 이러한 트랜스아미나제는 본원에서 TA2 트랜스아미나제, 트랜스아미나제 TA2 또는 TA2로 지칭되며, 이를 이용해 6-아미노카프로에이트 세미알데하이드를 HMD로 변환할 수 있다. 본원에 언급된 HMD 경로에서 6-아미노카프로에이트 세미알데하이드는 중간산물이며, 6-아미노카프로에이트에서 HMD로의 변환은 효소학적 단계이다. 즉, TA2는 예를 들어 본원에 기술된 HMD 경로를 비롯해 나일론 중간산물로 이어지는 다양한 경로들에 이용할 수 있다.
요망한 TA2 트랜스아미나제는 헥사메틸렌다이아민 (HMD) 합성 경로에서 원하는 반응을 수행할 수 있는 효소에 대한 메타게놈 발굴뿐 아니라 상동성 연구에 의해 동정되었다. TA2를 6-아미노카프로에이트 세미알데하이드 이용성에 대해 평가하기 위해, 일부 구현예에서, 분석은 6-아미노카프로에이트 세미알데하이드 또는 본원에 예시된 바와 같은 다른 후보 기질을 이용하여 정방향으로 수행할 수 있다. 마찬가지로, 분석은 또한 HMD 또는 다른 후보 기질을 이용하여 역방향으로도 수행할 수 있다. 분석은 또한 TA 트랜스아미나제 이용시와 같이 6ACA를 이용해 수행할 수도 있다. 이들 6ACA에 대해 활성인 TA2 트랜스아미나제는 6-아미노카프로에이트 세미알데하이드 -> HMD 변환 활성에 대해 스크리닝할 수 있다. 이러한 분석은 당해 기술 분야에 잘 알려진 방법을 이용하여 효소적 생산물에 대한 직접 또는 간접 측정으로 수행할 수 있다. 방법의 일 예는 실시예와 아래에 예시된 간접적인 방법이다.
일부 구현예에서, 에스케리키아 콜라이로부터 유래한 서열번호 265에 의해 암호화된 TA2 효소가 동정되었다. 다른 TA2 효소를 동정하기 위해, 서열번호 265를 이용하였다. 상동성 효소들이 표 11에 기술된 바와 같이 동정되었다. 일부 구현예에서, BLAST에 의해 TA2 효소 또는 서열을 동정하였다. 일부 구현예에서, TA2는 표 11의 TA2 아미노산 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, 표 11에서 동정된 TA2는 서열번호 265의 TA2 아미노산 서열들의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
일부 구현예에서, TA2 효소는 서열번호 265 및 267-296 중 임의 서열의 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50%의 아미노산 서열 동일성을 가진다. 일부 구현예에서, 6-아미노카프로에이트 세미알데하이드와 반응하여 HMD를 합성하는 TA2 효소의 아미노산 서열은 서열번호 265 및 267-296의 아미노산 서열들로부터 선택된다.
일부 구현예에서, TA2 효소는 기질로서 6-아미노카프로에이트 세미알데하이드에 대한 촉매 효율 및/또는 대사회전수가 6ACA를 기질로 사용할 경우와 비슷하다. 일부 구현예에서, 6-아미노카프로에이트 세미알데하이드에 대한 대사회전수 및/또는 촉매 효율이 6ACA가 기질일 경우와 비슷한 효소는, 서열번호 265 및 267-296의 임의의 TA2 아미노산 서열들의 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상의 연속 아미노산에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
동정한 TA2 효소들은 유전학적으로 매우 다양한 유기체들로부터 유래한다. 일부 예시적인 TA2에 대한 쌍별 서열 정렬을 아래 표 3에 나타낸다.
표 3. 예시적인 TA2들에 대한 쌍별 서열 정렬에서의 동일성 %
서열번호 265 서열번호 270 서열번호 289 서열번호 296
서열번호 265 45% 61% 95%
서열번호 270 45% 47% 47%
서열번호 289 61% 47% 61%
서열번호 296 95% 47% 61%
TA2 효소는 보존된 도메인을 가지고 있다. 다중 서열 정렬 및 HMM (hidden Markov models)에 기반하여, TA2 효소들은 유럽 생물정보학 위원회의 Pfam 데이터베이스 (pfam.xfam.org)에서 Pfam PF00202로 분류된다. TA2 효소는 피리독살 포스페이트 (PLP) 결합을 위한 활성 부위에 존재하는 보존된 라이신을 가지고 있다. PLP의 알데하이드 기와 라이신 잔기는 쉬프-염기 구조 (Schiff-base structure)를 형성해, 활성 입체구조를 구축할 수 있다.
일 측면에서, 하기를 코딩하는 외인성 핵산을 포함하는 비-천연성 미생물 유기체를 제공하며: (a) 서열번호 152, 153 또는 254의 아미노산의 하나 이상의 변이를 포함하는 조작된 카르복시산 리덕타제 (CAR) 효소; (b) 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264 중 임의의 서열에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 이상에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는 CAR; 또는 (c) 서열번호 265 및 267-296 중 임의의 서열에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 이상에 대해 적어도 50%의 서열 동일성을 가진 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소; 추가적으로 (d) 아디필-CoA와 반응하여 아디페이트-세미알데하이드를 합성하는 알데하이드 데하이드로게나제 (ALD) 효소를 코딩하는 하나 이상의 외인성 핵산을 더 포함하고, 여기서 알데하이드 데하이드로게나제는 기질로서 숙시닐-CoA, 아세틸-CoA, 또는 숙시닐-CoA와 아세틸-CoA 둘다와 비교해 아디필-CoA 기질에 대해 더 높은 촉매 효율을 가지거나, 및/또는 기질로서 숙시닐-CoA, 아세틸-CoA, 또는 숙시닐-CoA와 아세틸-CoA 둘다와 비교해 아디필-CoA 기질에 대해 더 높은 대사회전수를 가진다.
일부 구현예에서, ALD 효소를 코딩하는 외인성 핵산 한종은 비-천연성 미생물 유기체의 게놈에 통합된다. 일부 구현예에서, ALD 효소를 코딩하는 외인성 핵산은 미생물 유기체의 게놈에 통합되지 않으며, 예를 들어, 플라스미드이다. 일부 구현예에서, ALD 효소를 코딩하는 외인성 핵산은 미생물 유기체에 대해 이종적이다.
일부 구현예에서, 3-옥소아디필-CoA 티올라제 (Thl), 3-옥소아디필-CoA 데하이드로게나제 (Hbd) 및 3-옥소아디필-CoA 데하이드라타제 ("크로토나제" 또는 Crt), 5-카르복시-2-펜테노일-CoA 리덕타제 (Ter), 및 트랜스아미나제 (TA), 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 및 카르복시산 리덕타제 (CAR)를 코딩하는 유전자를 포함하는, 비-천연성 미생물 유기체에서 ALD 효소를 코딩하는 하나 이상의 외인성 핵산의 발현은, ALD 효소를 코딩하는 외인성 핵산 없이 3-옥소아디필-CoA 티올라제 (Thl), 3-옥소아디필-CoA 데하이드로게나제 (Hbd), 및 3-옥소아디필-CoA 데하이드라타제 ("크로토나제" 또는 Crt), 5-카르복시-2-펜테노일-CoA 리덕타제 (Ter), 및 트랜스아미나제 (TA), 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 및 카르복시산 리덕타제 (CAR)를 코딩하는 유전자를 포함하는 대조군 미생물과 비교해, HMD 생산을 증가시킨다.
기질로서 숙시닐-CoA, 아세틸 CoA 또는 이 둘다에 비해 아디필 CoA에 대해 촉매 효율이 더 높거나, 대사회전수가 더 높거나 또는 이 둘다인 ALD 효소를 동정하기 위해, 유전자 adh (서열번호 141)에 의해 암호화된 클로스트리듐 클루이베리 DSM555의 서열 예를 이용해, 다른 알데하이드 데하이드로게나제 효소들을 동정하였다. 상동성 효소들이 표 4에 나타낸 바와 같이 동정되었다.
일부 구현예에서, 알데하이드 데하이드로게나제 효소 또는 서열은 BLAST에 의해 동정한다. 일부 구현예에서, 알데하이드 데하이드로게나제는 표 4의 ALD 아미노산 서열의 연속 아미노산 적어도 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% 또는 100%의 서열 동일성을 공유한다.
이들 ALD 효소는 유전학적으로 매우 다양한 유기체들로부터 유래한다. 종종 서열들 간의 간단한 아미노산 서열 동일성이 이의 공통적인 기능을 나타내는 것은 아니다. 예를 들어, 표 4에 개시된 예시적인 일부 알데하이드 데하이드로게나제들에 대한 쌍별 서열 정렬을 아래 표 12에 나타낸다.
표 12. 예시적인 ALD들에 대한 쌍별 서열 정렬에서의 동일성 %
서열번호 298 서열번호 306 서열번호 323 서열번호 347
서열번호 298
기원 유기체: 펩토스트렙토코카시이 박테리움 오랄 		50% 56% 60%
서열번호 306
기원 유기체: 액시드아미노코커스 마실리엔시스		 50% 53% 57%
서열번호 323
기원 유기체: 콜린셀라 sp. GD7		 56% 53% 60%
서열번호 347
기원 유기체: 롬바우치아 리투세부렌시스 DSM		 60% 67% 60%
이들 ALD 효모는 복수의 보존된 도메인, 예를 들어, N-말단 도메인, C-말단 도메인 및 이의 활성 부위에 시스테인 잔기를 가진다. ALD는 로스만-폴드 타입 (Rossmann-fold type)의 뉴클레오티드 결합 구조를 가진 보조인자 결합 도메인을 포함한다. 로스만 폴드는 βαβ 폴드로서 지칭되며, 이는 베타 가닥-알파 나선-베타 가닥 의2차 구조로 된 얼터네이팅 모티프를 특징으로 하는 슈퍼-2차 구조이다. β-가닥은 β-시트 형성에 참여한다. βαβ 폴드 구조는 FAD, NAD 및 NADP와 같은 다이뉴클레오티드 코엔자임을 가진 효소에서 통상적으로 관찰된다. βαβ 폴드 구조는 첫번째 β-가닥과 α-나선 사이의 타이트한 루프 영역에 특이적인 Gly-풍부 서열 (GxGxxG)과 관련있다. 아울러, 보조인자 결합 도메인은 또한 기질 CoA에 결합하는 동일한 도메인을 가진다. 이는 ALD의 전형적인 특징이며, 먼저 기질 CoA가 결합해 중간산물이 형성된 다음 보조인자가 결합하여 화학 반응이 종료되며 수소화물 전달이 이루어진다.
복수의 서열 정렬 및 HMM (hidden Markov model)을 기반으로 ALD 효소는 유럽 생물정보학 위원회의 Pfam 데이터베이스 (pfam.xfam.org)에서 Pfam PF00171, Clan CL0099로 분류된다. 이들 효소는 효소 위원회 명명법에 따라 EC 1.2.1로 분류된다.
본원에 기술된 임의 효소에 대해, 일부 경우에, 주형 서열과 표적 서열에서 아미노산 모티프 간의 서열 동일성을 파악하기 위해 BLAST (Basic Local Alignment Search Tool) 알고리즘을 이용하는 것이 유용할 수 있다. 따라서, 바람직한 실행 방식에서, BLAST를 이용해 주형과 표적 단백질 간의 더 짧은 아미노산 가닥 (예, 서열 모티프)의 동일성을 동정 또는 파악한다. BLAST는 서열 2종 간에 짧게 일치되는 위치를 파악함으로써 스미스-워터만 알고리즘 (Smith-Waterman algorithm)을 계산하는 발견적 방법을 이용하여 유사한 서열을 탐색한다. (BLAST) 알고리즘은 특정 역치보다 높은 쿼리 서열과 유사한 라이브러리 서열을 동정할 수 있다. BLAST 알고리즘을 이용해 2 이상의 서열의 연관성을 결정하기 위한 예시적인 매개변수는, 예를 들어, 아래에 기술된 바와 같을 수 있다. 간략하게는, 아미노산 서열 정렬은 BLASTP 버전 2. 0. 8 (Jan-05-1999) 및 다음과 같은 매개변수를 이용해 수행할 수 있다: 행렬: 0 BLOSUM62; 갭 오픈: 11; 갭 연장: 1; x_드롭오프: 50; 기대: 10.0; 문자 크기: 3; 필터: on. 핵산 서열 정렬은 BLASTN 버전 2. 0. 6 (Sept-16-1998) 및 다음과 같은 매개변수를 이용해 수행할 수 있다: 매치: 1; 미스매치: -2; 갭 오픈: 5; 갭 연장: 2; x_드롭오프: 50; 기대: 10.0; 문자 크기: 11; 필터: off. 당해 기술 분야의 당업자라면, 예를 들어 비교 엄격성을 높이거나 또는 낮추고, 2 이상의 서열의 연관성을 결정하기 위해 상기한 매개변수에 어떤 수정을 가할 수 있는지 알 것이다.
부위-지향성 돌연변이 유발 또는 서열 변이 (예, 부위-특이적인 돌연변이 유발 또는 올리고뉴클레오티드-지향성)를 이용해 표적 TA DNA 서열에 특이적인 변화를 행함으로써 원하는 아미노산 치환을 가진 TA 코딩 DNA 서열 변이체를 제공할 수 있다. 대체로, 변이체 아미노산을 코딩하는 코돈을 제공하는 서열을 가진 올리뉴클레오티드를 이용한다. 일부 구현예에서, 치환에 대해 표적화된 바람직한 TA는 일반적으로 아미노산 150개 미만 길이이므로, 변이체 TA DNA 서열의 전체 코딩 영역은 인공 유전자로 합성하는 것이 바람직하다.
변이체 TA 또는 CAR 서열을 구축하는데 돌연변이 유발 올리뉴클레오티드를 이용하는 예시적인 기법으로는 파지미드에 배치된 TA 또는 CAR 유전자 서열을 활용할 수 있는 Kunkel 방법을 포함한다. E. coli TA ssDNA 형태의 파지미드는 주형에서 연장되는 프라이머인 올리뉴클레오티드를 이용한 돌연변이 유발용 주형이다.
TA 또는 CAR DNA 내 대상 위치에 인접한 제한 효소 부위에 따라, 카세트 돌연변이 유발을 이용해 대상 변이체 서열을 구축할 수 있다. 카세트 돌연변이 유발의 경우, DNA 단편을 합성해 제한 효소로 절단된 플라스미드에 삽입한 다음 TA 또는 CAR 변이체 돌연변이를 함유한 상보적인 올리뉴클레오티드 한쌍과 연결한다. 플라스미드와 올리뉴클레오티드의 제한 효소 단편을 서로 연결할 수 있다.
다른 구현예들에서, 변이체 TA 또는 CAR 서열을 구축하는데 이용되는 다른 기법은 PCR 부위-지향 돌연변이 유발이다. 돌연변이 생성 올리뉴클레오티드 프라이머를 이용해 원하는 돌연변이를 도입하여, 돌연변이된 서열을 가진 PCR 단편을 제공한다. 부가적인 올리뉴클레오티드를 이용해 제한 효소 절단 및 유전자 삽입에 적합한 제한효소 부위를 제공하도록 돌연변이된 단편의 양쪽 말단을 연장할 수 있다.
부위-지향성 돌연변이 유발 기법용 상업적인 키트 역시 이용가능하다. 예를 들어, Quikchange™ 키트는 pfu 중합효소와 같은 정확도가 높은 비-가닥-치환 DNA 중합효소를 이용해 유전자 영역을 PCR 증폭하기 위해 상보적인 돌연변이 생성 프라이머를 이용한다. 반응으로 풀린 닉 (nick) 형성된 환형 DNA가 생성된다. 주형 DNA는 메틸화된 DNA에 특이적인 DpnI과 같은 제한 효소로 효소 분해함으로써 제거한다.
일부 구현예에서, 최적화 방법은 방향성 진화 (directed evolution)이다. 방향성 진화는, 효소의 특성을 개선 및/또는 변형하기 위해, 특정 유전자에 표적화된 돌연변이를 도입하는 것을 수반하는, 강력한 apprTAh이다. 향상된 및/또는 변형된 효소는 복수의 (예, >104) 효소 변이체를 자동 스크리닝할 수 있는 민감한 고-처리 스크리닝 분석을 개발 및 구현함으로써 동정할 수 있다. 돌연변이 유발 및 스크리닝 라운드를 전형적으로 반복 실시하여, 효소에 최적화된 특성을 부여할 수 있다. 돌연변이를 유발하기 위한 유전자 영역을 동정하는데 도움이 될 수 있는 수학적 알고리즘 역시 개발되어 있으며, 제조 및 스크리닝해야 하는 효소 변이체의 개수를 현저하게 줄일 수 있다. 다양한 변이체 라이브러리 제조에 유효한 다수의 방향성 진화 기법들도 개발되어 있으며 (리뷰로서, Hibbert et al., Biomol. Eng 22:11-19 (2005); Huisman and Lalonde, In Biocatalysis in the pharmaceutical and biotechnology industries pgs. 717-742 (2007), Patel (ed.), CRC Press; Otten and Quax. Biomol. Eng 22:1-9 (2005); 및 Sen et al., Appl Biochem. Biotechnol 143:212-223 (2007) 참조), 다수의 효소 클래스들에서 매우 다양한 특성을 개선하는데 이러한 방법들이 성공적으로 적용된 바 있다. 방향성 진화 기법에 의해 개선되거나 및/또는 변형된 효소 특징으로는, 예를 들어, 비-천연 기질의 변환에 대한 선택성/특이성; 확실한 고온 처리를 위한 온도 안정성; 높거나 낮은 pH 조건에서의 생물학적 처리를 위한 pH 안정성; 기질 또는 생산물 관용성 (product tolerance), 이로써 높은 생산 역가를 달성할 수 있음; 비-천연 기질들을 망라하기 위한 광범위한 기질 결합성 등의, 결합성 (Km); 생산물, 기질 또는 주요 중간산물에 의한 저해를 없애기 위한, 저해성 (Ki); 원하는 플럭스를 달성하도록 효소 반응 속도를 높이기 위한, 활성 (kcat); 단백질 수율 및 전체 경로 플럭스를 높이기 위한, 발현 수준; 호기 조건에서 공기 민감성 효소 작용을 위한, 산소 안정성; 및 산소가 존재하지 않은 조건에서 호기성 효소의 작용을 위한, 혐기성 활성 등이 있다.
특정 효소의 바람직한 특징을 표적화하기 위해 유전자에 돌연변이 유발 및 다양화를 달성하는 여러가지 예시적인 방법들이 개발되어 있다. 이러한 방법들은 당해 기술 분야의 당업자들에게 잘 알려져 있다. 이러한 방법들 중 임의 방법을 이용해, 6ACA, 헥사메틸렌다이아민, 카프로락탐 또는 1,6-헥산다이올 경로 효소 또는 단백질의 활성을 변형 및 최적화할 수 있다. 이러한 방법으로는, 비-제한적인 예로, PCR 반응에 DNA 중합효소의 정확도 (fidelity)를 낮춤으로써 무작위 점 돌연변이를 도입하는 EpPCR (Pritchard et al., J Theor . Biol . 234:497-509 (2005)); 전체 환형 플라스미드를 주형으로 사용하고, 마지막 뉴클레오티드 2개에 엑소뉴클레아제 내성 티오포스페이트 결합을 가미한 랜덤 6 mer를 이용하여 플라스미드를 증폭한 다음, 세포로 형질전환하고, 세포내에서 플라스미드를 탠덤 리피트에서 다시 고리화하는 것을 제외하고는 epPCR과 동일한, 에러-유발 롤링 서클 증폭 (Error-prone Rolling Circle Amplification)(epRCA)(Fujii et al., Nucleic Acids Res. 32:e145 (2004); 및 Fujii et al., Nat. Protoc . 1:2493-2497 (2006)); 전형적으로 DNase I 또는 Endo V와 같은 뉴클레아제로 2개 이상의 변이체 유전자를 절단하여, DNA 중합효소의 존재 하에 어닐링 및 연장 사이클에 의해 재조립되는 랜덤 단편 풀을 제조함으로써, 키메라 유전자 라이브러리를 구축하는 과정을 수반하는, DNA 또는 패밀리 셔플링 (Family Shuffling)(Stemmer, Proc Natl Acad Sci USA 91:10747-10751 (1994); 및 Stemmer, Nature 370:389-391 (1994)); 주형을 프라이밍한 후 변성과 매우 짧은 간격 (약 5초)의 어닐링/연장으로 이루어진 2단계 PCR 사이클을 반복하는 과정을 수반하는, 스테거드 연장 (Staggered Extension, StEP)(Zhao et al., Nat. Biotechnol . 16:258-261 (1998)); 랜덤 서열 프라이머를 사용해 주형의 여러가지 세그먼트에 대해 상보적인 복수의 짧은 DNA 단편을 제조하는, 랜덤 프라이밍 재조합 (Random Priming Recombination, RPR)(Shao et al., Nucleic Acids Res 26:681-683 (1998)) 등이 있다.
추가적인 방법으로는, 선형화된 플라스미드 DNA를 사용해 미스매치 복원에 의해 복원되는 헤테로두플렉스를 형성하는 헤테로두플렉스 재조합 (Heteroduplex Recombination)(Volkov et al, Nucleic Acids Res. 27:e18 (1999); 및 Volkov et al., Methods Enzymol . 328:456-463 (2000)); DNase I 단편화와 단일 가닥 DNA (ssDNA)의 크기 분획화를 이용한 RACHITT (Random Chimeragenesis on Transient Templates)(Coco et al., Nat. Biotechnol. 19:354-359 (2001)); 주형의 풀로서 사용되는 단일-방향성 ssDNA 단편들의 존재 하에 프라이머로부터 한쪽 방향으로 성장하는 가닥들의 주형 스위칭을 수반하는 RETT (Recombined Extension on Truncated templates)(Lee et al., J. Molec . Catalysis 26:119-129 (2003)); 축중 프라이머 (degenerate primer)를 사용해 분자들 간의 재조합을 제어하는 DOGS (Degenerate Oligonucleotide Gene Shuffling)(Bergquist and Gibbs, Methods Mol . Biol 352:191-204 (2007); Bergquist et al., Biomol . Eng 22:63-72 (2005); Gibbs et al., Gene 271:13-20 (2001)); 대상 유전자 또는 유전자 단편에서 1 bp가 결손된 조합 라이브러리를 구축하는 ITCHY (Incremental Truncation for the Creation of Hybrid Enzyme)(Ostermeier et al., Proc . Natl . Acad . Sci . USA 96:3562-3567 (1999); 및 Ostermeier et al., Nat. Biotechnol . 17:1205-1209 (1999)); 포스포티오에이트 dNTA를 이용해 말단 절단체 (truncation)를 제조하는 것을 제외하고는 ITCHY와 유사한, THIO-ITCHY (Thio-Incremental Truncation for the Creation of Hybrid Enzyme)(Lutz et al., Nucleic Acids Res 29:E16 (2001)); 재조합 유전자에 대한 ITCHY와 DNA 셔플링 방법 2가지를 조합한, SCRATCHY (Lutz et al., Proc . Natl. Acad . Sci . USA 98:11248-11253 (2001)); epPCR을 통해 제조된 돌연변이를 이후 유용한 활성 보유에 대해 스크리닝/선별하는 RNDM (Random Drift Mutagenesis)(Bergquist et al., Biomol . Eng . 22:63-72 (2005)); 포스포티오에이트 뉴클레오티드의 랜덤 병합 및 절단을 이용하여 랜덤 길이의 단편들의 풀을 제조하고, 이러한 풀을 주형으로 사용하여 이노신 등의 "유니버셜" 염기들의 존재 하에 연장시키고, 이노신-함유 상보체의 복제로 랜덤 염기 병합이 이루어지고, 결과적으로 돌연변이가 유발되는, 랜덤 돌연변이 유발 방법인, SeSaM (Sequence Saturation Mutagenesis)(Wong et al., Biotechnol . J. 3:74-82 (2008); Wong et al., Nucleic Acids Res. 32:e26 (2004); 및 Wong et al., Anal. Biochem . 341:187-189 (2005)); "표적에서 모든 유전자 다양성"을 코딩하고 셔플링된 후대 (shuffled progeny)에 대해 매우 다양한 다양성을 허용할 수 있도록 설계된 중첩되는 올리고뉴클레오티드를 이용하는, 합성 셔플링 (Synthetic Shuffling)(Ness et al., Nat. Biotechnol . 20:1251-1255 (2002)); dUTP를 병합한 후 우라실 DNA 글리코실라제와 이후 피페리딘의 처리로 엔드포인트 DNA 단편화를 수행하는, 뉴클레오티드 교환 및 적출 기법 (Nucleotide Exchange and Excision Technology)인 NexT (Muller et al., Nucleic Acids Res. 33:e117 (2005)) 등이 있다.
추가적인 방법으로, 링커를 사용해 2종 간의 연관성이 멀거나 연관성이 없는 유전자들이 융합되게 촉진하고, 2종의 유전자들 간에 다양한 키메라를 제조함으로써 단일-교차 하이브리드 라이브러리를 제조하는, 서열 상동성-독립적인 단백질 재조합 (SHIPREC)(Sieber et al., Nat. Biotechnol . 19:456-460 (2001)); 출발 물질이 삽입체를 포함하는 슈퍼코일형의 이중 가닥 DNA (dsDNA) 플라스미드와 원하는 돌연변이 부위에 축중성인 2개의 프라이머를 포함하는, 유전자 부위 포화 돌연변이 유발 (Gene Site Saturation Mutagenesis, GSSM™)(Kretz et al., Methods Enzymol. 388:3-11 (2004)); 제한된 영역을 매우 많은 수의 가능한 아미노산 서열 변이로 치환하는 짧은 올리고뉴클레오티드 카세트의 사용을 수반하는, 조합 카세트 돌연변이 유발 (Combinatorial Cassette Mutagenesis, CCM)(Reidhaar-Olson et al. Methods Enzymol . 208:564-586 (1991); 및 Reidhaar-Olson et al. Science 241:53-57 (1988)); 기본적으로 CCM과 비슷하지만, 높은 돌연변이 유발율로 epPCR을 이용해 핫 스팟 및 핫 영역을 동정한 다음 CMCM에 의해 연장하여 단백질 서열 스페이스의 한정된 영역을 커버 (cover)하는, 조합형 다중 카세트 돌연변이 유발 (Combinatorial Multiple Cassette Mutagenesis, CMCM)(Reetz et al., Angew . Chem. Int . Ed Engl . 40:3589-3591 (2001)); DNA 폴리머라제 III의 돌연변이 서브유닛을 코딩하는 mutD5 유전자를 이용해, 조건부 ts 돌연변이 유발 플라스미드가 선택 과정 중에 랜덤 및 천연 돌연변이 빈도를 20 내지 4000 X로 증가시키며, 선택 과정이 필요 없을시 유해 돌연변이가 축적되는 것을 차단할 수 있는, 돌연변이 유발 균주 기법 (Mutator Strains technique)(Selifonova et al., Appl . Environ. Microbiol . 67:3645-3649 (2001)); Low et al., J. Mol . Biol . 260:359-3680 (1996)) 등이 있다.
추가적인 방법에 대한 예로는, 선택 아미노산의 조합 돌연변이 (combinatorial mutation)를 분석 및 최적화하는 다차원 돌연변이 유발 방법인, LTM (Look-Through Mutagenesis)(Rajpal et al., Proc . Natl . Acad . Sci . USA 102:8466-8471 (2005)); 한번에 복수의 유전자에 적용할 수 있거나, 또는 단일 유전자의 대규모 키메라 (복수의 돌연변이) 라이브러리를 제조할 수 있는 DNA 셔플링 방법인, 유전자 리어셈블리 (Tunable GeneReassembly™ (TGR™) Technology, Verenium Corporation); 특정 폴드를 가진 구조적으로 정의된 단백질 백본을 고정하고, 폴드와 전체 단백질 에너제틱스 (energetics)를 안정시킬 수 있는 아미노산 치환에 대한 서열 스페이스를 검색하는, 일반적으로 3차원 구조가 공지된 단백질에 대해 가장 효과적으로 작용하는 최적화 알고리즘인, PDA (in Silico Protein Design Automation)(Hayes et al., Proc . Natl . Acad . Sci . USA 99:15926-15931 (2002)); 및 구조/기능에 대한 지식을 이용해 효소 개선이 가능한 부위를 선택하는 단계, Stratagene QuikChange (Stratagene; San Diego CA)와 같은 돌연변이 유발 방법을 이용해 선택 부위에서의 포화 돌연변이 유발 (saturation mutagenesis)을 수행하는 단계, 바람직한 특징을 스크리닝/선별하는 단계, 및 개선된 클론(들)을 이용하여 다른 부위에 대해서도 다시 시작하여 바람직한 활성이 달성될 때까지 계속 반복하는 단계를 포함하는, ISM (Iterative Saturation Mutagenesis)(Reetz et al., Nat. Protoc. 2:891-903 (2007); 및 Reetz et al., Angew . Chem . Int . Ed Engl . 45:7745-7751 (2006)) 등이 있다.
돌연변이를 유발하기 위한 임의의 전술한 방법들은 단독으로 또는 임의 조합으로 이용할 수 있다. 아울러, 방향성 진화 방법들 중 임의의 한가지 방법 또는 조합을 본원에 기술된 적응 진화 기법과 함께 사용할 수 있다.
원하는 효소 활성을 가진 세포는 당해 기술 분야에서 공지된 임의 방법을 이용해 동정할 수 있다. 예를 들어, 효소 활성 분석을 이용해 효소 활성을 가진 세포를 동정할 수 있으며, 예를 들어 Enzyme Nomenclature, Academic Press, Inc., New York 2007을 참조한다. 아디페이트 세미알데하이드에서 TA 반응, 6ACA에서 CAR 반응 및/또는 6-아미노카프로에이트 세미알데하이드에서 TA2 반응을 확인하기 위해 이용할 수 있는 기타 분석으로는 GC/MS 분석을 포함한다. 다른 예로서, NADH/NADPH의 수준을 모니터링할 수 있다. 예를 들어, NADH/NADPH를 NADP/NADPH 분석 키트 (예, ABCAM™에서 입수가능한 ab65349)를 사용해 비색 측정으로 또는 분광 측정으로 모니터링할 수 있다.
개시된 TA 효소는 나일론 중간산물을 생산하기 위한 경로에 이용할 수 있다. 일부 구현예에서, 비-천연성 미생물은 아디페이트 세미알데하이드 또는 중간 산물로서 아디페이트 세미알데하이드를 이용하여 제조되는 나일론 중간산물을 생산하는데 이용할 수 있다. 본원에 기술된 TA 효소에 대한 기질로서 아디페이트 세미알데하이드를 이용한 중간산물의 일 예는 6ACA이다.
개시된 CAR 효소는 나일론 중간산물 및/또는 1,6-헥산다이올 중간산물 합성 경로에 이용할 수 있다. 일부 구현예에서, 비-천연성 미생물은 6ACA 또는 기타 나일론 중간산물, 또는 6ACA를 중간산물로서 이용해 생산되는 1,6-헥산다이올 중간산물을 생산하는데 이용할 수 있다. 본원에 기술된 CAR 효소에 대한 기질로서 6ACA를 이용한 나일론 및 1,6-헥산다이올의 중간산물의 일 예는 6-아미노카프로에이트 세미알데하이드이다. 즉, 일부 나일론 중간산물은 또한 1,6-헥산다이올 중간산물 (예를 들어, 도 8)일 수 있으며, 달리 언급되지 않은 한, 본원에서 바람직하게는 나일론 중간산물이다.
개시된 TA2 효소는 나일론 중간산물 합성 경로에 이용할 수 있다. 일부 구현예에서, 비-천연성 미생물은 6-아미노카프로에이트 세미알데하이드 또는 6-아미노카프로에이트 세미알데하이드를 중간산물로서 이용해 생산되는 기타 나일론 중간산물을 합성하는데 이용할 수 있다. 본원에 개시된 TA2 효소에 대한 기질로서 6-아미노카프로에이트 세미알데하이드를 이용하는 중간산물의 일 예는 헥사메틸렌다이아민이다.
일부 구현예에서, 유전자 변형된 세포 (예, 비-천연성 미생물)는 6-아미노카프로익산, 카프로락탐 및 헥사메틸렌다이아민과 같은 나일론 중간산물을 생산할 수 있다.
일부 구현예에서, 나일론 중간산물은 도 1에 기술된 경로를 이용해 생합성된다. 일부 구현예에서, 경로가 6-아미노카프로익산, 카프로락탐 및 헥사메틸렌다이아민을 생산하기 위해 충분한 양으로 발현되는 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하는, 본원에 기술된 유전자 변형된 세포 (예, 비-천연성 미생물)에서 도 1의 경로가 제공된다.
일부 구현예에서, 경로는 도 1에 도시된 바와 같은 HMD 경로이다. HMD 경로는, HMD 경로가 HMD를 생산하기 위해 충분한 양으로 발현되는 HMD 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하는, 본원에 기술된 유전자 변형된 세포 (예, 비-천연성 미생물)에 제공된다. 효소는 다음과 같다: 1A = 3-옥소아디필-CoA 티올라제; 1B = 3-옥소아디필-CoA 리덕타제; 1C = 3-하이드록시아디필-CoA 데하이드라타제; 1D = 아디페이트 세미알데하이드리덕타제; 1E = 3-옥소아디필-CoA/아실-CoA 트랜스퍼라제; 1F = 3-옥소아디필-CoA 신타제; 1G = 3-옥소아디필-CoA 하이드롤라제; 1H = 3-옥소아디페이트 리덕타제; 1I = 3-하이드록시아디페이트 데하이드라타제; 1J = 5-카르복시-2-펜테노에이트 리덕타제; 1K = 아디필-CoA/아실-CoA 트랜스퍼라제; 1L = 아디필-CoA 신타제; 1M = 아디필-CoA 하이드롤라제; 1N = 아디필-CoA 리덕타제 (알데하이드 생성); 1O = 6-아미노카프로에이트 트랜스아미나제; 1P = 6-아미노카프로에이트 데하이드로게나제; 1Q = 6-아미노카프로일-CoA/아실-CoA 트랜스퍼라제; 1R = 6-아미노카프로일-CoA 신타제; 1S = 아미도하이드롤라제; 1T = 자발적인 고리화; 1U = 6-아미노카프로일-CoA 리덕타제 (알데하이드 생성); 1V = HMD 트랜스아미나제; 1W = HMD 데하이드로게나제.
도 1을 참조하여, 일부 구현예에서, 비-천연성 미생물은 다음과 같은 경로 하나 이상을 가진다: ABCDNOPQRUVW; ABCDNOPQRT; 또는: ABCDNOPS. 아디페이트 세미알데하이드를 생산하기 위한 TA 효소를 포함하는 다른 예시적인 경로는 미국 특허 8,377,680에 기술된 것을 포함하며, 이 문헌은 그 전체가 원용에 의해 본 명세서에 포함된다.
또한, 도 1은 트랜스퍼라제 또는 신타제 효소에 의한 6-아미노카프로에이트 → 6-아미노카프로일-CoA (도 1, 단계 Q 또는 R) 변환 후 6-아미노카프로일-CoA의 자발적인 고리화에 의한 카프로락탐 형성 (도 1, 단계 T)으로 이루어진 경로를 도시한다. 다른 구현예들에서, 6-아미노카프로에이트는 6-아미노카프로일-CoA (도 1, 단계 Q 또는 R)로 활성화된 다음 환원 (도 1, 단계 U) 및 아민화 (도 1, 단계 V 또는 W)를 거쳐 HMD를 생성한다. 6-아미노카프로익산은 또한 6-아미노카프로일-CoA 대신 6-아미노카프로일-포스페이트로 활성화될 수 있다. 6-아미노카프로일-포스페이트는 자발적으로 고리화되어 카프로락탐을 형성할 수 있다. 일부 구현예에서, 6-아미노카프로일-포스페이트는 6-아미노카프로에이트 세미알데하이드로 환원될 수 있으며, 이후 이는 도 1에 도시된 바와 같이 HMD로 변환될 수 있다.
일부 구현예에서, 비-천연성 미생물은 도 4-10의 경로에 도시된 바와 같이 아디페이트, 6ACA, 카프로락톤, 헥사메틸렌다이아민 또는 카프로락탐을 합성할 수 있다.
일부 구현예에서, 비-천연성 미생물은 1,6-헥산다이올을 합성할 수 있다. 도 8은 6ACA, 6-아미노카프로일-CoA, 6-아미노카프로에이트 세미알데하이드, 아디페이트, 아디필-CoA 및 아디페이트 세미알데하이드와 같은 나일론 중간산물을 경유하여 이루어지는 1,6-헥산다이올 생합성 경로를 예시한다.
일부 구현예에서, 비-천연성 미생물 유기체는 알데하이드 데하이드로게나제 (ALD) 또는 트랜스에노일 리덕타제 (TER) 또는 이 둘다를 코딩하는 외인성으로 발현되는 핵산을 추가로 포함한다. ALD는 아디필-CoA와 반응하여 아디페이트 세미알데하이드를 생성하는 반면, TER은 5-카르복시-2-펜테노일-CoA (CPCoA)와 반응하여 아디필CoA를 생성한다.
일부 구현예에서, ALD 효소는 숙시닐-CoA 또는 아세틸-CoA 또는 이들 기질 둘다와 비교해, 아디필 CoA 기질에 대해 더 우수한 촉매 효율 및 활성을 가진다. 일부 구현예에서, ALD 효소는 하기 표 4에 나타낸 바와 같다. 일부 구현예에서, 본 발명의 비-천연성 미생물의 코딩 핵산으로부터 외인성으로 발현될 수 있는 TER 효소 서열은 아래 표 5에 나타낸 바와 같다.
일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 TA 효소 서열은 아래 표 6에 나타낸 바와 같다. 일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 TA 효소 변이체 서열은 아래 표 7에 나타낸 바와 같다.
일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 CAR 효소 서열은 아래 표 8에 나타낸다. 일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 CAR 변이체 서열은 아래 표 9에 나타낸다.
일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 CAR 효소 서열은 서열번호 153의 아미노산 서열을 포함하며, 아래 표 10에 나타낸 하나 이상의 아미노산 변이를 포함한다. 일부 구현예에서, CAR 효소는 아래 표 10에 나타낸 아미노산 변이 1, 2, 3, 4, 5, 6, 7 또는 8개를 포함할 수 있다.
일부 구현예에서, 본 발명의 비-천연성 미생물에서 코딩 핵산으로부터 외인성으로 발현될 수 있는 TA2 효소 서열은 아래 표 11에 나타낸다.
본원에 기술된 TA, CAR, TA2, TER 및/또는 ALD 효소들 중 임의의 것, 이중 일부 또는 모두는, 언급된 TA, CAR, TA2, TER 및/또는 ALD 효소적 변환 또는 변환들에서의 기질 및 생산물이 언급된 경로의 중간산물인 한, 본원에 기술된 임의의 생합성 경로에 이용될 수 있다. 예를 들어, TER은 5-카르복시-2-펜테노일-CoA (2,3-데하이드로아디필-CoA로도 언급됨) → 아디필-CoA 변환을 가진 언급된 효소에 대해 본원에 기술된 임의의 경로에서 치환될 수 있다. 마찬가지로, ALD는 아디필-CoA → 아디페이트 세미알데하이드 변환을 가진 언급된 효소에 대해 본원에 기술된 임의의 경로에서 치환될 수 있다. 나아가, TA 효소는 아디페이트 세미알데하이드 → 6ACA 변환을 가진 언급된 효소에 대해 본원에 기술된 임의의 경로에서 치환될 수 있다. 나아가, CAR 효소는 6ACA → 6-아미노카프로에이트 세미알데하이드 변환을 가진 언급된 효소에 대해 본원에 기술된 임의의 경로에서 치환될 수 있다. 아울러, TA2 효소는 6-아미노카프로에이트 → HMD 변환을 가진 언급된 효소에 대해 본원에 기술된 임의의 경로에서 치환될 수 있다. 이에, TA, CAR, TA2, TER 및/또는 ALD 중 임의의 1, 2, 3, 4 또는 모든 5종의 임의 조합 및/또는 순열을 본원에 기술된 생합성 경로에 이용할 수 있다.
TA, CAR, TA2, TER 및/또는 ALD 중 임의의 것, 일부 또는 이들 모두 이용할 수 있는 한가지 예시적인 경로는 TA, CAR, TA2, TER 및 ALD를 모두 이용하는 일 특정 구현예를 참조함으로써 도 10에 나타낸다. 일부 구현예에서, 나일론 중간산물은 도 10에 기술된 경로를 이용해 생합성된다. 일부 구현예에서, 도 10 경로는, 경로가 6-아미노카프로익산, 6-아미노카프로에이트 세미알데하이드 및 헥사메틸렌다이아민을 생산하기 위해 충분한 양으로 발현되는 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하는, 본원에 기술된 유전자 변형된 세포 (예, 비-천연성 미생물)에서 제공된다.
일부 구현예에서, 경로는 도 10에 나타낸 HMD 경로이다. HMD 경로는, HMD 경로가 HMD를 생산하기 위해 충분한 양으로 발현되는 HMD 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하는, 본원에 기술된 유전자 변형된 세포 (예, 비-천연성 미생물)에서 제공된다. 숙시닐-CoA 및 아세틸-CoA로부터 출발해, 효소들은 다음과 같이 지정된다: (A) 티올라제; (B) 하이드록시아디필-CoA 데하이드로게나제 (HBD); (C) 크로토나제; (D) 트랜스-에노일-CoA 리덕타제 (Ter); (E) 6ACA-알데하이드 데하이드로게나제 (ALD); (F) 6ACA-트랜스아미나제 (TA); (G) CoA 트랜스퍼라제/CoA 리가제; (H) HMD-알데하이드 데하이드로게나제 (ALD); (I) 카르복시산 리덕타제 (CAR), 및 (J) HMD-트랜스아미나제 (TA2). 포스포판테테이닐 트랜스퍼라제 (PPTase)를 코딩하는 외인성 핵산이 부가적으로 포함될 수 있다. CAR 효소를 이용하여 경로에서 단계 G 및 H를 생략할 수 있다. CAR을 이용하지 않을 경우, 단계 I를 생략할 수 있다.
도 10을 참조하여 본원에 기술된 CAR 효소를 이용하는 경우, 비-천연성 미생물은 다음과 같은 HMD 경로를 가진다: ABCDEFIJ, 여기서 단계 I은 6ACA → 6-아미노카프로에이트로의 CAR 변환이다. 상기 경로에서 효소 D, E, F 및 J는 각각 TER, ALD, TA 및 TA2 효소에 해당한다.
본원에서 사용되는 바와 같이, 용어 "비-천연성"은 미생물 유기체 또는 미생물에 대해 사용되는 경우, 미생물 유기체가 언급된 종의 야생형 균주를 비롯해, 언급된 종의 자연 발생 균주에서는 정상적으로 발견되지 않는 하나 이상의 유전자 변형을 가진 것을 의미하는 것으로 의도된다. 유전자 변이로는, 예를 들어, 대사 폴리펩타이드를 코딩하는 발현가능한 핵산을 도입하는 변형, 그외 핵산 부가, 핵산 결손 및/또는 미생물의 유전 물질의 기타 기능적인 파괴 등이 있다. 이러한 변형은, 예를 들어, 언급된 종들에 대해 이종의 폴리펩타이드, 상동적인 폴리펩타이드 또는 이종의 폴리펩타이드 및 상동적인 폴리펩타이드에 대한, 코딩 영역 및 이의 기능적 단편을 포함한다. 부가적인 변형으로는, 예를 들어, 변형이 유전자 또는 오페론의 발현을 변경하는, 비-코딩 조절 영역을 포함한다. 대사 폴리펩타이드에 대한 예로는 본원에 기술된 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 내 효소를 포함한다.
대사 변형은 자연 발생 상태로부터 변경된 생화학 반응을 지칭한다. 따라서, 비-천연성 미생물은 대사 폴리펩타이드 또는 이의 기능성 단편을 코딩하는 핵산에 유전자 변형을 가질 수 있다. 대사 변형에 대한 예는 본원에 개시되어 있다.
본원에서 사용되는 바와 같이, 용어 "미생물 (microbial)", "미생물 유기체" 또는 "미생물 (microorganism)"은 상호 호환적으로 사용되며, 고세균, 박테리아 또는 진핵생물류 범위에 속하는 미시 세포로서 존재하는 모든 유기체를 의미하는 것으로 의도된다. 즉, 이 용어는 미시 크기의 원핵생물 또는 진핵생물 세포 또는 유기체를 포괄하며, 모든 종의 박테리아, 고세균류 및 유박테리아 (eubacteria)뿐 아니라 효모 및 진균과 같은 진핵 미생물을 포함한다. 또한, 이 용어는 생화학적으로 생산하기 위해 배양가능한 임의 종의 세포 배양물을 포괄한다.
본원에서, 용어 "CoA" 또는 "코엔자임 A"는, 활성 효소 시스템을 구축하기 위해 다수의 효소 (주효소 (apoenzyme))들의 활성에 필요한, 유기 보조인자 또는 보결기 (효소의 비-단백질 부분)를 의미하는 것으로 의도된다. 코엔자임 A는 일부 축합 효소에서 작용하며, 아세틸 또는 기타 아실기 전달 및 지방산 합성과 산화, 피루베이트 산화 및 기타 아세틸화에 작용한다.
본원에서 사용되는 바와 같이, "아디페이트"는 화학식 -OOC-(CH2)4-COO- (도 1 참조)(IUPAC 명칭 헥산다이오에이트)을 가지며, 아디프산의 이온화된 형태 (IUPAC 명칭 헥산다이오익산)이며, 아디페이트와 아디프산은 전체적으로 상호 호환적으로 이의 임의의 염 형태를 비롯한 임의의 중성 또는 이온화된 형태의 화합물을 지칭하기 위해 사용될 수 있는 것으로 이해된다. 당해 기술 분야의 당업자라면 구체적인 형태가 pH에 의존함을 이해할 것이다.
본원에서 사용되는 바와 같이, "6-아미노카프로에이트"는 화학식 -OOC- (CH2)5-NH2으로서 (도 1 참조, 6-ACA로 약칭), 6-아미노카프로익산의 이온화된 형태 (IUPAC 명칭 6-아미노헥산산)이며, 6-아미노카프로에이트 및 6-아미노카프로익산은 전체적으로 상호 호환적으로 이의 임의의 염 형태를 비롯한 임의의 중성 또는 이온화된 형태의 화합물을 지칭하기 위해 사용될 수 있는 것으로 이해된다. 당해 기술 분야의 당업자라면 구체적인 형태가 pH에 의존함을 알 것이다.
본원에서 사용되는 바와 같이, "카프로락탐" (IUPAC 명칭 아제판-2-온)은 6-아미노헥산산의 락탐 (도 1, CPO로 약칭됨)이다.
본원에서 사용되는 바와 같이, "헥사메틸렌다이아민"은 또한 1,6-다이아미노헥산 또는 1,6-헥산다이아민이라고도 하며, 화학식 H2N(CH2)6NH2 (도 1, HMD로 약칭)를 가진다.
본원에서 사용되는 바와 같이, "1,6-헥산다이올"은 또한 헥산-1,6-다이올 및 헥사메틸렌다이올로도 지칭되며, 화학 구조 C6H14O2 (도 8 참조, HDO로 약칭)를 가진다.
본원에서 사용되는 바와 같이, 용어 "실질적으로 혐기성"은 배양 또는 증식 조건에 대해 사용되는 경우, 산소의 양이 액체 배지 내 용존 산소의 약 10% 미만의 포화도에 해당한다는 의미로 의도된다. 이 용어는 또한 산소 1% 미만의 대기가 유지되는 밀폐된 챔버 내 액체 배지 또는 고체 배지를 포함하는 것으로 의도된다.
본원에서 사용되는 바와 같이, 내삼투압제는 배양 또는 증식 조건에 대해 사용되는 경우, 삼투용질로서 작용하며 본원에 기술된 미생물 유기체가 삼투 스트레스로부터 생존하는데 일조하는 화합물을 지칭하는 것으로 의도된다. 내삼투압제로는, 베타인, 아미노산 및 당 트레할로스를 포함한다. 이에 대한 비-제한적인 예는 글리신 베타인, 프랄린 베타인, 다이메틸테틴, 다이메틸설포니오프로피오네이트, 3-다이메틸설포니오-2-메틸프로피오네이트, 피페콜산, 다이메틸설포니오아세테이트, 콜린, L-카르니틴 및 엑토인이다.
본원에서 사용되는 바와 같이, 용어 "증식-연계된"은 생화학적 생산과 관련하여 사용되는 경우, 미생물의 성장 단계 동안에 참조된 생화합물이 생합성되는 것을 의미하는 것으로 의도된다. 특정 구현예에서, 증식-연계된 생산은 편성 (obligatory), 즉 참조된 생화합물의 생합성이 미생물 성장 단계 동안에 필연적인 생산물임을 의미하는 것일 수 있다.
본원에서 사용되는 바와 같이, "대사 변형"은 자연 발생 상태로부터 변경된 생화학적 반응을 지칭하는 것으로 의도된다. 대사 변형은, 예를 들어, 반응에 참여하는 효소를 암호화하는 하나 이상의 유전자의 기능적 파괴에 의한 생화학적 반응 활성의 소거를 포함할 수 있다.
본원에서 사용되는 바와 같이, 용어 "유전자 파괴" 또는 이의 문법상 동의어는 코딩된 유전사 산물을 비활성으로 만드는 유전자 변이를 의미하는 것으로 의도된다. 유전자 변이는, 예를 들어, 전체 유전자의 결손, 전사 또는 변형에 필요한 조절 서열의 결손, 말단 절단된 유전자 산물을 만들게 되는 유전자의 일부 결손 또는 코딩된 유전자 산물을 불활화하는 임의의 다양한 돌연변이 전략에 의한 것일 수 있다. 유전자 파괴에 특히 이용가능한 한가지 방법은 비-천연성 미생물에서 유전자 회복 (genetic reversion) 발생을 낮추거나 또는 없앨 수 있으므로, 전체 유전자 결손이다.
본원에서 "외인성"은 언급된 분자 또는 언급된 활성이 숙주 미생물 유기체에 도입되는 것을 의미하는 것으로 의도된다. 이러한 분자는, 예를 들어, 숙주 염색체에 삽입에 의해 또는 플라스미드와 같은 비-염색체성 유전 물질로서와 같이, 코딩 핵산을 숙주 유전 물질에 도입함으로써, 도입될 수 있다. 따라서, 이 용어는, 코딩 핵산의 발현에 대해 적용되는 바와 같이, 코딩 핵산을 발현가능한 형태로 미생물 유기체에 도입하는 것을 의미한다. 생합성 활성에 대해 사용되는 경우, 이 용어는 숙주 참조 유기체에 도입되는 활성을 의미한다. 그 기원은, 예를 들어 숙주 미생물 유기체에 도입된 후 언급된 활성을 발현하는 동종의 또는 이종의 코딩 핵산일 수 있다. 이에, 용어 "내인성"은 숙주에 존재하는 언급된 분자 또는 활성에 대해 사용된다. 마찬가지로, 이 용어는, 코딩 핵산의 발현에 대해 사용될 경우, 미생물 유기체에 함유된 코딩 핵산의 발현을 지칭한다.
용어 "이종"은 언급된 종 이외의 다른 소스로부터 유래한 분자, 물질 또는 활성을 의미하며, "동종"은 숙주 미생물 유기체로부터 유래한 분자, 물질 또는 활성을 의미한다. 즉, 코딩 핵산의 외인성 발현은 이종의 또는 동종의 코딩 핵산 중 어느 하나 또는 둘다를 이용할 수 있다.
본원에서 사용되는 바와 같이, 용어 "약"은 언급된 값의 ± 10%를 의미한다. 용어 "약"은 반올림하는 것을 의미할 수 있다. 즉, 약 5%는 4.5% 내지 5.5%를 의미한다. 아울러, 지정된 수치를 참조하는 경우, 약은 또한 정확한 수치를 포함한다. 예를 들어, 약 5%는 또한 실제 5%를 포함한다.
본원에서 사용되는 바와 같이, 용어 "생물유래"는 6-아미노카프로익산, 1,6-헥산다이올, 카프로락톤, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 맥락에서, 이들 화합물이 미생물 유기체에서 합성되는 것을 의미한다.
2 이상의 외인성 핵산이 미생물 유기체에 포함되는 경우, 외인성 핵산은 상기 또는 하기 예시된 바와 같이 언급된 코딩 핵산 또는 생합성 활성을 의미하는 것으로 이해된다. 또한, 본원에 기술된 바와 같이, 이러한 외인성 핵산은 숙주 미생물 유기체에 개별 핵산 분자로, 폴리시스트론 핵산 분자로 또는 이의 조합으로 도입될 수 있으며, 여전히 2 이상의 외인성 핵산으로서 간주할 수 있는 것으로 또한 이해된다. 예를 들어, 본원에 기술된 바와 같이, 미생물 유기체는 원하는 경로 효소 또는 단백질을 코딩하는 2종 이상의 외인성 핵산을 발현하도록 조작될 수 있다. 원하는 활성을 코딩하는 2종의 외인성 핵산을 숙주 미생물 유기체에 도입하는 경우, 이들 2종의 외인성 핵산은 단일 핵산으로서, 예를 들어 단일 플라스미드 형태로 또는 분리된 플라스미드 형태로 도입할 수 있으며, 숙주 염색체 내 한 부위 또는 여러 부위에 병합될 수 있으며, 여전히 2종의 외인성 핵산으로 간주되는 것으로 이해된다. 마찬가지로, 3종 이상의 외인성 핵산을, 숙주 유기체에 임의의 원하는 조합으로, 예를 들어 하나의 플라스미드로, 각각의 개별 플라스미드로 도입할 수 있으며, 이는 숙주 염색체에 병합되지 않고, 염색체-외 요소로 잔류하지만, 여전히 2 이상의 외인성 핵산으로 간주되는 것으로 이해된다. 언급된 외인성 핵산 또는 생합성 활성의 개수는 숙주 유기체에 도입되는 분리된 핵산의 개수를 지칭하는 것이 아니라, 코딩 핵산의 개수 또는 생합성 활성의 개수를 지칭한다.
본 발명의 비-천연성 미생물 유기체는 안정적인 유전자 변이를 포함할 수 있는데, 이는 이러한 변이를 상실하지 않으면서 5 세대 이상 미생물을 배양가능한 것을 의미한다. 일반적으로, 안정적인 유전자 변이는 10 세대 이상 유지되는 변형을 포함하며, 특히 안정적인 변형은 약 25 세대 이상 유지될 것이며, 보다 구체적으로는 안정적인 유전자 변형은 50 세대 이상, 예를 들어 무기한으로 유지될 것이다.
유전자 파괴의 경우, 특히 유용한 안정적인 변이는 유전자 결손이다. 안정적인 유전자 변이 도입에 유전자 결손을 이용하는 것이, 특히 유전자 변이되기 이전의 표현형으로 복구될 가능성을 낮추므로 유용하다. 예를 들어, 안정적인 증식-연계된 생화합물의 생산은, 예를 들어, 대사 변형 세트에 포함된 하나 이상의 반응을 촉매하는 효소에 대한 코딩 유전자를 결손시킴으로써, 달성할 수 있다. 증식-연계된 생화합물의 생산 안정성은, 각각의 파괴된 활성에 대한 복수의 보완적인 회복 (compensatory reversion) 발생 가능성을 현저하게 낮추는, 복수의 결손을 통해 추가적으로 높일 수 있다.
당해 기술 분야의 당업자라면, 본원에 예시된 대사 변형을 포함한 유전자 변이가, E. coli와 같은 적절한 유기체 및 이의 대응되는 대사 반응 또는 원하는 대사 경로를 위한 유전자 등의 바람직한 유전 물질에 적합한 소스 유기체에 대해 기술됨을, 이해할 것이다. 그러나, 매우 다양한 유기체들에서 전체 게놈 서열 분석 및 게놈학 분야의 높은 기술 수준을 감안한다면, 당해 기술 분야의 당업자라면 본원에 기술된 교시 내용 및 지침을 기본적으로 다른 모든 유기체들에도 적용할 수 있음을 쉽게 알 것이다. 예를 들어, 본원에 예시된 E. coli의 대사 변이는 언급된 종이 아닌 다른 종 유래의 동일한 또는 유사한 코딩 핵산을 병합함으로써, 다른 종에도 쉽게 적용할 수 있다. 이러한 유전자 변이로는, 예를 들어 일반적으로 종 상동체 (species homolog)의 유전자 변이 등이 있으며, 구체적으로 오르소로그 (ortholog), 파라로그 (paralog) 또는 비-오르소로그 유전자 치환 (non-orthologous gene displacement)을 포함한다.
오르소로그는, 수직 직계 (vertical descent) 관계이면서 여러가지 유기체들에서 실질적으로 동일하거나 상동한 기능을 담당하는, 유전자 또는 유전자들이다. 예를 들어, 마우스 에폭사이드 하이드롤라제와 인간 에폭사이드 하이드롤라제는 에폭사이드의 가수분해라는 생물학적 기능 측면에서 오르소로그로 간주할 수 있다. 예를 들어, 유전자들이 상동적이거나 또는 공통 조상으로부터 진화적으로 관련있는 것으로 보기에 충분한 서열 유사성을 공유하는 경우, 이들 유전자들은 수직 직계 관계이다. 또한, 유전자가, 3차 구조를 공유하지만, 1차 서열 유사성이 확인불가한 수준으로 공통 조상으로부터 진화된 것임을 의미하는 충분한 수준의 서열 유사성을 반드시 가지고 있지 않은 경우에도, 오르소로그로 간주할 수 있다. 오르소로그 유전자들은 아미노산 서열 아이덴터티 약 25% 내지 100%의 서열 유사성을 가진 단백질을 코딩할 수 있다. 25% 미만의 아미노산 유사성을 공유하는 단백질을 코딩하는 유전자들 역시, 이들의 3차원 구조에 유사성이 있다면, 수직 직계에 의해 생겨난 것으로 간주할 수 있다. 조직 플라스미노겐 활성인자 및 엘라스타제 등의 세린 프로테아제 패밀리 효소에 속하는 구성원들은 공통 조상으로부터 수직 직계에 의해 생겨난 것으로 간주된다.
오르소로그는, 예를 들어, 진화를 통해 구조적으로 또는 전체 활성 측면에서 분화된 유전자 또는 이로 코딩되는 유전자 산물을 포함한다. 예를 들어, 어떤 종이 2가지 기능을 나타내는 유전자 산물을 코딩하고 있으며 이 기능들이 제2의 종에서 별개의 유전자들로 분리되어 있다면, 이들 유전자 3개와 이의 대응되는 산물은 오르소로그로 간주한다. 당해 기술 분야의 당업자라면, 생화학적 산물 생산시, 비-천연성 미생물을 구축하기 위해 도입 또는 파괴시킬 대사 활성을 가지고 있는 오르소로그 유전자를 선택해야 함을, 알 것이다. 분리가능한 활성들을 나타내는 오르소로그의 예는, 개개 활성이 2종 이상의 종들에서 또는 하나의 종에서 개별 유전자 산물로 분리되어 있는 경우이다. 구체적인 예는, 세린 프로테아제 활성을 가진 2가지 타입, 즉 엘라스타제 단백질 분해 활성과 플라스미노겐 단백질 분해 활성이, 플라스미노겐 활성인자 및 엘라스타제로서 개별 분자로 분리된 경우이다. 두 번째 예는, 마이코플라스마 5'-3' 엑소뉴클레아제 및 드로소필라 DNA 중합효소 III 활성이 분리된 경우이다. 첫 번째 종 유래의 DNA 중합효소는, 2번째 종 유래의 엑소뉴클레아제 또는 중합효소 중 어느 하나 또는 이들 둘다에 대해 오르소로그인 것으로 간주할 수 있으며, 그 역도 성립할 수 있다.
이와는 반대로, 파라로그는, 예를 들어, 복제 및 이후 진화적 분화 관계에 있는 상동체이며, 기능이 유사하거나 또는 공통적이지만, 동일한 것은 아니다. 파라로그는, 예를 들어, 동일 종 또는 다른 종으로부터 기원하거나 또는 유래할 수 있다. 예를 들어, 마이크로솜 에폭사이드 하이드롤라제 (에폭사이드 하이드롤라제 I)와 가용성 에폭사이드 하이드롤라제 (에폭사이드 하이드롤라제 II)는, 이들이 별개의 반응을 촉매하고 동일 종에서 다른 기능을 가지고 있는, 공통 조상으로부터 함께 진화된 2종의 별개의 효소이므로, 파라로그로 간주할 수 있다. 파라로그는 서로 유의미한 수준의 서열 유사성을 보이는 동일한 종으로부터 유래된 단백질들이므로, 이들은 상동적이거나 또는 공통 조상으로부터 함께 진화된 관계임을 시사한다. 파라로그 단백질 패밀리 그룹으로는 HipA 상동체, 루시퍼라제 유전자, 펩티다제 등이 있다.
비-오르소로그 유전자 치환 (nonorthologous gene displacement)은 어떤 종 유래의 비-오르소로그 유전자가 다른 종에서 언급된 유전자의 기능을 치환할 수 있는 것을 의미한다. 치환은, 예를 들어 여러가지 종들에서 언급된 기능과 비교해, 기원 종에서 동일하거나 또는 유사한 작용을 실질적으로 수행할 수 있는 것을 포함한다. 일반적으로, 비-오르소로그 유전자 치환은 언급된 기능을 코딩하는 공지된 유전자와 구조적으로 관련있는 것으로 구분할 수 있지만, 구조적으로 관련성은 낮지만 기능적으로 유사한 유전자 및 이의 유전자 산물도 그럼에도 불구하고 여전히 본 발명에 사용되는 용어의 의미에 포함될 것이다. 기능 유사성에는, 예를 들어 치환하고자 하는 기능을 코딩하는 유전자에 대해, 비-오르소로그 유전자 산물의 활성부 또는 결합부에서 어느 정도 이상의 구조 유사성이 요구된다. 따라서, 비-오르소로그 유전자는 예를 들어 파라로그 또는 비-관련 유전자 (unrelated gene)를 포함한다.
이에, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 능력을 갖춘 본 발명의 비-천연성 미생물 유기체를 동정하고 구축함에 있어, 당해 기술 분야의 당업자는, 본 발명에 제공된 교시 내용 및 지침을 특정 종들에 적용하여, 대사 변형의 식별이 오르소로그의 동정 및 이의 함유 또는 불활성화를 포함할 수 있음을 알 것이다. 당해 기술 분야의 당업자라면, 또한, 파라로그 및/또는 비-오르소로그 유전자 치환이, 유사하거나 또는 실질적으로 유사한 대사 반응을 촉매하는 효소를 코딩하는 언급된 미생물에 존재하는 한, 진화 관계의 유전자들을 이용할 수 있다. 유전자 파괴 전략에서는, 진화 관계의 유전자들도 숙주 세포, 파라로그 또는 오르소로그에서 파괴 또는 결손시켜, 파괴에 표적이 되는 효소 활성들의 기능적 중복성 (functional redundancy)이 설계된 대사 변형의 회로를 단축하도록 하기 위해, 활성을 줄이거나 또는 없앨 수 있다.
오르소로그, 파라로그 및 비-오르소로그 유전자 치환은 당해 기술 분야의 당업자에게 널리 공지된 방법으로 결정할 수 있다. 예를 들어, 2종의 폴리펩타이드에 대한 핵산 또는 아미노산 서열을 조사함으로써, 비교 서열들 간의 서열 동일성 및 유사성을 확인한다. 이러한 유사성을 토대로, 당해 기술 분야의 당업자는 이들 단백질들이 공통 조상으로부터 진화된 관계임을 의미할 만큼 유사성이 충분히 높은지를 결정할 수 있다. 당해 기술 분야의 당업자들에게 널리 공지된 알고리즘, 예를 들어 Align, BLAST, Clustal W 등으로 원 (raw) 서열의 유사성 또는 동일성을 비교 및 확인하고, 또한, 서열에서 갭의 존재나 유의 수준을 결정하여, 가중치 (weight) 또는 스코어를 할당할 수 있다. 이들 알고리즘은 또한 당해 기술 분야에 공지되어 있으며, 뉴클레오타이드 서열 유사성 또는 동일성 결정에 마찬가지로 적용가능하다. 관계 (relatedness)를 정할 만큼 충분한 유사성에 대한 매개변수들은, 널리 공지된 통계학적 유사성 계산법, 또는 랜덤 폴리펩타이드에서 유사한 매칭을 발견할 확률, 그리고 확인된 매칭의 유의 수준을 토대로 산출한다. 2 이상 서열들에 대한 전산적 비교는, 또한, 필요한 경우, 당해 기술 분야의 당업자에 의해 시각적으로 최적화될 수 있다. 관련 유전자 산물 또는 단백질은 높은 유사성, 예를 들어 25% 내지 100%의 서열 동일성을 가지는 것으로 볼 수 있다. 비-관련 단백질은, 충분한 크기의 데이터베이스를 검색한다면, 우연히 발생할 것으로 예상되는 수준 (약 5%)과 기본적으로 동일한, 동일성을 가질 수 있다. 5% 내지 24% 사이의 서열은, 비교되는 서열들이 관련성이 있다고 판단할 만큼 충분한 상동성을 보이거나 또는 그렇지 않을 수 있다. 데이터 세트의 크기를 감안해 이러한 매칭의 유의 수준을 결정하기 위한 추가적인 통계학적 분석을 수행하여, 이들 서열들의 관련성을 결정할 수 있다.
BLAST 알고리즘을 사용해 2 이상의 서열들의 관계를 확인하기 위한 매개변수의 예는, 다음과 같을 수 있다. 간략하게는, 아미노산 서열 정렬은 BLASTP 버전 2.2.29+ (2014년 1월 14일) 및 하기의 매개변수들을 사용하여 수행할 수 있다: 매트릭스: 0 BLOSUM62; 갭 오픈 (gap open): 11; 갭 연장 (gap extension): 1; x_드롭오프: 50; 예상: 10.0; 문자 크기: 3; 필터: 온 (on). 핵산 서열 정렬은 BLASTN 버전 2.0.6 (1998년 9월 16일) 및 하기의 매개변수들을 사용하여 수행할 수 있다: 매치: 1; 미스매치: -2; 갭 오픈: 5; 갭 연장: 2; x_드롭오프: 50; 예상: 10.0; 문자 크기: 11; 필터: 오프. 당해 기술 분야의 당업자는, 예를 들어 비교시 엄격성을 높이거나 또는 낮추고, 2 이상 서열의 관계를 정하기 위해, 상기한 매개변수에 어떤 변화를 가할 수 있음을 알 것이다.
도면에 기술된 바와 같은 경로 등의 본원에 개시된 임의 경로를 이용해, 필요에 따라 임의의 경로 중간산물 또는 산물을 생산하는 비-천연성 미생물 유기체를 구축할 수 있는 것으로 이해된다. 본원에 기술된 바와 같이, 중간산물을 생산하는 이러한 미생물 유기체는 원하는 산물을 생산하기 위해 하류 경로 효소를 발현하는 다른 미생물 유기체와 조합하여 이용할 수 있다. 그러나, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 중간산물을 생산하는 비-천연성 미생물 유기체를 원하는 산물로서 중간산물을 생산하는데 이용할 수 있는 것으로 이해된다.
본 발명은 대사 반응, 반응제 또는 이의 생산물을 일반적으로 참조하거나, 또는 참조한 대사 반응, 반응제 또는 생산물과 관련있거나 또는 이를 촉매하는 효소를 코딩하는 하나 이상의 핵산 또는 유전자를 구체적으로 참조하여 본원에 기술된다. 본원에 명확하게 달리 언급되지 않은 한, 당해 기술 분야의 당업자는, 반응에 대한 언급 역시 반응의 반응제 및 생산물에 대한 언급임을 이해할 것이다. 마찬가지로, 본원에 명확하게 달리 언급되지 않은 한, 반응제 또는 생산물에 대한 언급 역시 반응을 언급하는 것이며, 이들 임의의 대사 구성성분에 대한 언급 또한 참조 반응, 반응제 또는 생산물을 촉진하는 효소를 코딩하는 유전자 또는 유전자들을 언급하는 것이다. 마찬가지로, 널리 공지된 대사 생화학, 효소학 및 게놈 분야를 감안하여, 유전자 또는 코딩 핵산에 대한 언급은 대응되는 코딩된 효소 및 이것이 촉매하는 반응뿐 아니라 반응의 반응제 및 생산물을 또한 언급하는 것이다.
비-천연성 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 중 하나 이상에 참여하는 하나 이상의 효소를 코딩하는 발현가능한 핵산을 도입함으로써 생산할 수 있다. 생합성을 위해 선정된 숙주 미생물 유기체에 따라, 구체적인 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 일부 또는 전부에 대한 핵산들을 발현시킬 수 있다. 예를 들어, 선정된 숙주에 원하는 생합성 경로에 대한 하나 이상의 효소이 결핍되어 있다면, 이 결핍 효소(들)에 대한 발현가능한 핵산을 후속적인 외인성 발현을 위해 숙주에 도입한다. 대안적으로, 선정된 숙주가 일부 경로 유전자를 내인성 발현하지만 다른 유전자는 결핍되어 있다면, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성을 달성하기 위한 결핍 효소(들)에 대한 코딩 핵산이 필요하다. 즉, 비-천연성 미생물 유기체는 원하는 생합성 경로를 달성하기 위해 외인성 효소 활성을 도입함으로써 구축할 수 있거나, 또는 원하는 생합성 경로는 하나 이상의 내인성 효소와 함께 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올과 같은 원하는 산물을 생산하는 하나 이상의 외인성 효소 활성을 도입함으로써 달성할 수 있다.
선택된 숙주 미생물 유기체의 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 구성요소에 따라, 비-천연성 미생물 유기체는 하나 이상의 외인성으로 발현되는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로-코딩 핵산 및 하나 이상의 아디페이트, 6-아미노카프로익산 또는 카프로락탐 생합성 경로들에 대한 최대한으로는 모든 코딩 핵산을 함유할 것이다. 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성은 대응되는 코딩 핵산의 외인성 발현을 통해 경로 효소가 결핍된 숙주에서 확립할 수 있다. 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로의 모든 효소가 결핍된 숙주의 경우에는, 경로의 모든 효소들이 심지어 숙주가 경로 효소 하나 이상을 함유하는 경우에도 발현할 수 있는 것으로 이해됨에도 불구하고, 경로의 모든 효소들을 외인성 발현으로 포함시킬 수 있다.
본원에 제공된 교시 내용 및 지침을 감안하여, 발현가능한 형태로 도입하기 위한 코딩 핵산의 개수는 적어도 선택 숙주 세포의 아디페이트, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로에서 결여된 것에 대응함을, 당해 기술 분야의 당업자라면 이해할 것이다. 따라서, 본 발명의 비-천연성 미생물 유기체는, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로를 구성하는 상기한 효소들을 코딩하는 핵산들을 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 또는 12종, 최대 이들 전부를 포함할 수 있다. 일부 구현예에서, 비-천연성 미생물 유기체는 또한 숙주 미생물 유기체에 다른 유용한 기능을 부여하거나 또는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성을 촉진하거나 또는 최적화하는 다른 유전자 변형을 포함할 수 있다. 이러한 다른 기능성으로는, 본원에 개시된 아디페이트 경로 효소를 비롯하여, 아디페이트 합성의 경우 숙시닐-CoA 및/또는 아세틸-CoA, 또는 6-아미노카프로익산, 카프로락탐 또는 HMD 합성의 경우 아디필-CoA 또는 아디페이트, 또는 6-아미노카프로에이트 합성의 경우 피루베이트 및 숙시닉 세미알데하이드, 글루타메이트, 글루타릴-CoA, 호모라이신 또는 2-아미노-7-옥소서바레이트, 또는 헥사메틸렌다이아민 합성의 경우 6-아미노카프로에이트, 글루타메이트, 글루타릴-CoA, 피루베이트 및 4-아미노부타날, 또는 2-아미노-7-옥소서바레이트와 같이, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 전구체들 중 하나 이상의 합성 증가를 포함할 수 있다.
일부 구현예에서, 비-천연성 미생물 유기체는 아디페이트 세미알데하이드와 반응하여 6ACA를 생성하고; 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116 중 어느 하나에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50% 아미노산 서열 동일성을 가진 아미노산 서열을 포함하는 트랜스아미나제로부터 선택되는, 트랜스아미나제를 코딩하는 하나 이상의 외인성 핵산을 가진다.
일부 구현예에서, 비-천연성 미생물 유기체는 6ACA와 반응해 6-아미노카프로에이트 세미알데하이드를 생성하고; 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264 중 어느 하나에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50% 아미노산 서열 동일성을 가진 아미노산 서열을 포함하는 CAR로부터 선택되는, CAR을 코딩하는 하나 이상의 외인성 핵산을 가진다.
일부 구현예에서, 비-천연성 미생물 유기체는 6ACA와 반응해 6-아미노카프로에이트 세미알데하이드를 생성하고; 서열번호 265 및 267-296 중 어느 하나에서 연속 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 약 50% 아미노산 서열 동일성을 가진 아미노산 서열을 포함하는 CAR로부터 선택되는, CAR을 코딩하는 하나 이상의 외인성 핵산을 가진다.
일반적으로, 숙주 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로의 전구체를 천연 생산 분자로서 또는 원하는 전구체의 데 노보 생산 또는 숙주 미생물 유기체에 의해 천연 생산되는 전구체의 생산 증가를 제공하는 조작된 생산물로서 생산하도록 선택된다. 숙주 유기체는 본원에 기술된 바와 같이 전구체의 생산을 높이도록 조작될 수 있다. 아울러, 원하는 전구체를 생산하도록 조작된 미생물 유기체는 숙주 유기체로서 이용할 수 있으며, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로의 효소 또는 단백질을 발현하도록 추가로 조작할 수 있다.
일부 구현예에서, 비-천연성 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 합성할 수 있는 효소학적 능력을 가진 숙주로부터 구축된다. 이러한 특정 구현예에서, 예를 들어 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 반응을 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산하도록 유도하기 위해, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로의 생산물 합성 또는 축적을 높이는 것이 유용할 수 있다. 합성 또는 축적 증가는 예를 들어 전술한 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소 중 하나 이상의 코딩 핵산의 과다 발현에 의해 달성될 수 있다. 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소 또는 효소들의 과다 발현은, 예를 들어, 내인성 유전자 또는 유전자들의 외인성 발현을 통해 또는 이종의 유전자 또는 유전자들의 외인성 발현을 통해 이루어질 수 있다. 따라서, 자연 발생 유기체는, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 효소를 코딩하는 핵산 적어도 1, 2, 3, 4, 5, 6, 7, 8,9,10, 11, 12, 13 또는 14종, 즉 최대한으로는 모든 핵산의 과다 발현을 통해, 예를 들어 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하는 비-천연성 미생물 유기체로 쉽게 구축할 수 있다. 아울러, 비-천연성 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로에서 효소의 활성 증가를 달성하는 내인성 유전자의 돌연변이 유발에 의해 구축할 수 있다.
특히 유익한 구현예에서, 코딩 핵산의 외인성 발현을 이용한다. 외인성 발현은, 사용자에 의해 조절되는 원하는 발현 수준을 달성하기 위해, 발현 및/또는 조절 요소를 맞춤 조절하는 능력을 숙주 및 어플리케이션에 부여한다. 그러나, 내인성 발현도, 유도성 프로모터 또는 다른 조절 인자와 연계되었을 경우, 유전자의 프로모터의 유도 또는 네거티브 조절 작동인자를 제거함으로써와 같이, 다른 구현예에서 이용할 수 있다. 따라서, 자연 발생 유도성 프로모터를 가진 내인성 유전자는 적절한 유도성 물질을 제공함으로써 상향-조절하거나, 또는 내인성 유전자의 조절 영역을 유도성 조절 인자가 병합되도록 조작하여, 원하는 시점에 내인성 유전자의 발현 증가를 조절할 수 있다. 마찬가지로, 비-천연성 미생물 유기체에 도입된 외인성 유전자에 대한 조절 인자로서 유도성 프로모터를 포함할 수 있다.
일부 구현예에서, 비-천연성 미생물 유기체는 하나 이상의 유전자 파괴를 포함하며, 이 경우 유기체 6-ACA, 아디페이트 및/또는 HMD를 생산하게 된다. 파괴는, 유전자 파괴가 비-천연성 유기체에 아디페이트, 6-ACA 및/또는 HMD의 생산 증가를 부여하도록, 유전자 파괴가 효소 활성을 감소시키는 경우 아디페이트, 6-ACA 및/또는 HMD의 생산 유기체의 증식과 연계시키는 효소를 코딩하는 유전자에서 발생한다. 따라서, 일부 구현예에서, 하나 이상의 유전자 파괴를 포함하는 비-천연성 미생물 유기체를 제공하며, 하나 이상의 유전자 파괴는 단백질 또는 효소를 코딩하는 유전자에서 이루어지며, 하나 이상의 유전자 파괴는 유기체에서 아디페이트, 6-ACA 및/또는 HMD의 생산 증가를 부여한다. 본원에 기술된 바와 같이, 이러한 유기체는 아디페이트, 6-ACA 및/또는 HMD의 생산 경로를 포함한다.
방법에서, 임의의 하나 이상의 외인성 핵산을 미생물 유기체에 도입해 비-천연성 미생물 유기체를 생산할 수 있는 것으로 이해된다. 핵산은, 예를 들어 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로를 미생물 유기체에 부여하기 위해 도입할 수 있다. 대안적으로, 코딩 핵산을 도입하여, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 능력을 부여하기 위해 필요한 반응들 중 일부를 촉매하는 생합성 능력을 가진 중간 미생물 유기체를 구축할 수 있다. 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로를 가진 비-천연성 미생물 유기체는 원하는 효소를 코딩하는 외인성 핵산 적어도 2종을 포함할 수 있다. 아디페이트 생산 경우에, 2 이상의 외인성 핵산은 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제 및 3-하이드록시아실-CoA 데하이드로게나제, 또는 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제 및 3-하이드록시아디필-CoA 데하이드라타제, 또는 3-하이드록시아디필-CoA 및 아디페이트 세미알데하이드 트랜스아미나제, 또는 3-하이드록시아실-CoA 및 아디필-CoA 신테타제 등의 조합과 같은 효소를 코딩할 수 있다. 카프로락탐 생산 경우에, 2 이상의 외인성 핵산은 CoA-의존적인 트랜스-에노일-CoA 리덕타제 및 트랜스아미나제, 또는 CoA-의존적인 트랜스-에노일-CoA 리덕타제 및 아미도하이드롤라제, 또는 트랜스아미나제 및 아미도하이드롤라제의 조합과 같은 효소를 코딩할 수 있다. 6-아미노카프로익산을 생산하는 경우, 2 이상의 외인성 핵산은 4-하이드록시-2-옥소헵탄-1,7-다이오에이트 (HODH) TAolase 및 2-옥소헵트-4-엔-1,7-다이오에이트 (OHED) 하이드라타제, 또는 2-옥소헵트-4-엔-1,7-다이오에이트 (OHED) 하이드라타제 및 2-아미노헵탄-1,7-다이오에이트 (2-AHD) 데카르복실라제, 3-하이드록시아디필-CoA 데하이드라타제 및 아디필-CoA 데하이드로게나제, 글루타밀-CoA 트랜스퍼라제 및 6-아미노피멜로일-CoA 하이드롤라제, 또는 글루타릴-CoA β-케토티올라제 및 3-아미노피멜레이트 2,3-아미노무타제의 조합과 같은 효소를 코딩할 수 있다. 헥사메틸렌다이아민을 생산하는 경우, 2 이상의 외인성 핵산은 6-아미노카프로에이트 키나제 및 [(6-아미노헥사노일)옥시]포스포네이트 (6-AHOP) 옥시도리덕타제, 또는 6-아세트아미도헥사노에이트 키나제 및 [(6-아세트아미도헥사노일)옥시]포스포네이트 (6-AAHOP) 옥시도리덕타제, 6-아미노카프로에이트 N-아세틸트랜스퍼라제 및 6-아세트아미도헥사노일-CoA 옥시도리덕타제, 3-하이드록시-6-아미노피멜로일-CoA 데하이드라타제 및 2-아미노-7-옥소헵타노에이트 아미노트랜스퍼라제, 또는 3-옥소피멜로일-CoA 리가제 및 호모라이신 데카르복실라제의 조합과 같은 효소를 코딩할 수 있다. 따라서, 생합성 경로의 2종 이상의 효소들의 임의 조합이 비-천연성 미생물 유기체에 포함될 수 있는 것으로 이해된다. 도 10을 참조하여, 6ACA, 6-아미노카프로에이트 세미알데하이드 또는 HMD의 경우, 2 이상의 외인성 핵산은 단계 10A 및 10B, 10B 및 10C, 10C 및 10D, 10D 및 10E, 10E 및 10F, 10F 및 10I 및/또는 10I 및 10J에 표시된 효소들의 조합, 또는 단계 10A, 10B, 10C, 10D, 10E, 10F, 10I 및/또는 10J에 표시된 효소 2종, 3종, 4종, 5종, 6종, 7종 및/또는 8종의 임의 조합과 같은 효소를 코딩할 수 있다.
마찬가지로, 원하는 생합성 경로의 효소 조합이 대응되는 원하는 산물 생산을 달성하는 한, 비-천연성 미생물 유기체에 생합성 경로의 3종 이상의 효소들의 임의 조합을, 예를 들어, 아디페이트를 생산하는 경우, 필요에 따라 효소 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제, 3-하이드록시아실-CoA 데하이드로게나제, 및 3-하이드록시아디필-CoA 데하이드라타제; 또는 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제, 3-하이드록시아실-CoA 데하이드로게나제 및 아디페이트 세미알데하이드리덕타제; 또는 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제, 3-하이드록시아실-CoA 데하이드로게나제 및 아디필-CoA 신테타제; 또는 3-하이드록시아실-CoA 데하이드로게나제, 3-하이드록시아디필-CoA 데하이드라타제 및 아디필-CoA: 아세틸-CoA 트랜스퍼라제 등의 조합을 포함시킬 수 있는 것으로 이해된다. 6-아미노카프로익산을 생산하는 경우, 3 이상의 외인성 핵산이 4-하이드록시-2-옥소헵탄-1,7-다이오에이트 (HODH) TAolase, 2-옥소헵트-4-엔-1,7-다이오에이트 (OHED) 하이드라타제 및 2-옥소헵탄-1,7-다이오에이트 (2-OHD) 데카르복실라제, 또는 2-옥소헵트-4-엔-1,7-다이오에이트 (OHED) 하이드라타제, 2-아미노헵트-4-엔-1,7-다이오에이트 (2-AHE) 리덕타제 및 2-아미노헵탄-1,7-다이오에이트 (2-AHD) 데카르복실라제, 또는 3-하이드록시아디필-CoA 데하이드라타제, 2,3-데하이드로아디필-CoA 리덕타제 및 아디필-CoA 데하이드로게나제, 또는 6-아미노-7-카르복시헵트-2-에노일-CoA 리덕타제, 6-아미노피멜로일-CoA 하이드롤라제 및 2-아미노피멜레이트 데카르복실라제, 또는 글루타릴-CoA β-케토티올라제, 3-아민화 옥시도리덕타제 및 2-아미노피멜레이트 데카르복실라제, 또는 3-옥소아디필-CoA 티올라제, 5-카르복시-2-펜테노에이트 리덕타제 및 아디페이트 리덕타제의 조합과 같은 효소를 코딩할 수 있다. 헥사메틸렌다이아민을 생산하는 경우, 3 이상의 외인성 핵산이 6-아미노카프로에이트 키나제, [(6-아미노헥사노일)옥시]포스포네이트 (6-AHOP) 옥시도리덕타제 및 6-아미노카프로익 세미알데하이드 아미노트랜스퍼라제, 또는 6-아미노카프로에이트 N-아세틸트랜스퍼라제, 6-아세트아미도헥사노에이트 키나제 및 [(6-아세트아미도헥사노일)옥시]포스포네이트 (6-AAHOP) 옥시도리덕타제, 또는 6-아미노카프로에이트 N-아세틸트랜스퍼라제, [(6-아세트아미도헥사노일)옥시]포스포네이트 (6-AAHOP) 아실트랜스퍼라제 및 6-아세트아미도헥사노일-CoA 옥시도리덕타제, 또는 3-옥소-6-아미노피멜로일-CoA 옥시도리덕타제, 3-하이드록시-6-아미노피멜로일-CoA 데하이드라타제 및 호모라이신 데카르복실라제, 또는 2-옥소-4-하이드록시-7-아미노헵타노에이트 TAolase, 2-옥소-7-아미노헵트-3-에노에이트 리덕타제 및 호모라이신 데카르복실라제, 또는 6-아세트아미도헥사노에이트 리덕타제, 6-아세트아미도헥사날 아미노트랜스퍼라제 및 6-아세트아미도헥산아민 N-아세틸트랜스퍼라제의 조합과 같은 효소를 코딩할 수 있다. 도 10을 참조하여 6ACA, 6-아미노카프로에이트 세미알데하이드 또는 HMD를 생산하는 경우, 3 이상의 외인성 핵산이 단계 10A, 10B 및 10C; 10B, 10C 및 10D; 10C, 10D 및 10E; 10D, 10E 및 10F; 10E, 10F 및/또는 10I; 10F, 10I 및 10J에 표시된 효소들의 조합, 또는 단계 10A, 10B, 10C, 10D, 10E, 10F, 10I 및/또는 10J에 표시된 효소 3종, 4종, 5종, 6종, 7종 및/또는 8종의 임의 조합과 같은 효소를 코딩할 수 있다. 마찬가지로, 본원에 기술된 생합성 경로의 4종 이상의 효소의 임의 조합이, 원하는 생합성 경로의 효소 조합이 대응되는 원하는 산물 생산을 달성하는 한, 비-천연성 미생물 유기체에 포함될 수 있다.
본원에 기술된 바와 같이 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성과 더불어, 비-천연성 미생물 유기체 및 방법은 또한 서로, 그리고 다른 경로를 통해 생산물의 생합성을 달성하기 위해 다른 미생물 유기체 및 당해 기술 분야에 잘 알려진 방법과 다양한 조합으로 이용할 수 있다. 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 균주가 아닌 다른 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위한 한가지 대안은, 아디페이트, 6-아미노카프로익산 또는 카프로락탐 경로 중간산물을 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올로 변환할 수 있는, 다른 미생물 유기체를 부가함으로써 이루어진다. 이러한 한가지 방법은, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로의 중간산물을 생산하는 미생물 유기체를 배양하는 것이다. 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로의 중간산물은 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로의 중간산물을 6-아미노카프로익산, 카프로락탐 또는 헥사메틸렌다이아민으로 변환하는, 제2 미생물 유기체에 기질로 이용할 수 있다. 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로의 중간산물은 제2의 유기체의 다른 배양물에 직접 첨가하거나, 또는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로의 중간산물 생산 균주의 오리지널 배양물은, 예를 들어, 세포 분리에 의해 이들 미생물 유기체를 제거한 다음, 발효 브로스에 제2의 유기체를 후속적으로 첨가하여 중간산물의 정제 단계 없이 최종 생산물을 제조할 수 있다.
다른 구현예들에서, 비-천연성 미생물 유기체 및 방법은, 예를 들어 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 달성하기 위해 매우 다양한 하위-경로들로 조합될 수 있다. 이들 구현예에서, 원하는 생산물을 위한 생합성 경로는 여러 미생물 유기체들에 분할되어 있을 수 있으며, 이들 여러 미생물 유기체들을 공-배양하여 최종 생산물을 생산할 수 있다. 이러한 생합성 공정에서, 하나의 미생물 유기체의 생산물은 최종 생산물이 합성될 때까지 제2 미생물 유기체의 기질이 된다. 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성은 하나의 경로 중간산물을 다른 경로 중간산물 또는 생산물로 변환하기 위한 생합성 경로를 포함하는 미생물 유기체를 구축함으로써 달성할 수 있다. 대안적으로, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올은 동일 용기에서 2종의 유기체를 이용한 공-배양 또는 공-발효를 미생물 유기체로부터 생합성 방식으로 생산할 수 있으며, 이때 제1 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 중간산물을 생산하고, 제2 미생물 유기체는 이러한 중간산물을 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올로 변환한다.
본원에 제공된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자라면, 하위-경로를 구비한 다른 비-천연성 미생물 유기체와의 공-배양과, 그리고 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위한 당해 기술 분야에서 잘 알려진 다른 화학적 및/또는 생화학적 공정들의 조합과 더불어, 비-천연성 미생물 유기체 및 방법에 대해 매우 다양한 조합 및 치환들이 존재함을, 알 것이다.
마찬가지로, 당해 기술 분야의 당업자라면, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해 하나 이상의 유전자 파괴를 도입하는데 요망되는 특징을 토대로, 숙주 유기체를 선택할 수 있음을 이해할 것이다. 따라서, 유전자를 파괴하기 위해 숙주 유기체에 유전자 변형을 도입하고자 한다면, 요망되는 대사 반응이 충분히 파괴되도록 유사하지만 동일하지 않은 대사 반응을 촉매하는 임의의 상동체, 오르소로그 또는 파라로그를 마찬가지로 파괴할 수 있는 것으로 이해된다. 서로 다른 유기체들 간에는 대사 네트워크에 일부 차이가 존재하므로, 당해 기술 분야의 당업자라면, 주어진 유기체에서 파괴할 실제 유전자들이 유기체들에 따라 서로 다를 수 있음을 알 것이다. 그러나, 본원에 제공된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자는, 또한, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 강화할 대상 종에서 유기체를 구축하는데 필요한 동계 (cognate) 대사 변이를 식별하기 위해, 임의의 적절한 숙주 미생물에, 본 방법을 적용할 수 있음을, 알 것이다. 특정 구현예에서, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 유기체의 증식과 결합시키는 것을 포함하며, 요망되는 경우 본원에 기술된 바와 같이, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생산을 유기체의 증식과 필연적으로 결부시킬 수 있다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소에 대한 코딩 핵산의 소스는, 예를 들어, 코딩된 유전자 산물이 언급된 반응을 촉매할 수 있는 임의 종을 포함할 수 있다. 이러한 종은 원핵생물 및 진핵생물 유기체를 둘다 포함하며, 비-제한적인 예로는 고세균 및 유박테리아 등의 박테리아, 및 효모, 식물, 곤충, 동물 및 포유류, 예로 인간 등의 진핵생물 등이 있다. 일부 구현예에서, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소에 대한 코딩 핵산의 소스는 표 6, 8 및 11에 나타낸다. 일부 구현예에서, 트랜스아미나제 효소의 코딩 핵산의 소스는 표 6에 나타낸다. 일부 구현예에서, 트랜스아미나제 효소의 코딩 핵산의 소스는 아크로모박터 (Achromobacter), 액시드아미노코커스 (Acidaminococcus), 콜린셀라 (Collinsella), 펩토스트렙토코카세아에 (Peptostreptococcaceae), 파엔아르토박터 (Paenarthrobacter) 또는 롬보우스치아 (Romboustsia) 속으로부터 유래한다. 일부 구현예에서, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소에 대한 코딩 핵산의 소스는 에스케리키아 콜라이 (Escherichia coli), 에스케리키아 콜라이 str . K12, 에스케리키아 콜라이 C, 에스케리키아 콜라이 W, 슈도모나스 (Pseudomonas) sp, 슈도모나스 크나크무시 (Pseudomonas knackmussii), 슈도모나스 sp . Strain B13, 슈도모나스 푸티다 (Pseudomonas putida), 슈도모나스 플루오레센스 (Pseudomonas fluorescens), 슈도모나스 스투체리 (Pseudomonas stutzeri), 슈도모나스 멘도시나 (Pseudomonas mendocina), 로도슈도모나스 파울스트리스 (Rhodopseudomonas palustris), 마이코박테리움 투베르쿨로시스 (Mycobacterium tuberculosis), 비브리오 콜레라 (Vibrio cholera), 헬리코박터 필로리 (Heliobacter pylori), 클렙시엘라 뉴모니애 (Klebsiella pneumoniae), 세라티아 프로테아마쿨란스 (Serratia proteamaculans), 스트렙토마이세스 sp. 2065, 슈도모나스 에어루지노사 (Pseudomonas aeruginosa), 슈도모나스 에어루지노사 PAO1, 랄스토니아 유토파 (Ralstonia eutropha), 랄스토니아 유트로파 H16, 클로스트리듐 아세토부틸리컴 (Clostridium acetobutylicum), 유글레나 그라실리스 (Euglena gracilis), 트레포네마 덴티콜라 (Treponema denticola), 클로스트리듐 클루베리 (Clostridium kluyveri), 호모 사피엔스 (Homo sapiens), 라투스 노르베기쿠스 (Rattus norvegicus), 아시네토박터 sp. ADP1, 아시네토박터 sp. Strain M-1, 스트렙토마이세스 코엘리콜러 (Streptomyces coelicolor), 유박테리움 바르케리 (Eubacterium barkeri), 펩토스트렙토코커스 어사카롤리티쿠스 (Peptostreptococcus asaccharolyticus), 클로스트리듐 보툴리눔 (Clostridium botulinum), 클로스트리듐 보툴리눔 A3 str, 클로스트리듐 티로부티리컴 (Clostridium tyrobutyricum), 클로스트리듐 파스테리아눔 (Clostridium pasteurianum), 클로스트리듐 서모아세티쿰 (Clostridium thermoaceticum)(모렐라 서모아세티쿰 (Moorella thermoaceticum), 모렐라 서모아세티카 (Moorella thermoacetica), 아시네토박터 칼코아세티쿠스 (Acinetobacter calcoaceticus), 무스 무스쿨러스 (Mus musculus), 수스 스크로파 (Sus scrofa), 플라보박테리움 sp. (Flavobacterium sp), 아르트로박터 아우레센스 (Arthrobacter aurescens), 페니실리움 크리소게눔 (Penicillium chrysogenum), 아스퍼질러스 나이거 (Aspergillus niger), 아스퍼질러스 니둘란스 (Aspergillus nidulans), 바실러스 섭틸리스 (Bacillus subtilis), 사카로마이세스 세레비지애 (Saccharomyces cerevisiae), 자이모나스 모빌리스 (Zymomonas mobilis), 만헤미아 숙시니시프로두센스 (Mannheimia succiniciproducens), 클로스트리둠 롱달리이 (Clostridium ljungdahlii), 클로스트리듐 카르복시디보란스 (Clostridium carboxydivorans), 지오바실러스 스테아로서모필러스 (Geobacillus stearothermophilus), 아그로박테리움 투메팍시엔스 (Agrobacterium tumefaciens), 아크로모박터 크실르옥시단스 (Achromobacter xylosoxidans), 아크로모박터 데니트리피칸스 (Achromobacter denitrificans), 아라비돕시스 탈리아나 (Arabidopsis thaliana), 헤모필러스 인플루엔자 (Haemophilus influenzae), 아시다미노코커스 퍼멘트란스 (Acidaminococcus fermentans), 클로스트리듐 sp . M62/1, 푸조박테리움 뉴클레아툼 (Fusobacterium nucleatum), 보스 타우루스 (Bos taurus), 주글로에아 라미게라 (Zoogloea ramigera), 로도박터 스페로이데스 (Rhodobacter sphaeroides), 클로스트리듐 베이예린키이 (Clostridium beijerinckii), 메탈로스페라 세둘라 (Metallosphaera sedula), 서모안에어로박터 종 (Thermoanaerobacter species), 서모안에어로박터 브로키이 (Thermoanaerobacter brockii), 아시네토박터 베일리이 (Acinetobacter baylyi), 포르피로모나스 깅기발리스 (Porphyromonas gingivalis), 루코노스톡 메센테로이데스 (Leuconostoc mesenteroides), 설폴로부스 토코다이 (Sulfolobus tokodaii), 설폴로부스 토코다이 7, 설폴로부스 솔파타리쿠스 (Sulfolobus solfataricus), 설폴로부스 솔파타리쿠스 (Sulfolobus solfataricus), 설폴로부스 액시도칼다리우스 (Sulfolobus acidocaldarius), 살모넬라 티피쿠리움 (Salmonella typhimurium), 살모넬라 엔테리카 (Salmonella enterica), 서모토가 마리티마 (Thermotoga maritima), 할로박테리움 살리나룸 (Halobacterium salinarum), 바실러스 세레우스 (Bacillus cereus), 클로스트리듐 디피실 (Clostridium difficile), 알칼리필루스 메탈리레디게네스 (Alkaliphilus metalliredigenes), 서모안에어로박터 텡콩엔시스 (Thermoanaerobacter tengcongensis), 사카로마이세스 클루베리 (Saccharomyces kluyveri), 헬리코박터 필로리 (Helicobacter pylori), 코리네박테리움 글루타미쿰 (Corynebacterium glutamicum), 클로스트리듐 사카로퍼부틸아세토니쿰 (Clostridium saccharoperbutylacetonicum), 슈도모나스 클로로라피스 (Pseudomonas chlororaphis), 스트렙토마이세스 클라불리게루스 (Streptomyces clavuligerus), 캄필로박터 제주니 (Campylobacter jejuni), 서무스 서모필러스 (Thermus thermophilus), 펠로토카쿨럼 써모프로피오니쿰 (Pelotomaculum thermopropionicum), 박테로이데스 카필로수스 (Bacteroides capillosus), 안에어로트룬쿠스 콜리호미니스 (Anaerotruncus colihominis), 나트라안에어로비우스 서모필러스 (Natranaerobius thermophilius), 아르카에오글로부스 풀기두스 (Archaeoglobus fulgidus), 아르카에오글로부스 풀기두스 DSM 4304, 할로아르쿨라 마리스모르투이 (Haloarcula marismortui), 피로바쿨럼 에어로필럼 (Pyrobaculum aerophilum), 피로바쿨럼 에어로필럼 str . IM2, 니코티아나 타바쿰 (Nicotiana tabacum), 멘테 피페리타 (Menthe piperita), 피누스 타에다 (Pinus taeda), 호르데움 불가리 (Hordeum vulgare), 지아 메이스 (Zea mays), 로도코커스 오파쿠스 (Rhodococcus opacus), 쿠프리아비두스 네카토르 (Cupriavidus necator), 브라디리조비움 자포니컴 (Bradyrhizobium japonicum), 브라디리조비움 자포니쿰 USDA110, 아스카리우스 수움 (Ascarius suum), 부티레이트-생산 박테리움 L2-50, 바실러스 메가테리움 (Bacillus megaterium), 메타노코커스 마리팔루디스 (Methanococcus maripaludis), 메타노사르시나 마제이 (Methanosarcina mazei), 메타노사르시아 마제이 (Methanosarcina mazei), 메타노카르시나 바르케리 (Methanocarcina barkeri), 메타노칼도코커스 야나키이 (Methanocaldococcus jannaschii), 카에노랍디티스 엘레간스 (Caenorhabditis elegans), 라이슈마니아 마조르 (Leishmania major), 메틸로마이크로비윰 알칼리필룸 (Methylomicrobium alcaliphilum) 20Z, 클로모할로박터 살렉시겐스 (Chromohalobacter salexigens), 아르카에글루부스 풀기두스 (Archaeglubus fulgidus), 클라마이도모나스 라인하르드티이 (Chlamydomonas reinhardtii), 트리코모나스 바기날리스 (trichomonas vaginalis) G3, 트리파노소마 브루세이 (Trypanosoma brucei), 마이코플라나 라모스 (Mycoplana ramose), 미크로코커스 루테아스 (Micrococcus luteas), 아세토박터 파스테리안스 (Acetobacter pasteurians), 클루베로마이세스 락티스 (Kluyveromyces lactis), 메소리조비윰 로티 (Mesorhizobium loti), 락토코커스 락티스 (Lactococcus lactis), 라이시니바실러스 스페리쿠스 (Lysinibacillus sphaericus), 칸디다 보이디니이 (Candida boidinii), 칸디다 알비칸스 (Candida albicans) SC5314, 버크홀데리아 암비파리아 (Burkholderia ambifaria) AMMD, 아스카리스 수운 (Ascaris suun), 아시네토박터 바우마니이 (Acinetobacter baumanii), 아시네토박터 칼코아세티쿠스 (Acinetobacter calcoaceticus), 버크폴데리아 피마툼 (Burkholderia phymatum), 칸디다 알비칸스 (Candida albicans), 클로스트리듐 섭테르미날 (Clostridium subterminale), 쿠프리아비두스 타이와넨시스 (Cupriavidus taiwanensis), 플라보박테리움 루테센스 (Flavobacterium lutescens), 라첸시아 클루이베리 (Lachancea kluyveri), 락토바실러스 sp . 30a, 렙토스피라 인테로간스 (Leptospira interrogans), 모렐라 서모아세티카 (Moorella thermoacetica), 믹소코커스 크산투스 (Myxococcus xanthus), 니코티아나 글루티노사 (Nicotiana glutinosa), 노카르디아 오웬시스 (Nocardia iowensis)( sp . NRRL 5646), 슈도모나스 라이네케이 (Pseudomonas reinekei) MT1, 랄스토니아 유트로파 (Ralstonia eutropha) JMP134, 랄스토니아 메탈리두란스 (Ralstonia metallidurans), 로도코커스 조스티이 (Rhodococcus jostii), 시조사카로마이세스 폼베 (Schizosaccharomyces pombe), 셀레노모나스 루미난티눔 (Selenomonas ruminantium), 스트렙토마이세스 클라불리게누스 (Streptomyces clavuligenus), 신트로푸스 아시디트로피쿠스 (Syntrophus aciditrophicus), 비브리오 파라헤몰리티쿠스 (Vibrio parahaemolyticus), 비브리오 불니피쿠스 (Vibrio vulnificus)와 같은 종뿐 아니라 대응되는 유전자에 대한 소스 유기체로서 이용가능하거나 또는 본원에 기술된 기타 예시적인 종이다 (실시예 참조). 그러나, 미생물 게놈 395종 및 다양한 효모, 진균, 식물 및 포유류 게놈을 비롯해, 현재 550종 이상에서 이용가능한 전체 게놈 서열을 이용해 (NCBI와 같은 공공의 데이터베이스에서 이용가능한 데이터의 절반 이상을 이용해), 공지 유전자의 상동체, 오르소로그, 파라로그 및 비-오르소로거스 유전자 치환 등의, 관련있거나 또는 동떨어진 종들에서 하나 이상의 유전자에 대해 필요한 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 활성을 코딩하는 유전자의 동정, 및 유기체들 간의 유전자 변이의 상호 대체는 일반적이며, 당해 기술 분야에 잘 알려져 있다. 이에, E. coli와 같은 특정 유기체를 참조하여 본원에 기술된 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 달성할 수 있는 대사 변이는, 비슷한 원핵생물 및 진핵생물 유기체 등의 다른 미생물에도 쉽게 적용할 수 있다. 본원에 제공된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자라면 하나의 유기체에서 예시된 대사 변이가 다른 유기체에도 동일하게 적용될 수 있음을 알 것이다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로가 비-관련 종에 존재하는 경우와 같이 일부 경우에, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성은, 예를 들어, 언급된 반응을 대체하기 위해 유사하지만 동일하진 않은 대사 반응을 촉매하는 비-관련 종들로부터 유래한 파라로그 또는 파라로그들의 외인성 발현에 의해, 숙주 종에 부여할 수도 있다. 여러가지 유기체들 간에 대사 네트워크에 일부 차이가 존재하므로, 당해 기술 분야의 당업자라면, 서로 다른 유기체들 간의 실제 유전자 용법 (gene usage)이 다를 수 있음을 알 것이다. 그러나, 본원에 제공된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자라면, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 합성할 미생물 유기체를 대상 종에서 구축하기 위해, 본원에 예시된 내용에 대한 동계 (cognate) 대사 변이를 이용해 모든 미생물 유기체에 본 발명의 교시 내용 및 방법을 적용할 수 있음을, 알 것이다.
숙주 미생물 유기체는, 예를 들어, 박테리아, 효모, 진균 또는 발효 공정에 적용가능한 다양한 임의의 기타 미생물로부터 선택할 수 있으며, 이로부터 비-천연성 미생물 유기체를 구축할 수 있다. 박테리아의 예로는 에스케리키아 콜라이 (Escherichia coli), 클렙시엘라 옥시토카 (Klebsiella oxytoca), 안에어로비오스피릴룸 숙시니시프로두센스 (Anaerobiospirillum succiniciproducens), 액티노바실러스 숙시노게네스 (Actinobacillus succinogenes), 만하이미아 숙시니시프로두센스 (Mannheimia succiniciproducens), 리조비움 에틸리 (Rhizobium etli), 바실러스 섭틸리스 (Bacillus subtilis), 코리네박테리움 글루타미쿰 (Corynebacterium glutamicum), 클루코노박터 옥시단스 (Gluconobacter oxydans), 자이모모나스 모빌리스 (Zymomonas mobilis), 락토코커스 락티스 (Lactococcus lactis), 락토바실러스 플란타룸 (Lactobacillus plantarum), 스트렙토마이세스 코엘리콜러 (Streptomyces coelicolor), 클로스트리듐 아세토부틸리툼 (Clostridium acetobutylicum), 슈도모나스 플루오레센스 (Pseudomonas fluorescens) 및 슈도모나스 푸티다 (Pseudomonas putida)로부터 선택되는 종 등이 있다. 효모 또는 진균에 대한 예는, 사카로마이세스 세레비지애 (Saccharomyces cerevisiae), 시조사카로마이세스 폼베 (Schizosaccharomyces pombe), 클루이베로마이세스 락티스 (Kluyveromyces lactis), 클루이베로마이세스 마르시아누스 (Kluyveromyces marxianus), 아스퍼질러스 테레우스 (Aspergillus terreus), 아스퍼질러스 나이거 (Aspergillus niger), 피키아 파스토리스 (Pichia pastoris), 리조푸스 아리주스 (Rhizopus arrhizus), 리조부스 오리제 (Rhizobus oryzae) 등으로부터 선택되는 종을 포함한다. 예를 들어, E. coli는 유전자 조작에 적합한 잘 규명된 미생물 유기체이므로, 이 균주가 특히 유용한 숙주 유기체이다. 특히 유용한 숙주 유기체는 사카로마이세스 세레비지애 (Saccharomyces cerevisiae)와 같은 효모를 포함한다. 임의의 적절한 미생물 숙주 유기체를 이용해 원하는 생산물을 생산하도록 대사 및/또는 유전자 변형을 도입할 수 있는 것으로 이해된다.
비-천연성 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올-생산 숙주를 구축하는 방법 및 발현 수준을 검사하는 방법은, 예를 들어, 당해 기술 분야에 잘 알려진 재조합 및 검출 방법으로 수행할 수 있다. 이러한 방법은, 예를 들어, Sambrook et al., Molecular Cloning: A Laboratory Manual, Third Ed., Cold Spring Harbor Laboratory, New York (2001); 및 Ausubel et al., Current Protocols in Molecular Biology, John Wiley and Sons, Baltimore, MD (1999)에서 기술된 바와 같이 확인할 수 있다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해 경로에 참여하는 외인성 핵산 서열은, 비-제한적으로, 접합, 전기천공, 화학적 형질전환, 형질도입, 형질감염 및 초음파 형질전환 등의 당해 기술 분야에 잘 알려진 기법을 이용해, 숙주 세포에 안정적으로 또는 일시적으로 도입할 수 있다. E. coli 또는 기타 원핵생물 세포에서 외인성 발현을 위해, 진핵생물 핵산의 유전자 또는 cDNA 내 일부 핵산 서열은, 필요에 따라, 원핵생물 숙주 세포에 형질전환하기 전에 제거될 수 있는, N-말단 미토콘드리아 또는 그외 타겟팅 신호와 같은 타겟팅 신호를 코딩할 수 있다. 예를 들어, 미토콘드리아 리더 서열의 제거는 E. coli에서 발현 증가를 유도한다 (Hoffmeister et al., J. Biol . Chem. 280:4329-4338 (2005)). 효모 또는 기타 진핵생물 세포에서 외인성 발현을 위해, 유전자는 리더 서열의 부가 없이 세포질에서 발현시키거나, 또는 숙주 세포에 적합한 미토콘드리아 타겟팅 또는 방출 신호와 같은 적절한 타겟팅 서열을 부가함으로써, 미토콘드리아 또는 그외 소기관으로 타겟팅하거나 또는 분비하도록 타겟팅할 수 있다. 따라서, 타겟팅 서열을 제거 또는 포함시키 위한 핵산 서열에 대한 적절한 변형이 원하는 특성을 부여하기 위해 외인성 핵산 서열에 포함될 수 있는 것으로 이해된다. 또한, 유전자는 단백질의 최적화된 발현을 달성하기 위해 당해 기술 분야에 잘 알려진 기법으로 코돈 최적화를 이행할 수 있다.
발현 벡터 또는 벡터는, 본원에 예시된 바와 같이, 숙주 유기체에서 발현 조절 서열 기능에 작동가능하게 연결된, 하나 이상의 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 코딩 핵산을 포함하도록 구축할 수 있다. 미생물 숙주 유기체에서 이용하기 위해 적용가능한 발현 벡터로는, 예를 들어, 벡터 및 숙주 염색체의 안정적인 삽입을 위해 작동가능한 선택 서열 또는 마커를 포함한, 플라스미드, 파지 벡터, 바이러스 벡터, 에피솜 및 인공 염색체 등이 있다. 또한, 발현 벡터는 하나 이상의 선별가능한 마커 유전자와 적절한 발현 조절 서열을 포함할 수 있다. 또한, 예를 들어, 항생제 또는 독소에 대해 내성을 제공하거나, 영양요구성 결핍을 보완하거나 또는 배양 배지에 없는 중요한 영양분을 공급하는, 선별가능한 마커 유전자도 포함할 수 있다. 발현 조절 서열은 당해 기술 분야에 잘 공지되어 있는 구성적 프로모터, 유도성 프로모터, 전사 인핸서, 전사 종결인자 등을 포함할 수 있다. 2 이상의 외인성 코딩 핵산을 공동-발현시킬 경우, 이들 2종의 핵산은, 예를 들어, 단일한 발현 벡터에 또는 분리된 발현 벡터들에 삽입될 수 있다. 하나의 벡터에서 발현하는 경우, 하나의 공통적인 발현 조절 서열을 코딩 핵산에 작동가능하게 연결하거나 또는 유도 프로모터 하나 및 구성적 프로모터 하나 등의 서로 다른 발현 조절 서열을 작동가능하게 연결할 수 있다. 대사 또는 합성 경로에 참여하는 외인성 핵산 서열의 형질전환은 당해 기술 분야에 잘 알려진 방법으로 검증할 수 있다. 이러한 방법으로는, 예를 들어, mRNA의 노던 블롯 또는 중합효소 연쇄 반응 (PCR) 증폭과 같은 핵산 분석, 또는 유전자 산물 발현에 대한 면역블롯팅, 또는 도입된 핵산 서열 또는 이의 대응되는 유전자 산물의 발현을 검사하기 위한 그외 적절한 분석 방법 등이 있다. 당해 기술 분야의 당업자라면, 외인성 핵산이 원하는 생산물을 생산하기 위해 충분한 양으로 발현되는 것으로 이해하며, 또한 당해 기술 분야에 잘 알려진 방법 및 본원에 기술된 방법을 이용해 충분한 발현을 수득하도록 발현 수준을 최적화할 수 있음을 알 것이다.
일부 구현예는 아디페이트, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올와 같은 원하는 중간산물 또는 생산물을 생산하는 방법이다. 예를 들어, 아디페이트 생산 방법은 아디페이트 경로를 가진 비-천연성 미생물 유기체를 배양하는 것을 수반할 수 있으며, 그 경로는 아디페이트를 생산하기 위해 충분한 기간 동안 조건 하에 아디페이트를 생산하기 위해 충분한 양으로 발현되는 아디페이트 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하며, 아디페이트 경로는 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제, 3-하이드록시아실-CoA 데하이드로게나제, 3-하이드록시아디필-CoA 데하이드라타제, 아디페이트 세미알데하이드리덕타제, 및 아디필-CoA 신테타제 또는 포스포트랜스아디필라제/아디페이트 키나제 또는 아디필-CoA: 아세틸-CoA 트랜스퍼라제 또는 아디필-CoA 하이드롤라제를 포함한다. 아울러, 아디페이트 생산 방법은 아디페이트 경로를 가진 비-천연성 미생물 유기체를 배양하는 것을 수반할 수 있으며, 경로는 아디페이트를 생산하기 위해 충분한 기간 동안 조건 하에 아디페이트를 생산하기 위해 충분한 양으로 발현되는 아디페이트 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하며, 아디페이트 경로는 숙시닐-CoA: 아세틸-CoA 아실 트랜스퍼라제, 3-옥소아디필-CoA 트랜스퍼라제, 3-옥소아디페이트 리덕타제, 3-하이드록시아디페이트 데하이드라타제, 및 2-에노에이트 리덕타제를 포함한다.
나아가, 6-아미노카프로익산 생산 방법은 6-아미노카프로익산 경로를 가진 비-천연성 미생물 유기체를 배양하는 것을 수반할 수 있으며, 그 경로는 6-아미노카프로익산을 생산하기 위해 충분한 기간 동안 조건 하에 6-아미노카프로익산을 생산하기 위해 충분한 양으로 발현되는 6-아미노카프로익산 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하며, 6-아미노카프로익산 경로는 CoA-의존적인 트랜스-에노일-CoA 리덕타제 및 트랜스아미나제 또는 6-아미노카프로에이트 데하이드로게나제를 포함한다. 아울러, 카프로락탐 생산 방법은 카프로락탐 경로를 가진 비-천연성 미생물 유기체를 배양하는 것을 수반할 수 있으며, 경로는 카프로락탐을 생산하기 위해 충분한 기간 동안 조건 하에 카프로락탐을 생산할 만큼 충분한 양으로 발현되는 카프로락탐 경로 효소를 코딩하는 하나 이상의 외인성 핵산을 포함하며, 카프로락탐 경로는 CoA-의존적인 알데하이드 데하이드로게나제, 트랜스아미나제 또는 6-아미노카프로에이트 데하이드로게나제, 및 아미도하이드롤라제를 포함한다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생산에 대한 적절한 정제 및/또는 이를 검사하기 위한 분석은, 잘 알려진 방법으로 수행할 수 있다. 검사할 각 조작된 균주를 트리플리케이트 (triplicate) 배양과 같은 적절한 리플리케이트로 배양할 수 있다. 예를 들어, 조작된 생산 숙주에서 생산물 및 부산물의 형성을 모니터링할 수 있다. 최종 생산물 및 중간산물, 및 기타 유기 화합물은 HPLC (고 성능 액체 크로마토그래피), GC-MS (가스 크로마토그래피-질량 분광분석) 및 LC-MS (액체 크로마토그래피-질량 분광분석) 또는 당해 기술 분야에서 잘 알려진 통상적인 공정을 이용한 그외 적합한 분석 방법 등의 방법으로 분석할 수 있다. 발효 브로스로의 생산물 분비를 또한 배양 상층액을 이용해 검사할 수 있다. 부산물 및 잔류 글루코스는, 예를 들어, 글루코스 및 알코올에 대한 굴절율 검출기, 및 유기산에 대한 UV 검출기를 이용해, HPLC에 의해 또는 당해 기술 분야에 잘 알려진 그외 적합한 분석 및 검출 방법으로 정량할 수 있다 (Lin et al., Biotechnol . Bioeng. 90:775-779 (2005)). 또한, 외인성 DNA 서열로부터 유래하는 개별 효소 활성은 당해 기술 분야에 잘 알려진 방법을 이용해 분석할 수 있다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올은 당해 기술 분야에 잘 알려진 다양한 방법을 이용해 배양물 내 다른 성분들로부터 분리할 수 있다. 이러한 분리 방법으로는, 예를 들어, 추출 공정뿐 아니라 연속적인 액체-액체 추출, 투석증발 (pervaporation), 막 여과, 막 분리, 역 삼투압, 전기 투석, 증류, 결정화, 원심분리, 추출 여과 (extractive filtration), 이온 교환 크로마토그래피, 크기 배제 크로마토그래피, 흡착 크로마토그래피 및 한외여과를 포함한 방법 등이 있다. 전술한 방법들 모두 당해 기술 분야에 잘 공지되어 있다.
본원에 기술된 임의의 비-천연성 미생물 유기체를 배양하여 생합성 생산물을 생산 및/또는 분비시킬 수 있다. 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 균주는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생합성하기 위해 배양할 수 있다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해, 재조합 균주를 탄소원 및 기타 필수 영양분이 첨가된 배지에서 배양한다. 전체 공정 비용을 줄이기 위해 발효 장치를 혐기성 상태로 유지시키는 것이 종종 바람직하며, 매우 바람직할 수 있다. 이러한 조건은, 예를 들어, 배지를 질소로 퍼징한 다음 격막 (septum) 및 크림프-캡 (crimp-cap)으로 플라스크를 밀봉함으로써, 달성할 수 있다. 혐기성 상태에서는 증식이 관찰되지 않는 균주의 경우, 격막에 제한적인 호기를 위해 작은 구멍을 뚫어 미세호기 (microaerobic) 또는 실질적으로 혐기 조건을 적용할 수 있다. 예시적인 혐기 조건들은 기존에 기술되어 있으며, 당해 기술 분야에 잘 알려져 있다. 예시적인 호기 및 혐기 조건들은 2011년 3월 24일에 출원된 미국 특허 7,947,483에 기술되어 있다. 발효는 본원에 기술된 바와 같이 배치, 피드-배치 또는 연속적인 방식으로 수행할 수 있다.
배지의 pH는, 필요에 따라 배양 배지를 원하는 pH에서 유지시키기 위해, NaOH와 같은 염기 또는 기타 염기 또는 산을 첨가함으로써, 원하는 pH, 특히 중성 pH, 예를 들어 약 pH 7에서 유지할 수 있다. 증식율은 분광광도계 (600 nm)를 사용해 광학 밀도를 측정함으로써 확인할 수 있으며, 글루코스 흡수율 (glucose uptake rate)은 시간 경과에 따른 탄소원 고갈을 모니터링함으로써 결정할 수 있다.
증식 배지는, 예를 들어, 비-천연성 미생물에 탄소원을 공급할 수 있는, 임의의 탄수화물 소스를 포함할 수 있다. 이러한 소스로는, 예를 들어, 글루코스, 자일로스, 아라비노스, 갈락토스, 만노스, 프럭토스, 슈크로스 및 전분과 같은 당 등이 있다. 그외 탄수화물 소스로는 예를 들어 재생가능한 공급원료 (renewable feedstock) 및 바이오매스 (biomass) 등이 있다. 본 방법에서 공급원료로서 이용가능한 바이오매스 타입의 예로는 셀룰로스 바이오매스, 헤미셀룰로스 바이오매스 및 리그닌 공급원료 또는 공급원료의 일부 등이 있다. 이러한 바이오매스 공급원료는, 예를 들어, 글루코스, 자일로스, 아라비노스, 갈락토스, 만노스, 프럭토스 및 전분과 같은 탄소원으로서 유용한 탄수화물 물질을 포함한다. 본원에 제공된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자라면, 상기에 예시된 것 이외의 다른 재생가능한 공급원료 및 바이오매스 역시 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해 미생물 유기체를 배양하는데 이용할 수 있음을, 알 것이다.
상기에 예시된 것과 같은 재생가능한 공급원료 외에도, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 레불린산 미생물 유기체는, 또한 이의 탄소원으로서 합성가스 (syngas)에서 증식하도록 변형될 수 있다. 이러한 구체적인 구현예에서, 하나 이상의 단백질 또는 효소를, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 유기체에서 발현시켜, 합성가스 또는 기타 기체성 탄소원을 이용하는 대사 경로를 제공한다.
합성가스 또는 발생로 가스 (producer gas)로도 알려진 합성 가스 (synthesis gas)는, 석탄 및 농업 작물 및 잔재 (residues) 등의 바이오매스 물질과 같은 탄소질 물질의 주요 기화 산물이다. 합성가스는 주로 H2 및 CO로 구성된 혼합물이며, 비-제한적인 예로, 석탄, 석탄 오일, 천연 가스, 바이오매스 및 폐 유기물 등의 임의의 유기 공급원료의 기화로부터 수득할 수 있다. 기화는 일반적으로 높은 연료/산소 비율 하에 수행된다. 합성 가스는 주로 H2 및 CO이지만, CO2 및 기타 기체도 소량 포함할 수 있다. 따라서, 합성 가스는 CO, 추가적으로 CO2 등의 가스성 탄소에 대한 비용 효율적인 소스를 제공해준다.
우드-룬달 (Wood-Ljungdahl) 경로는 CO와 H2를 아세틸-CoA와 아세테이트 등의 기타 생산물로 변환하는 반응을 촉매한다. 또한, CO 및 합성 가스를 이용할 수 있는 유기체는, 일반적으로, 우드-룬달 경로에 포함된 효소 및 변환으로 된 동일한 기본 세트를 통해, CO2 및 CO2/H2 혼합물을 이용할 수 있는 능력을 가지고 있다. 또한, 동일 유기체가 CO를 이용할 수 있고 동일한 경로가 관여한다는 것이 밝혀지기 전에는, 오랫동안 미생물이 이산화탄소를 H2-의존적인 방식으로 아세테이트로 변환하는 것으로 인식하였다. 수소가 존재하여 필요한 환원 당량을 제공하는 한, 여러 아세토젠 (acetogen)들이 이산화탄소의 존재 하에 증식해 아세테이트와 같은 화합물을 생산하는 것으로 확인된 바 있다 (예, Drake, Acetogenesis, pp. 3-60 Chapman and Hall, New York, (1994) 참조). 이를 아래 등식으로 요약할 수 있다:
2CO2 + 4H2 + nADP + nPi → CH3COOH + 2H2O + nATP
그래서, 우르-룬달 경로를 가진 비-천연성 미생물은 CO2 및 H2 혼합물을 이용할 수 있을 뿐만 아니라 아세틸-CoA 및 기타 원하는 생산물을 생산할 수 있다.
우드-룬달 경로는 당해 기술 분야에 잘 알려져 있으며, 2가지 분지, 즉 (1) 메틸 분지와 (2) 카보닐 분지로 나눌 수 있는 12가지 반응으로 구성된다. 메틸 분지는 합성 가스를 메틸-테트라하이드로폴레이트(메틸-THF)로 변환하고, 카보닐 분지는 메틸-THF를 아세틸-CoA로 변환한다. 메틸 분지에서의 반응들은 다음과 같은 효소에 의해 순차적으로 촉매된다: 페레독신옥시도리덕타제, 포르메이트 데하이드로게나제, 포르밀테트라하이드로폴레이트 신테타제, 메테닐테트라하이드로폴레이트 사이클로데하이드라타제, 메틸렌테트라하이드로폴레이트 데하이드로게나제 및 메틸렌테트라하이드로폴레이트 리덕타제. 카르보닐 분지에서의 반응들은 다음과 같은 효소 또는 단백질에 의해 순차적으로 촉매되며: 코발아미드 코리노이드/철-황 단백질, 메틸트랜스퍼라제, 일산화탄소 데하이드로게나제, 아세틸-CoA 신타제, 아세틸-CoA 신타제 다이설파이드 리덕타제 및 하이드로게나제, 이들 효소는 또한 메틸테트라하이드로폴레이트:코리노이드 단백질 메틸트랜스퍼라제 (예, AcsE), 코리노이드 철-황 단백질, 니켈-단백질 어셈블리 단백질 (예, AcsF), 페레독신, 아세틸-CoA 신타제, 일산화탄소 데하이드로게나제 및 니켈-단백질 어셈블리 단백질 (예, CooC)로도 언급될 수 있다. AA 경로를 구축하기에 충분한 개수의 코딩 핵산을 도입하는 것에 대한 본원에 제공된 교시 내용 및 지침에 따라, 당해 기술 분야의 당업자라면, 적어도 숙주 유기체에 존재하지 않는 우드-룬달 효소 또는 단백질을 코딩하는 핵산을 도입하는 것과 관련하여, 동일한 조작 설계를 수행할 수 있음을 이해할 것이다. 즉, 변형된 유기체에 우드-룬달의 전체 경로가 포함되도록 하나 이상의 코딩 핵산을 본 발명의 미생물 유기체에 도입함으로써, 합성가스의 이용 능력을 부여하게 될 것이다.
또한, 일산화탄소 데하이드로게나제 및/또는 하이드로게나제와 커플링된 환원성 (역) 트리카르복시산 사이클을 CO, CO2 및/또는 H2를 아세틸-CoA 및 아세테이트와 같은 기타 생산물로 변환하는데, 이용할 수 있다. 환원성 TCA 경로를 통해 탄소를 고정할 수 있는 유기체는 하나 이상의 다음과 같은 효소를 이용할 수 있다: ATP 사이트레이트-리아제, 사이트레이트 리아제, 아코니타제, 이소사이트레이트 데하이드로게나제, α-케토글루타레이트:페레독신옥시도리덕타제, 숙시닐-CoA 신테타제, 숙시닐-CoA 트랜스퍼라제, 푸마레이트 리덕타제, 푸마라제, 말레이트 데하이드로게나제, NAD(P)H:페레독신옥시도리덕타제, 일산화탄소 데하이드로게나제 및 하이드로게나제. 구체적으로, 일산화탄소 데하이드로게나제 및 하이드로게나제에 의해 CO 및/또는 H2로부터 추출된 환원 당량을 이용하여, 환원성 TCA 사이클을 통해 CO2를 아세틸-CoA 또는 아세테이트에 고정한다. 아세테이트는 아세틸-CoA 트랜스퍼라제, 아세테이트 키나제/포스포트랜스아세틸라제 및 아세틸-CoA 신테타제와 같은 효소에 의해 아세틸-CoA로 변환할 수 있다. 아세틸-CoA는, 피루베이트:페레독신 옥시도리덕타제 및 글루코스 신생 합성 (gluconeogenesis) 효소에 의해 p-톨루에이트, 테레파탈레이트, 또는 (2-하이드록시-3-메틸-4-옥소부톡시) 포스포네이트 전구체, 글리세르알데하이드-3-포스페이트, 포스포에놀피루베이트 및 피루베이트로 변환할 수 있다. p-톨루에이트, 테레프탈레이트 또는 (2-하이드록시-3-메틸-4-옥소부톡시) 포스포네이트 경로를 구축하도록 충분한 개수의 코딩 핵산을 도입하는 것에 대한 본원에 제시된 교시된 내용 및 지침에 따라, 당해 기술 분야의 당업자라면, 숙주 유기체에 없는 환원성 TCA 경로 효소 또는 단백질을 코딩하는 핵산을 적어도 도입하는 것에 대하여, 동일한 조작 설계를 수행할 수 있음을 알 것이다. 따라서, 변형된 유기체가 환원성 TCA 경로 전체를 포함하도록 본 발명의 미생물 유기체에 하나 이상의 코딩 핵산이 도입되면, 합성가스 활용 능력이 부여될 것이다.
본원에 제시된 교시 내용 및 지침을 감안해, 당해 기술 분야의 당업자라면, 탄수화물과 같은 탄소원에서 배양시 생합성 화합물을 분비하는 비-천연성 미생물 유기체를 생산할 수 있음을 알 것이다. 이러한 화합물로는, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 및 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로에서 임의의 중간 대사산물을 포함한다. 예를 들면, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로 중 일부 또는 전체를 포함하는 등의, 요망되는 화합물 또는 중간산물의 생합성을 달성하는데 필요한 효소 활성 중 하나 이상을 조작하는 것이 필요한 전부이다. 이에, 일부 구현예는, 탄수화물에서 배양시, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산 및/또는 분비하고, 탄수화물에서 배양시 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생합성 경로에서 확인되는 임의의 중간 대사산물을 생산 및/또는 분비하는, 비-천연성 미생물 유기체를 제공한다. 예를 들어, 아디페이트 생산 미생물 유기체는 중간산물, 예를 들어, 필요에 따라, 3-옥소아디필-CoA, 3-하이드록시아디필-CoA, 5-카르복시-2-펜테노일-CoA 또는 아디필-CoA (도 1 참조)로부터의 합성을 개시할 수 있다. 아울러, 아디페이트 생산 미생물 유기체는 중간산물, 예를 들어, 3-옥소아디필-CoA, 3-옥소아디페이트, 3-하이드록시아디페이트 또는 헥사-2-엔다이오에이트로부터 합성을 개시할 수 있다. 6-아미노카프로익산 생산 미생물 유기체는 중간산물, 예를 들어, 아디페이트 세미알데하이드로부터 합성을 개시할 수 있다. 카프로락탐 생산 미생물 유기체는 중간산물, 필요에 따라, 예를 들어, 아디페이트 세미알데하이드 또는 6-아미노카프로익산 (도 1 참조)으로부터 합성을 개시할 수 있다.
표 4. 아디필 - CoA에 대한 알데하이드 데하이드로게나제의 활성
번호 유기체 등재 번호/서열번호. 활성 - NADH 활성 - NADPH
1 클로스트리듐 클루이베리 DSM555 서열번호: 141 - +
2 포르피로모나스 깅기발리스 W83 서열번호: 142 + -
3 클로스트리듐 디피실 630 서열번호: 143 - +
4 클루이베라 인테스티니 WP_071196317.1 + -
5 클로스트리듐 네오나탈 WP_058295546.1 - -
6 에어로코커스 sp. HMSC062B07 WP_070558456.1 - -
7 펩토스트렙토코카시이 박테리움 오랄 WP_021676458.1 + -
8 다사니아 마리나 WP_026244399.1 - -
9 포스피로모나다시이 박테리움 COT-184 WP_036830068.1 - -
10 클로스트리듐 룬덴스 WP_027623222.1 - -
11 안에어로콜룸나 제준시스 WP_073279774.1 + -
12 클로스트리듐 호모프로피오니컴 WP_052222510.1 - -
13 지오스포로박터 페리레두센스 WP_069981616.1 - -
14 리스테리아 이바노비이 WP_038407128.1 - -
15 바실러스 솔리 WP_066062455.1 + -
16 엔테로코커스 리보룸 WP_069697141.1 - -
17 데스누에시엘라 마실리엔시스 WP_055665162.1 + -
18 박테로이달 박테리움 KA00251 WP_066041885.1 - -
19 칼단에어로비우스 폴리사카롤리티쿠스 WP_026487268.1 + -
20 클로스트리듐 sp. ASF356 WP_004036483.1 - -
21 클로스트리디알 박테리움 DRI-13 WP_034420506.1 - -
22 푸조박테리움 울세란스 ATCC 49185 WP_005981617.1 - -
23 안에어로콜루마 제준시스 WP_073279351.1 - -
24 셀룰로실리티쿰 sp. I15G10I2 WP_070001026.1 + -
25 지오스포로박터 페리레두센스 WP_083273866.1 + -
26 펠로시누스 sp. UFO1 WP_038668911.1 - -
27 바실러스 코를렌시스 WP_084362095.1 + -
28 액시드아미노코커스 마실리엔시스 WP_075579339.1 + -
29 유박테리움 sp. SB2 WP_050640767.1 - -
30 에르위니아 텔레오그릴리 WP_058911295.1 - -
31 라크노스피라시이 박테리움 32 WP_016223553.1 + -
32 유박테리움 플렉시카우다툼 WP_004061597.1 + -
33 클로스트리듐 sp. KNHs205 WP_033166114.1 + -
34 부티리시모나스 비로사 WP_027200274.1 - -
35 말로노모나스 루브라 WP_072908980.1 - -
36 로빈소니엘라 페오리엔시스 WP_044292972.1 + -
37 클로스트리듐 타에니오스포룸 WP_069679818.1 - -
38 칼디트릭스 아비시 WP_006928331.1 + -
39 피스시코커스 인테스티날리스 WP_084343789.1 - -
40 스포로무사 스페어로이데스 WP_075753933.1 + -
41 바실러스 sp. FJAT-25547 WP_057762439.1 + -
42 도레아 sp. D27 WP_049729435.1 + -
43 오실리박터 sp. 13 WP_081646270.1 - -
44 엔테로코커스 포에니쿨리콜라 (Cola) WP_010767571.1 + -
45 블라우티아 쉰키이 WP_044941637.1 + -
46 셔틀워티아 사텔레스 DSM 14600 WP_006905683.1 - -
47 클로스트리듐 인테스티날 WP_073018444.1 + -
48 마실리오클로스트리듐 콜라이 WP_069989048.1 - -
49 클로아시바실러스 포르코룸 WP_066745012.1 - -
50 클로스트리듐 sp. CL-2 WP_032120205.1 - -
51 클로스트리디아 박테리움 UC5.1-1D10 WP_054330586.1 - -
52 메틸로박테리움 sp. CCH5-D2 WP_082772960.1 - -
53 스포로사르시나 글로비스포라 WP_053435653.1 + +
54 라크노스피라시이 박테리움 AC3007 WP_031546337.1 - -
55 라크노스피라시이 박테리움 28-4 WP_016290199.1 - -
56 엔테로코커스 아비움 WP_034875865.1 - -
57 데설포토마쿨럼 서모시스테르넘 WP_027356260.1 - -
58 로도박터 에스투아리 WP_076486054.1 + -
59 클로스트리듐 그란티이 WP_073337420.1 + -
60 콜린셀라 sp. GD7 WP_066830323.1 + -
61 클로스트리듐 에스테르테티컴 WP_071611886.1 - -
62 박테리움 MS4 WP_038325413.1 - -
63 클로스트리듐 글리시리지닐리티컴 WP_009268007.1 + -
64 바실러스 호리코시이 WP_082892049.1 - -
65 서민콜라 페리아세티카 WP_052218568.1 + -
66 라크노스피라시이 박테리움 AC3007 WP_035653923.1 + -
67 유박테리움 sp. 14-2 WP_016216571.1 + -
68 칸디다투스 마리스피로케타 어소시아타 WP_069895590.1 - -
69 클로스트리듐 드라케이 WP_032078293.1 - -
70 할란에어로비움 쿠시네리 WP_076543773.1 - -
71 클로스트리듐 팔락스 WP_072896506.1 - -
72 플라보니프락토르 플라우티이 WP_009261118.1 - -
73 클로스트리듐 프로피오니컴 WP_066049640.1 - -
74 안에어로살리박터 마실리엔시스 WP_042682918.1 + -
75 클로스트리듐 인돌리스 DSM 755 WP_024295710.1 + -
76 가보니박터 마실리엔시스 WP_059027034.1 - -
77 카타박터 홍콩엔시스 WP_046444791.1 + +
78 데설피티박터 알칼리톨레란스 WP_028307735.1 - -
79 포르피로모나스 레비이 WP_018357742.1 - -
80 바실러스 서모톨레란스 WP_039235348.1 + -
81 데설피티박터 알칼리톨레란스 WP_028307055.1 - -
82 그라실리바실러스 케켄시스 WP_073203236.1 + +
83 락토니팍터 롱고비포르미스 WP_072848455.1 - -
84 프로피오니스포라 sp. 2/2-37 WP_054258533.1 + -
85 에리시펠로트릭스 라바 WP_067632640.1 - -
86 클로스트리듐 카우오에이 WP_021875658.1 + -
87 서모안에어로박테리움 아오테아로엔스 WP_014757178.1 + -
88 루미노코커스 sp. AT10 WP_059066688.1 + -
89 포르피로모나스 sp. HMSC077F02 WP_070707924.1 - -
90 아세토박테리움 데할로게난스 WP_026396046.1 + -
91 스피로케타 알칼리카 WP_018526526.1 + -
92 알리스티페스 sp. ZOR0009 WP_047449305.1 - -
93 클로스트리디이살리박터 파우시보란스 WP_026895448.1 - -
94 클로스트리듐 카미니서말 DSM 15212 WP_073149471.1 + +
95 칼단에어로비우스 피젠시스 WP_073341480.1 + -
96 클로스트리듐 클루이베리 WP_073539833.1 - -
97 펠로시누스 퍼멘탄스 WP_007958399.1 + -
98 할란에어로비움 사카롤리티컴 아종 사카롤리티컴 DSM 6643 WP_005487288.1 - -
99 안에어로아르쿠스 버르키넨시스 DSM 6283 WP_018702299.1 - -
100 블라우티아 웩슬레라 WP_026648408.1 + -
101 파에니바실러스 sp. OSY-SE WP_019424162.1 + -
102 브라키스피라 인터메디아 PWSA WP_014488056.1 - -
103 스피로케테스 박테리움 GWC2_52_13 OHD32879.1 + -
104 서모안에어로박테랄리스 박테리움 50_218 KUK31085.1 - -
105 코할에시박터 마리스플라비 WP_090072157.1 - -
106 그라실리바실러스 우레일리티쿠스 WP_089739945.1 - -
107 롬바우치아 리투세부렌시스 DSM WP_092724914.1 + -
108 비-배양 클로스트리듐 sp. SCJ29526.1 - -
109 클로스트리듐 sp. CAG:448 CDC62685.1 + -
110 클로스트리듐 울투넨스 Esp CCQ95129.1 - -
111 예르시니아 베르코비에리이 ATCC 43970 WP_005274635.1 + -
112 프로테오카텔라 스페니치 WP_028829945.1 + -
113 클로스트리듐 sp. MSTE9 WP_009063988.1 - -
114 스피로케타 아프리카나 WP_014454236.1 - -
115 델타프로테오박테리아 박테리움 RIFCSPHIGHO2_02_FULL_40_11 OGQ13386.1 - -
116 클로스트리디알 박테리움 PH28_bin88 KKM11466.1 - -
117 펠로시누스 프로피오니쿠스 DSM WP_090932308.1 + -
118 프로피오니스포라 비브리오이데스 WP_091747803.1 - -
119 나트로닌콜라 페리레두센스 WP_090549432.1 - -
120 비-배양 루미노코커스 sp. WP_112331601.1 - -
121 피르미쿠테스 박테리움 CAG:41 WP_022229858.1 - -
122 타네렐라 sp. 경구 ETK11816.1 - -
123 클로스트리듐 sp. DL-VIII WP_009171375.1 - -
124 데설포불부스 자포니쿠스 WP_028581706.1 - -
125 베일로넬라 sp. 오랄 WP_009353657.1 - -
126 바실러스 셀레니티레두센스 WP_013174003.1 - -
127 델타프로테오박테리아 박테리움 GWA2_38_16 OGP02283.1 - -
128 클로스트리디아시이 박테리움 BRH KJS20094.1 - -
129 클로스트리듐 카다베리스 WP_035770223.1 - -
130 비브리오 행저우엔시스 WP_103880502.1 - -
131 할란에어로비움 콩올렌스 SDI24694.1 - -
132 비-배양 유박테리움 sp. SCH28733.1 - -
133 오실리박터 sp. CAG:241 CDB26907.1 - -
134 클로스트리듐 sp. KLE ERI68946.1 + -
135 칼달칼리바실러스 서마룸 TA2.A1 WP_007505383.1 + -
136 부드비시아 아큐아티카 WP_029095874.1 - -
137 칼달칼리바실러스 서마룸 TA2.A1 WP_007505383.1 + -
138 로도스피릴륨 루브룸 ATCC 11170 WP_011388669.1 - -
139 박테로이데테스 박테리움 GWE2_39_28 OFX78235.1 - -
140 데설포포로시누스 sp. BICA1 KJS46946.1 - -
141 클로스트리듐 울리기노섬 WP_090094411.1 - -
142 슈도부티리비브리오 sp. ACV-2 WP_090301343.1 - -
143 스포롤리투스 서모필러스 DSM WP_093690468.1 - -
144 유박테리아시이 박테리움 CHKCI004 WP_087275421.1 - -
145 블라우티아 sp. CAG:257 CDA04862.1 + -
146 리스테리아 마르티이 FSL EFR88049.1 + -
147 데설포포로시누스 sp. OT WP_009624792.1 - -
148 클로스트리듐 메톡시벤조보란스 WP_024346771.1 + -
149 바실러스 sp. m3-13 WP_010197697.1 + -
150 박테리움 CG2_30_54_10 OIP28307.1 + -
151 할란에어로비움 sp. 4-GBenrich ODS50009.1 - -
152 칸디다투스 이지마플라스마 sp. KFZ26741.1 + +
153 데설포토마쿨럼 구토이데움 WP_092244224.1 - -
154 바실러스 달리엔시스 WP_090843272.1 - -
155 스포로무사 액시도보란스 WP_093796665.1 - -
156 클로스트리듐 sp. C105KSO15 WP_089994985.1 - -
157 피르미쿠테스 박테리움 CAG:41 CCZ36420.1 + -
158 푸조박테리움 뉴클레아툼 아종 WP_085057258.1 + -
159 서모안에어로박테리움 크실라놀리티컴 LX-11 WP_013788835.1 + -
160 엔테로코커스 팔렌스 WP_010758150.1 - -
161 포르피로모나스 우에노니스 WP_007364879.1 - -
162 테네리쿠테스 박테리움 GWD2_38_27 OHE32257.1 - -
163 클로스트리디아 박테리움 BRH_c25 KUO67763.1 - -
164 리스테리아 모노사이토게네스 WP_012951491.1 + -
165 클로스트리듐 라발렌스 WP_092361844.1 + -
166 아세트안에어로박테리움 일롱가텀 WP_092640331.1 + -
167 알칼리필루스 펩티디퍼멘탄스 DSM WP_091539210.1 + -
168 클로스트리듐 sp. C105KSO15 WP_089983798.1 - -
169 루미노코커스 sp. CAG:17 CCY97458.1 - -
170 클로스트리듐 힐레모니이 DSM 15053 EEG72288.1 - -
171 아세토네마 롱검 DSM 6540 EGO64744.1 - -
172 브라키스피라 이노센스 WP_020003501.1 - -
173 클로스트리듐 사카로부틸리컴 WP_022747467.1 - -
174 테네리쿠테스 박테리움 GWD2_38_27 OHE28831.1 - -
175 바실러스 sp. FJAT-25547 WP_053476394.1 - -
176 클로스트리듐 포풀레티 WP_092561044.1 + -
177 나트로닌콜라 펩티디보란스 WP_090442614.1 - -
178 메가스페라 파우시보란스 WP_091652222.1 - -
179 안에어로비움 아세트에틸리컴 WP_091232027.1 - -
180 유박테리움 리모섬 ALU13318.1 - -
181 포르피로모나스 sp. CAG:1061 CCY08492.1 - -
182 클로스트리듐 베이에링키이 strain NRRL B593 AAD31841.1 - -
183 클로스트리듐 스티클란디이 DSM 519 WP_013360893.1 - -
184 바실러스 오리지테라이 WP_017754440.1 - -
185 예르시니아 엔테로콜리티카 WP_005157703.1 - -
186 신트로포박테랄리스 박테리움 GWC2_56_13 OHE18777.1 - -
187 칸디다투스 박테로이데스 페리오칼리포르니쿠스 KQM08700.1 + -
188 안에어로콜룸나 아미노발레리카 WP_091689178.1 + -
189 나트로닌콜라 펩티디보란스 WP_090439673.1 - -
190 덴드로스포로박터 퀘르시콜러스 WP_092070189.1 - -
191 비-배양 플라보니프락터 sp. SCJ32847.1 - -
192 지오바실러스 sp. Y4.1MC1 OUM85091.1 - -
193 클로스트리듐 볼테아 CAG:59 CCX97030.1 - -
194 로제부리아 이눌리니보란스 A2-194 WP_118109132.1 - -
표 5. 5-카르복시-2-펜테노일-CoA 리덕타제
후보 # 종 등재 번호/서열번호 활성
CP-CoA		 활성
Cr-CoA
1 칸디다 트로피칼리스 XP_026596596.1/ 서열번호 144 + +
2 코랄리오마르가리타 아카지멘시스 DSM 45221 WP_013043307.1 - ND
3 비브리오 카리벤티쿠스 ATCC BAA-2122 WP_009599222.1 - ND
4 세팔로티코쿠스 프리무스 WP_068629633.1 + ND
5 오피투타세아 TSB47 WP_068772922.1 + ND
6 푸니세이코카시이 MEDG31 PDH30576.1 + ND
7 루브리탈레아 마리나 WP_018969548.1 + ND
8 루브리탈레아 프로푼디 WP_105041881.1 + ND
9 루브리탈레아 스쿠알레니파 SHK09753.1 + ND
10 베루코마이크로비에 박테리움 PAW64593.1 - ND
11 비브리오 헤파타리우스 WP_053410267.1 + ND
12 비브리오 나트리에겐스 WP_065302224.1 - ND
13 비브리오 오웬시이 LMG 25430 WP_009705827.1 - ND
14 비브리오 sp. EJY3 WP_014231565.1 + ND
15 아라비돕시스 탈리아나 CAB75790.1 + ND
16 라투스 노르베기쿠스 NP_058905.1 - ND
17 코랄리오마르가리타 sp. OUU72757.1 + ND
18 할로페룰라 sp. WP_035604676.1 + ND
19 오피투타시이 BACL24 KRP37089.1 + ND
20 오피투타시이 EW11 WP_107744621.1 + ND
21 푸니세이코카시이 MED-G30 PDH31188.1 + ND
22 테리마이크로비움 사카리필럼 WP_075078790.1 + ND
23 비브리오 오웬시이 ATCC WP_038894812.1 + ND
24 드로소필라 멜라노가스터 NP_610914.2
서열번호 145		 + +
25 호모 사피엔스 NP_057095.4 + ND
26 유글레나 그라실리스 Q5EU90.1의 말단 절단 버전 + +
비-천연성 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해 충분한 양으로 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 경로 효소를 코딩하는 핵산 하나 이상을 외인성으로 발현하도록 본원에 예시된 바와 같이 당해 기술 분야에 잘 알려진 방법을 이용해 구축된다. 미생물 유기체는 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하기 위해 충분한 조건에서 배양하는 것으로 이해된다. 본원에 제공된 교시 내용 및 지침에 따라, 비-천연성 미생물 유기체는 세포내 농도 약 0.1-200 mM 또는 그 이상으로 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 달성할 수 있다. 일반적으로, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 세포내 농도는 약 3-150 mM, 특히 약 5-200 mM, 보다 특히 약 8-100 mM, 예를 들어, 약 10 mM, 20 mM, 50 mM, 80 mM 이상이다. 이러한 예시된 범위들 각각 간의, 그리고 그 보다 높은 세포내 농도 역시 비-천연성 미생물 유기체에서 달성될 수 있다.
일부 구현예에서, 배양 조건은 혐기성 또는 실질적으로 혐기성 배양 또는 유지 조건을 포함한다. 예시적인 혐기성 조건은 종래에 개시되어 있으며, 당해 기술 분야에 잘 알려져 있다. 발효 공정에 대한 예시적인 혐기성 조건은 본원에 기술되어 있으며, 예를 들어 2011년 5월 24일자 미국 특허 7,947,483에 기술되어 있다. 이러한 조건들 중 임의의 조건을 비-천연성 미생물 유기체와 함께 이용할 수 있으며, 아울러 당해 분야에 잘 알려진 다른 혐기성 조건도 적용할 수 있다. 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 균주는, 이러한 혐기성 조건에서, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 세포내 농도 5-10 mM 또는 그 이상으로, 아울러 본원에 예시된 다른 모든 농도로 합성할 수 있다. 전술한 내용에서 세포내 농도가 언급되더라도, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생산하는 미생물 유기체가 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 세포내에서 생산하거나, 및/또는 배양 배지로 생산물을 분비할 수 있는 것으로 이해된다.
배양 조건은 예를 들어 액체 배양 공정뿐 아니라 발효 및 기타 대량 배양 공정을 포함할 수 있다. 본원에 기술된 바와 같이, 특히 유용한 생합성 생산물의 수율은 혐기성 또는 실질적인 혐기성 배양 조건 하에 달성할 수 있다.
본원에 기술된 바와 같이, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 달성하기 위한 증식 조건의 일 예는 혐기성 배양 또는 발효 조건을 포함한다. 특정 구현예에서, 비-천연성 미생물 유기체는 혐기성 또는 실질적인 혐기성 조건 하에 유지, 배양 또는 발효할 수 있다. 간략하게는, 혐기성 조건은 산소가 결여된 환경을 의미한다. 실질적인 혐기성 조건은, 예를 들어, 배지내 용해 산소가 포화도 0-10%로 유지되는, 배양, 배치 발효 또는 연속 발효를 포함한다. 실질적인 혐기성 조건은 또한 산소 1% 미만의 대기가 유지되는 밀폐된 챔버 안에서 액체 배지 또는 고체 아가에서 세포를 배양하거나 또는 세포를 휴지시키는 것을 포함한다. 산소 %는, 예를 들어 배양물에 N2/CO2 혼합물 또는 기타 적절한 비-산소성 기체 또는 기체들을 퍼징함으로써 유지시킬 수 있다.
본원에 기술된 배양 조건은 대규모로 확장할 수 있으며, 예를 들어 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 제조하기 위해 연속 배양할 수 있다. 배양 공정의 예로는, 피드-배치 발효 (fed-batch fermentation) 및 배치 분리 (batch separation); 피드-배치 발효 및 연속 분리, 또는 연속 발효 및 연속 분리가 있다. 이들 공정 모두 당해 기술 분야에 잘 공지되어 있다. 발효 공정은, 특히, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 상업적인 양으로 생합성하는데 유용하다. 일반적으로, 그리고 비-연속적인 배양 공정을 이용하는 경우와 같이, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 연속 생산 및/또는 거의 연속적인 생산은, 비-천연성 미생물 유기체를 지수기 (exponential phase) 상태로 증식을 유지시키거나 및/또는 거의 유지시키기에 충분한 영양분 및 배지에서 배양하는 것을 포함할 것이다. 이러한 조건에서의 연속 배양은, 예를 들어 1일, 2일, 3일, 4일, 5일, 6일, 7일 또는 그 이상의 기간 동안의 증식을 포함할 수 있다. 추가적으로, 연속 배양은 1주일, 2주일, 3주일, 4주일, 5주일 또는 그 이상에서 최대 수개월을 포함할 수 있다. 대안적으로, 유기체는 특정 용도에 적합하다면, 수시간 배양할 수 있다. 연속적인 및/또는 거의 연속적인 배양 조건은 이러한 예시적인 기간들 사이의 모든 시간 간격을 포함하는 것으로 이해하여야 한다. 아울러, 미생물 유기체를 배양하는 시간은 원하는 목적을 위해 생산물을 충분한 양으로 생산하기 위해 충분한 기간인 것으로 이해된다.
발효 공정은 당해 기술 분야에 잘 공지되어 있다. 간략하게는, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 생합성에 의해 생산하기 위한 발효는, 예를 들어, 피드-배치 발효 및 배치 분리; 피드-배치 발효 및 연속 분리, 또는 연속 발효 및 연속 분리로 이용할 수 있다. 배치 및 연속 발효 공정의 예들은 당해 기술 분야에 잘 공지되어 있다.
6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 균주는, 예를 들어, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올을 상당량으로 연속 생산하기 위한 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올 생산 균주를 이용한 전술한 발효 공정과 더불어, 또한 예를 들어 생산물을 다른 화합물로 변환하는 화학적 합성 공정에 동시에 투입하거나, 또는 생산물을 발효 배양물로부터 분리한 다음 필요에 따라 생산물을 다른 화합물로 변환하는 화학적 변환을 거칠 수 있다. 본원에 기술된 바와 같이, 3-옥소아디페이트, 헥사-2-엔다이오에이트를 이용한 아디페이트 경로에서 중간산물은 예를 들어 플라티늄 촉매 상에서 화학적 수소화 반응에 의해 아디페이트로 변환될 수 있다.
본원에 기술된 바와 같이, 6-아미노카프로익산, 카프로락탐, 헥사메틸렌다이아민 또는 1,6-헥산다이올의 생합성을 달성하기 위한 예시적인 생장 조건은 배양 조건에 내삼투압제 (osmoprotectant)의 첨가를 포함할 수 있다. 특정 구현예에서, 비-천연성 미생물 유기체를 내삼투압제가 존재하는 조건에서 전술한 바와 같이 유지, 증식 및 발효시킬 수 있다. 간략하게는, 내삼투압제는 삼투 물질 (osmolyte)로서 작용하며 본원에 기술된 미생물 유기체가 삼투 스트레스로부터 생존하는데 일조하는 화합물을 지칭한다. 내삼투압제로는, 베타인, 아미노산 및 당 트레할로스를 포함하지만, 이들로 한정되는 것은 아니다. 이에 대한 비-제한적인 예로는 글리신 베타인, 프랄린 베타인, 다이메틸테틴, 다이메틸설포니오프로피오네이트, 3-다이메틸설포니오-2-메틸프로피오네이트, 피페콜산, 다이메틸설포니오아세테이트, 콜린, L-카르니틴 및 엑토인 등이 있다. 일 측면에서, 내삼투압제는 글리신 베타인이다. 당해 기술 분야의 당업자라면, 본원에 기술된 미생물 유기체를 삼투 스트레스로부터 보호하기에 적합한 내삼투압제의 함량 및 종류가 사용되는 미생물 유기체에 따라 결정됨을 알 것이다. 예를 들어, 6-아미노카프로익산이 다양한 양으로 존재하는 조건 하에 에스케리키아 콜라이는 2 mM 글리신 베타인의 존재 하에 적절하게 배양한다. 배양 조건에서 내삼투압제의 함량은, 예를 들어 약 0.1 mM 이하, 약 0.5 mM 이하, 약 1.0 mM 이하, 약 1.5 mM 이하, 약 2.0 mM 이하, 약 2.5 mM 이하, 약 3.0 mM 이하, 약 5.0 mM 이하, 약 7.0 mM 이하, 약 10 mM 이하, 약 50 mM 이하, 약 100 mM 이하 또는 약 500 mM 이하일 수 있다.
경로의 성공적인 조작은 충분한 활성과 특이성을 가진 적절한 효소 세트를 동정하는 것을 수반한다. 이는 적절한 효소 세트를 동정하고, 이의 대응한 유전자를 생산 숙주에 클로닝하고, 발효 조건을 최적화하고, 발효 후 생산물 형성을 분석하는 것을 수반한다. 생산 숙주를 6-아미노카프로익산 또는 카프로락탐을 생산하도록 조작하기 위해, 하나 이상의 외인성 DNA 서열(들)을 숙주 미생물에서 발현시킬 수 있다. 아울러, 미생물은 기능적으로 결손된 내인성 유전자(들)를 가질 수 있다. 이러한 변형은 재생가능한 공급원료를 이용해 6-아미노카프로익산 또는 카프로락탐의 생산을 허용할 것이다.
일부 구현예에서, 6-아미노카프로익산에서 HMD로의 변환 공정 중에 사이클릭 이민 또는 카프로락탐의 형성 최소화 또는 심지어 제거는 고리화를 방지하기 위해 6-아미노카프로익산의 아민 기에 관능기 (예를 들어, 아세틸, 숙시닐)를 부가하는 것을 수반한다. 이는 에스케리키아 콜라이에서 L-글루타메이트로부터 오르니틴을 생성하는 것과 비슷하다. 구체적으로, 먼저 글루타메이트를 N-아세틸글루타메이트 신타제에 의해 N-아세틸-L-글루타메이트로 변환한다. N-아세틸-L-글루타메이트는 이후 N-아세틸글루타밀-포스페이트로 활성화되며, 환원 및 트랜스아민화를 걸쳐 N-아세틸-L-오르니틴이 생성된다. 그 후, N-아세틸-L-오르니틴 데아세틸라제에 의해 N-아세틸-L-오르니틴으로부터 아세틸 기가 제거되어 L-오르니틴이 생성된다. 이러한 경로는, 글루타메이트로부터 글루타메이트-5-포스페이 생성과 후속적인 글루타메이트-5-세미알데하이드로의 환원으로 (S)-1-피롤린-5-카르복실레이트, 즉 글루타메이트-5-세미알데하이드로부터 자발적으로 생성된 사이클릭 이민이 형성되므로, 필수적이다. 6-아미노카프로익산으로부터 HMD를 생성하는 경우, 단계는 6-아미노카프로익산의 아세틸-6-아미노카프로익산으로의 아세틸화, 카르복시산 기의 CoA 또는 포스페이트 기에 의한 활성화, 환원, 아민화 및 탈아세틸화를 수반할 수 있다.
본 발명은, 추가적으로, 생물유래 산물이 대기 이산화탄소 흡수원을 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드, 및/또는 HDO, 또는 본원에 개시된 기타 생산물을 포함하는 배양물 배지를 제공한다. 특정 구현예에서, 배양물 배지는 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO 경로를 가진 비-천연성 미생물 유기체로부터 분리될 수 있다. 다른 구현예에서, 본 발명은 대기 이산화탄소 흡수원을 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 제공한다. 특정 구현예에서, 청구항 61-62의 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO는 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95% 또는 적어도 98%의 Fm 값을 가진다. 본 발명의 이러한 생물유래 산물은 본원에 기술된 바와 같이 본 발명의 방법에 의해 생산할 수 있다.
본 발명은, 추가적으로, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO, 및 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO 이외의 다른 화합물을 포함하는 조성물을 제공한다. 이러한 생물유래 산물 이외의 다른 화합물은 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 가진 본 발명의 비-천연성 미생물 유기체의 미량의 세포 분획일 수 있다. 조성물은 예를 들어 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO, 또는 본 발명의 미생물 유기체의 세포 용해물 또는 배양 상층액을 포함할 수 있다. 일부 구현예에서, 본 발명은 대기 이산화탄소 흡수원을 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 포함하는 조성물을 제공한다. 특정 구현예에서, 청구항 61-62의 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO는 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95% 또는 적어도 98%의 Fm 값을 가진다. 본 발명의 이러한 생물유래 산물을 포함하는 조성물은 본원에 기술된 바와 같이 본 발명의 방법에 의해 생산할 수 있다.
실시예
실시예 1. 6- 아미노카프로익산 ( 6ACA )에 대한 활성을 가진 트랜스아미나제의 동정
트랜스아미나제를 코딩하는 핵산을 메타게놈 라이브러리 및 공공 데이터베이스에서 BLAST (basic local alignment search tool)을 이용해 생물정보학적으로 동정하였다 (표 6). 각 트랜스아미나제를 코딩하는 유전자를 합성 및 발현시키고, 6-아미노카프로익산 (6ACA) 및 γ-아미노부티르산 (GABA)에 대한 촉매 활성을 효소-연계된 분석으로 평가하였다.
표 6의 TA 효소 후보물질을 코딩하는 핵산을 저 카피수 벡터에 구성적 프로모터 하에 클로닝하고, 구조체를 표준 기법을 이용해 E. coli에 형질전환하였다. 형질전환체를 항생제 존재 하에 LB 배지에서 밤새 35℃에서 배양한 다음 세포를 15,000 xg로 실온에서 회전 다운시켰다. 세포용해물을 제조하기 위해, 상층액은 제거하고, TA 유전자를 발현하는 E. coli 세포를 리소자임, 뉴클레아제 및 10 mM DTT가 함유된 화학적 세포용해 용액에 재현탁하였다. 세포용해물은 즉시 사용하였다.
트랜스아미나제 분석 용액은 0.1 M Tris-HCl, pH 8. 0; 0.3 mM 6ACA, 0.3 mM GABA, 0.3 mM HMD, 또는 20 mM Ala; 0.1 mM γ-케토글루타레이트; 1 mM NAD; 및 50 U/mL 글루타메이트 데하이드로게나제를 함유한다. 분석은 TA 세포용해물을 첨가하여 개시하였으며, 실온에서 수행하였다. TA 비-함유 세포용해물과 비교해 340 nm에서 NADH의 흡광도 증가에 의해 활성을 모니터링하였다. Δ흡광도/분으로서 선형적인 비율을 계산하였다. 비율 > 100은 (++)로 표시하고, 비율 1-100은 (+)로 표시하고, 활성이 거의 또는 전혀 없는 경우는 (-)로 표시한다. ND = 검출 안함.
표 6은 TA 상동체 1, 3, 4, 5, 9, 12, 26, 27, 30, 31, 38, 50, 64, 74, 78, 79, 81, 91, 106, 108 및 116이 6ACA에 대해 최고 활성 수준을 가짐을 보여준다.
표 6. 트랜스아미나제 후보 유전자
상동체 # 유기체 서열번호 등재 번호 활성 6ACA 활성 GABA 생체내 6ACA 생산
1 아크로모박터 크실로스옥시단스 서열번호 1 WP_013395096.1 ++ ++ +
2 메타게노믹 HAC67230.1 - ++
3 메타게노믹 서열번호 3 WP_100856578.1 ++ ++ +
4 메타게노믹 서열번호 4 WP_025513437.1 ++ ++
5 메타게노믹 서열번호 5 WP_056075635.1 ++ ++
6 메타게노믹 WP_017521342.1 + ++
7 메타게노믹 WP_017201530.1 ND ND
8 메타게노믹 WP_059316136.1 + ++
9 메타게노믹 서열번호 9 WP_024817707.1 ++ ++
10 메타게노믹 WP_093015681.1 + ++
11 메타게노믹 WP_069902234.1 - ++
12 메타게노믹 서열번호 12 WP_009357183.1 ++ ++
13 팬아르트로박터 아우레센스 TC1 서열번호 13 서열번호 13 + ++ +
14 메타게노믹 WP_052967527.1 - ++
15 메타게노믹 서열번호 15 + ++
16 메타게노믹 WP_043819139.1 - +
17 메타게노믹 WP_062073360.1 + ++
18 메타게노믹 WP_015937959.1 + ++
19 메타게노믹 WP_078774761.1 + ++
20 메타게노믹 WP_046815379.1 + ++
21 메타게노믹 WP_090288152.1 - +
22 메타게노믹 WP_056075635.1 ND ND
23 메타게노믹 WP_003220503.1 - -
24 메타게노믹 WP_003255866.1 - +
25 메타게노믹 WP_104171925.1 - +
26 메타게노믹 서열번호 26 WP_123429804.1 ++ ++ +
27 메타게노믹 서열번호 27 WP_030536079.1 ++ ++ +
28 메타게노믹 WP_040078233.1 + ++
29 메타게노믹 EQM68262.1 - -
30 메타게노믹 서열번호 30 WP_026539700.1 ++ ++
31 메타게노믹 서열번호 31 WP_012250302.1 ++ ++ +
32 메타게노믹 WP_007983072.1 - -
33 메타게노믹 WP_045059477.1 - +
34 메타게노믹 WP_093432282.1 - ++
35 메타게노믹 WP_125050266.1 - ++
36 메타게노믹 서열번호 36 - ++
37 메타게노믹 WP_134929664.1 - -
38 메타게노믹 서열번호 38 WP_056075635.1 ++ ++
39 메타게노믹 WP_065926318.1 - -
40 메타게노믹 WP_123366550.1 - -
41 메타게노믹 WP_019473946.1 - ++
42 메타게노믹 WP_065926966.1 - ++
43 메타게노믹 WP_121733815.1 - ++
44 메타게노믹 WP_015937959.1 - -
45 메타게노믹 WP_071291640.1 + +
46 메타게노믹 WP_111045681.1 - -
47 메타게노믹 WP_056737712.1 + ++
48 메타게노믹 WP_042650496.1 - ++
49 메타게노믹 WP_106886181.1 + ++
50 메타게노믹 서열번호 50 WP_056563276.1 ++ ++ +
51 메타게노믹 WP_017197131.1 + ++
52 메타게노믹 서열번호 52 WP_099790225.1 + ++ +
53 메타게노믹 WP_048393168.1 - +
54 메타게노믹 WP_123366550.1 - ++
55 메타게노믹 WP_017391017.1 + ++
56 메타게노믹 서열번호 56 + ++
57 메타게노믹 WP_056075635.1 - -
58 메타게노믹 WP_054597933.1 - -
59 메타게노믹 WP_095746204.1 - -
60 메타게노믹 WP_003220503.1 - -
61 메타게노믹 WP_017197131.1 - -
62 메타게노믹 WP_052967527.1 - ++
63 메타게노믹 WP_021472307.1 - -
64 아르트로박터 sp. Edens01 서열번호 64 WP_055239729.1 ++ ++ +
65 아르트로박터 크리탈로포이에테스 WP_074699490.1 - -
66 아르트로박터 sp. KI72 WP_079941468.1 - ++
67 아르트로박터 아길리스 WP_087028133.1 + ++
68 메타게노믹 WP_119966131.1 + ND
69 메타게노믹 RIK89039.1 + ND
70 메타게노믹 WP_016152939.1 - ND
71 메타게노믹 WP_089085686.1 + ND
72 메타게노믹 WP_054094475.1 - ND
73 메타게노믹 WP_105516444.1 + ++
74 메타게노믹 서열번호 74 WP_123787193.1 ++ ++
75 메타게노믹 WP_088966344.1 - ND
76 메타게노믹 WP_119775651.1 + ND
77 메타게노믹 서열번호 77 + ++
78 메타게노믹 서열번호 78 WP_011748622.1 ++ ND
79 메타게노믹 서열번호 79 WP_111824632.1 ++ ++
80 메타게노믹 HAU57754.1 + ND
81 메타게노믹 서열번호 81 SHM39441.1 ++ ++
82 메타게노믹 WP_043683590.1 + ND
83 메타게노믹 서열번호 83 - ND
84 메타게노믹 WP_121579846.1 + ND
85 메타게노믹 WP_101193102.1 + ND
86 메타게노믹 WP_012249988.1 + ++
87 메타게노믹 WP_119775651.1 - ND
88 메타게노믹 OGB44516.1 + ND
89 메타게노믹 WP_102820733.1 + ND
90 메타게노믹 SHM39441.1 + ++
91 메타게노믹 서열번호 91 SHM39441.1 ++ ++
92 메타게노믹 WP_088966344.1 + ++
93 메타게노믹 RIK89039.1 + ND
94 메타게노믹 WP_043683590.1 + ND
95 메타게노믹 WP_137155920.1 + ND
96 메타게노믹 WP_099059309.1 + ++
97 메타게노믹 WP_101193102.1 ND ND
98 메타게노믹 WP_043683590.1 + ND
99 메타게노믹 WP_062685190.1 + ++
100 메타게노믹 WP_081768742.1 + ND
101 메타게노믹 ODT51733.1 + ND
102 메타게노믹 WP_104959793.1 + ND
103 메타게노믹 WP_043683590.1 + ND
104 메타게노믹 HAU57754.1 + ND
105 메타게노믹 WP_009615038.1 - ND
106 메타게노믹 서열번호 106 SHM39441.1 ++ ++
107 메타게노믹 WP_056323744.1 + ++
108 메타게노믹 서열번호 108 WP_056323744.1 ++ ++
109 메타게노믹 WP_088966344.1 + ++
110 메타게노믹 SHM39441.1 + ND
111 메타게노믹 WP_125868825.1 + ND
112 메타게노믹 서열번호 112 + ND
113 메타게노믹 WP_124644434.1 + ND
114 메타게노믹 WP_101193102.1 + ND
115 메타게노믹 WP_057067610.1 + ND
116 메타게노믹 서열번호 116 ODT32214.1 ++ ++
117 메타게노믹 WP_136961719.1 + ND
118 메타게노믹 WP_093109347.1 - ND
119 메타게노믹 WP_043683590.1 + ND
120 메타게노믹 WP_043683590.1 - ND
121 메타게노믹 WP_008955628.1 + ND
122 메타게노믹 SHM39441.1 + ND
123 메타게노믹 WP_003832711.1 + ND
124 메타게노믹 WP_116003699.1 + ND
125 메타게노믹 WP_120809350.1 - ND
126 메타게노믹 WP_026133539.1 + ++
127 메타게노믹 WP_119775651.1 + ND
128 메타게노믹 SHM39441.1 + ++
129 메타게노믹 WP_043683590.1 + ND
130 메타게노믹 WP_015475018.1 - ND
131 메타게노믹 WP_047290758.1 ND ND
132 메타게노믹 WP_116810265.1 - ND
133 사카로마이세스 세레비지애 서열번호 133 NP_011533.3 + ++
134 클로스트리듐 비리드 서열번호 134 WP_027096390.1 + ++
135 굴로시박터 몰리나티보락스 서열번호 135 WP_026937197.1 + ++
136 코쿠리아 리조필라 서열번호 136 WP_012399017.1 ++ ++
137 아르트로박터 sp. FB24 서열번호 137 ABK04473.1 ++ ++
138 슈도모나스 sp. AAC 서열번호 138 WP_009615038.1 + +
139 슈도모나스 푸티다 KG-4 서열번호 139 WP_043861306.1 + +
140 알칼리게네스 A. 패칼리스 서열번호 140 WP_006225725.1 + +
실시예 2. 트랜스아미나제 상동체들에 대한 생체내 분석.
생체내 트랜스아미나제 상동체들의 활성을 검사하기 위해, 선택한 트랜스아미나제를 코딩하는 유전자들을, 1) 3-옥소아디필-CoA 티올라제 (Thl), 2) 3-옥소아디필-CoA 데하이드로게나제 (Hbd), 3) 3-옥소아디필-CoA 데하이드라타제 ("크로토나제" 또는 Crt), 4) 5-카르복시-2-펜테노일-CoA 리덕타제 (Ter); 및 5) 알데하이드 데하이드로게나제 (Ald)를 코딩하는 도입된 유전자를 또한 포함하는 E. coli 균주에 형질전환하였다. Thl, Hbd, Crt, Ter, Ald 유전자들은 US 8,377,680 (예, 실시예 8, 그 전체가 원용에 의해 본 명세서에 포함됨)에 언급되어 있다. 이들 유전자는 TA 효소를 제외한 6-아미노카프로에이트 (6ACA) 생산에 필수적인 경로 효소들을 모두 함유한 E. coli 균주에 도입된다.
TA 유전자를 발현하는 벡터를 Thl/Hbd/Crt/Ter/Ald E. coli 균주에 형질전환하였으며, 형질전환체에서 6ACA 생산을 검사하였다. 조작된 E. coli 세포에는 최소 배지 하에 2% 글루코스를 제공하였으며, 35℃에서 18시간 동안 인큐베이션한 다음 세포를 회수하고, 상층액을 분석용 HPLC 또는 표준 LC/MS 분석 방법을 통해 6ACA 생산을 평가하였다. 표 6에 나타낸 바와 같이, Thl, Hbd, Crt, Ter 및 Ald 유전자를 가진 E. coli에서 TA 효소를 코딩하는 유전자의 발현으로, 이들 균주에서 6ACA 생산이 달성되었다.
실시예 3. 트랜스아미나제 변이체 .
단백질의 결정 구조를 조사함으로써, 서열번호 1에 의해 코딩된, 아크로모박터 크실로스옥시단스의 상동체 1 TA에서, 아미노산의 돌연변이 위치를 동정하였으며, 서열번호 1을 코딩하는 유전자에 대해 선택 아미노산 위치에서 포화 돌연변이 유발을 수행하였다. 수득한 변이체들을 대상으로 실시예 1에 기술한 바와 같이 세포용해물 분석으로 활성을 검사하였다. TA 서열번호 1의 결과를 도 2에 나타낸다. 도 2는 활성에 중요한 서열번호 1의 위치들을 표시한다.
아미노산 위치 V114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265 및 L386뿐 아니라 G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416 및 A421의 코돈에서 TA 효소를 코딩하는 유전자 (서열번호 1)에 돌연변이를 유발하여, 변이체들을 구축하였다. 돌연변이는 단독으로, 그리고 다른 아미노산 위치에서의 돌연변이와 조합하여 수행하였다. 아미노산 위치들에서 돌연변이는 축중 프라이머 서열 및 PCR을 이용해 수행하였으며, 변이된 유전자 서열 혼합물을 E. coli에 형질전환하였다. 형질전환체는 실시예 1에 기술된 바와 같이 세포용해물 분석으로 검사하였다. 분석에서 야생형 대조군에 비해 활성이 높은 세포용해물의 기원 클론에 대해 트리플리케이트 세포용해물 분석으로 다시 검사하였다. 야생형 활성에 비해 높은 것으로 계속 검증된 클론들은 함유된 TA 유전자의 서열을 분석하기 위해 준비하였다.
표 7 및 도 3은 활성 클론들의 변이체 TA 유전자 서열에서 발견된 돌연변이들을 나타낸다. 야생형 활성보다 높은 것으로 확인된 변이체들은 "+" 또는 "++"로 표시하며, 이는 TA 유전자 내 단일 돌연변이 및 조합 (다중) 돌연변이를 포함한다. 표 7은, 변이체의 기원이 되는 야생형 TA에 비해 활성이 우수한 복수의 변이체를 생성하는, 아미노산 위치 114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265, L386, G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416, A421, G17, M21, A50, A76, Y77, Q78, I79, G84, F107, T108, K119, G139, M142, A152, P153, E205, G209, G211, D238, M285, A290, G291, G292, L293, Y297, M353, S387, S388 및 G392 (위치는 서열번호 1을 기준으로 식별)에 돌연변이가 존재하는, 야생형 TA (서열번호 1)보다 활성이 우수한 것으로 입증된 복수의 변이체들을 나타낸다.
아울러, 변이체들 중 몇몇은 6ACA 또는 GABA 대신 기질로서 20 mM 알라닌을 이용해 분석하였다.
표 7. 트랜스아미나제 변이체
변이체 # 서열번호 1 대비 아미노산 치환 활성 6ACA 활성 GABA 활성 Ala 생체내 6ACA 생산
1 A113V + ++ ND
2 E112K - - ND
3 I49V + ++ ND
4 T264S + ++ ND
5 G19R C22S D70N L186V K318M G336S S416Y + ++ ND
6 V111A + ++ ND
7 I203L + ++ ND
8 T148I + ++ ND
9 G19R D70N D99E L186V K318M G336S S416N + ++ ND
10 T109S + ++ ND
11 T148V + ++ ND
12 S136A ++ ++ ND
13 Q208R + ++ ND
14 L386V + ++ ND
15 G144C + ++ ND
16 I49V S136A T148I + ++ ND
17 S136C + ++ ND
18 S136G + ++ ND
19 I204K + ++ ND
20 M265C + ++ ND
21 V207E + ++ ND
22 S136A T148I V207E ++ ++ ND
23 V207T + ++ ND
24 I204Q + ++ ND
25 I204T + ++ ND
26 L386C + ++ ND
27 M265N + ++ ND
28 G19R D70N L186V K318M G336S S416Y + ++ ND
29 A237T + ++ ND
30 A237D + ++ ND
31 A237V + ++ ND
32 A237G + ++ ND
33 A237S ++ ++ ND
34 G243C + ++ ND
35 I49V S136A T148I V207E ++ ++ ND
36 M265A + ++ ND
37 T216V + ++ ND
38 G19R D70N F133L L186V K318M G336S S416Y + ++ ND
39 T216A + ++ ND
40 G19R C22S D70N L186V K318M G336S S416Y + ++ ND
41 T216C + ++ ND
42 T242A + ++ ND
43 T264P + ++ ND
44 F137W Y154N + ++ ND
45 Y154N + ++ ND
46 Y154I + ++ ND
47 G19R D70N L186V K318M G336S S416D + ++ ND
48 Y154L + ++ ND
49 Y154V + ++ ND
50 Y154F + ++ ND
51 Y154T + ++ ND
52 Y154C + + ND
53 Y154M + ++ ND
54 S136A T148I ++ ++ ND
55 F137T Y154K - ND +
56 F137I - ND +
57 G19R D70N K150R L186V L234I K318M G336S V390D S416N + ++ ND
58 T148D + ND +
59 L386A + ND +
60 R94H S178T A315V R338L + ++ ND
61 K226T R338L + ++ ND
62 R338L + ++ ND
63 L386C + ND +
64 G19R D70N L186V K318M G336S A406E S416Y + ++ ND
65 G19R D70N L186V K318M G336S L386P S416Y A421E + ++ ND
66 G19R D70N A76G L186V K318M G336S L386P S416Y A421E ++ ++ ND
67 G19R D70N A76Q L186V K318M G336S L386P S416Y A421E ++ ++ ND
68 G19R D70N G139E L186V K318M G336S L386P S416Y A421E + ++ ND
69 G19R D70N L186V G291S K318M G336S L386P S416Y A421E ++ ++ ND
70 G19R D70N L186V G292C K318M G336S L386P S416Y A421E ++ ++ ND
71 G19R I49Y D70N L186V K318M G336S L386P S416Y A421E ++ ++ ND
72 G19R D70N I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
73 G19R D70N K119Y L186V K318M G336S L386P S416Y A421E + ++ ND
74 G19R D70N L186V K318M G336S L386P L293C S416Y A421E ++ ++ ND
75 G19R D70N L186V K318M G336S L386P L293M S416Y A421E ++ ++ ND
76 G19R D70N M142S L186V K318M G336S L386P S416Y A421E ++ ++ ND
77 G19R D70N M142C L186V K318M G336S L386P S416Y A421E ++ ++ ND
78 G19R D70N M142Y L186V K318M G336S L386P S416Y A421E ++ ++ ND
79 G19R D70N P153D L186V K318M G336S L386P S416Y A421E ++ ++ ND
80 G19R D70N Q78V L186V K318M G336S L386P S416Y A421E ++ ++ ND
81 G19R D70N Q78A L186V K318M G336S L386P S416Y A421E ++ ++ ND
82 G19R D70N Q78Y L186V K318M G336S L386P S416Y A421E ++ ++ ND
83 G19R D70N Q78N L186V K318M G336S L386P S416Y A421E ++ ++ ND
84 G19R D70N V111S L186V K318M G336S L386P S416Y A421E ++ ++ ND
85 G19R D70N V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
86 G19R D70N Y154W L186V K318M G336S L386P S416Y A421E + ++ ND
87 G19R D70N Y154F L186V K318M G336S L386P S416Y A421E ++ ++ ND
88 G19R D70N Y77F L186V K318M G336S L386P S416Y A421E ++ ++ ND
89 G19R D70N I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
90 G19R D70N Q78N L186V K318M G336S L386P S416Y A421E ++ ++ + +
91 G19R D70N Q78N I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
92 G19R D70N Q78Y L186V K318M G336S L386P S416Y A421E ++ ++ ND
93 G19R D70N Q78Y I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
94 G19R D70N A76G L186V K318M G336S L386P S416Y A421E ++ ++ ND
95 G19R D70N A76G I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
96 G19R D70N A76G Q78N L186V K318M G336S L386P S416Y A421E ++ ++ ND
97 G19R D70N A76G Q78N I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
98 G19R D70N A76G Q78Y L186V K318M G336S L386P S416Y A421E ++ ++ ND
99 G19R D70N A76G Q78Y I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
100 G19R D70N A76G L186V K318M G336S L386P S416Y A421E ++ ++ ND
101 G19R D70N A76Q I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
102 G19R D70N A76Q Q78N L186V K318M G336S L386P S416Y A421E ++ ++ ND
103 G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E ++ ++ + +
104 G19R D70N A76Q Q78Y L186V K318M G336S L386P S416Y A421E - ++ ND
105 G19R D70N A76Q Q78Y I79V L186V K318M G336S L386P S416Y A421E + ++ ND
106 G19R D70N V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
107 G19R D70N I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
108 G19R D70N Q78N V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
109 G19R D70N Q78N I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
110 G19R D70N Q78Y V111A L186V K318M G336S L386P S416Y A421E ++ ++ + +
111 G19R D70N Q78Y I79V V11A L186V K318M G336S L386P S416Y A421E ++ ++ ND
112 G19R D70N A76G V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
113 G19R D70N A76G I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
114 G19R D70N A76G Q78N V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
115 G19R D70N A76G Q78N I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
116 G19R D70N A76G Q78Y V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
117 G19R D70N A76G Q78Y I79V V11A L186V K318M G336S L386P S416Y A421E ++ ++ ND
118 G19R D70N A76Q V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
119 G19R D70N A76Q I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ + +
120 G19R D70N A76Q Q78N V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
121 G19R D70N A76Q Q78N I79V V111A L186V K318M G336S L386P S416Y A421E ++ ++ ND
122 G19R D70N A76Q Q78Y V111A L186V K318M G336S L386P S416Y A421E + ++ ND
123 G19R D70N A76Q Q78Y I79V V11A L186V K318M G336S L386P S416Y A421E + ++ ND
124 A76Q Q78N I79V L386P + + + +
125 G19R D70N A76Q Q78N I79V S136A M142I L186I A290L K318M G336S L386P V390A S416Y A421E ++ ++ ND
126 G19R D70N A76Q Q78N I79V K318M G336S L386P V390L S416Y A421E ++ ++ ND +
127 G19R D70N A76Q Q78N I79V K318M G336S L386P V390L S416Y A421E ++ ++ ND
128 G19R D70N A76Q Q78N I79V S136A L186V Y297F K318M G336S L386V V390A S416Y A421E ++ ++ ND
129 G19R D70N A76Q Q78N I79V S136A A152V L186M A290L Y297F K318M G336S L386I S416Y A421E ++ ++ ND
130 G19R D70N A76Q Q78N I79V A152T L186I Y297F K318M G336S L386V V390L S416Y A421E ++ ++ + +
G19R D70N A76Q Q78N I79V A152T L186I Y297F K318M G336S L386P V390L S416Y A421E
131 G19R D70N A76Q Q78N I79V S136G A152T L186M K318M G336S L386V S416Y A421E ++ ++ ND
132 G19R D70N A76Q Q78N I79V A152T L186M A290L K318M G336S L386V S416Y A421E ++ ++ ND
133 G19R D70N A76Q Q78N I79V S136A A152V L186M Y297F K318M G336S L386P V390A S416Y A421E ++ ++ ND
134 G19R D70N A76Q Q78N I79V S136G A152V L186I Y297F K318M G336S L386P S416Y A421E ++ ++ ND
135 G19R D70N A76Q Q78N I79V S136G A152T L186M A290L K318M G336S L386V S416Y A421E ++ ++ ND
136 G19R D70N A76Q Q78N I79V S136A A152V Y297F K318M G336S L386V V390A S416Y A421E ++ ++ + +
137 G19R D70N A76Q Q78N I79V S136A L186M A290L K318M G336S L386I V390L S416Y A421E ++ ++ ND
138 G19R D70N A76Q Q78N I79V S136A A152T L186M K318M G336S L386V S416Y A421E ++ ++ ND
139 G19R D70N A76Q Q78N I79V S136A L186M A290L K318M G336S L386V S416Y A421E ++ ++ ND
140 G19R D70N A76Q Q78N I79V S136A A152T L186I A290L K318M G336S L386V V390L S416Y A421E ++ ++ ND
141 G19R D70N A76Q Q78N I79V S136A L186I K318M G336S L386V Y297F V390A S416Y A421E ++ ++ ND
142 G19R D70N A76Q Q78N I79V S136A K318M G336S L386V V390L S416Y A421E ++ ++ ND
143 G19R D70N A76Q Q78N I79V S136A K318M G336S L386V V390A S416Y A421E ++ ++ ND
144 G19R D70N A76Q Q78N I79V S136G K318M G336S Y297F L386P S416Y A421E ++ ++ ND
145 G19R D70N A76Q Q78N I79V A152T A290L K318M G336S Y297F L386P S416Y A421E ++ ++ ND
146 G19R D70N A76Q Q78N I79V A152T A290L K318M G336S Y297F L386P S416Y A421E ++ ++ ND
147 G19R D70N A76Q Q78N I79V S136A A152T L186A A290L K318M G336S Y297F L386P V390A S416Y A421E ++ ++ ND
148 G19R D70N A76Q Q78N I79V S136G A152V L186M A290L K318M G336S Y297F L386P S416Y A421E ++ ++ ND
149 G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ + +
150 G17A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
151 G19K D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
152 G19Q D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
153 M21Q G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
154 M21Q M285I G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
155 G17S G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
156 G17Y G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
157 C22M G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
158 C22Y G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
159 N70A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
160 N70Y G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
161 G19R A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
162 G19R D70C A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
163 A50N G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
164 F107M G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
165 F107S G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
166 F107Q G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
167 T108Q G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - - ND
168 T108A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
169 E112M G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
170 S136D G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
171 S136G G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E ++ ++ ND
172 S136A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
173 A152M G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
174 A152V G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
175 A152C G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
176 A152L G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
177 A152T G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
178 A152Q G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
179 K150H G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
180 G19R D70N A76Q Q78N I79V L186I K318M G336S L386P S416Y A421E + ++ ND
181 G19R D70N A76Q Q78N I79V L186M K318M G336S L386P S416Y A421E + ++ ND
182 E205D G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
183 D238E G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
184 D238I G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
185 G84V G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
186 D238M G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
187 G209G G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
188 G211N G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
189 T242F G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
190 A290D G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
191 A290K G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
192 A290I G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
193 Y297F G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
194 Y297P G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
195 M353N G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
196 G19R D70N A76Q Q78N I79V L186V K318F G336S L386P S416Y A421E + ++ ND
197 S387Y G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
198 C388A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
199 G389G G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
200 G392T G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E - + ND
201 G392N G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
202 V390L G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + ++ ND
203 V390D G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
204 V390A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
205 G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416W A421E + + ND
206 G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416C A421E + + ND
207 G392A G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421E + + ND
208 G19R D70N A76Q Q78N I79V L186V K318M G336S L386S S416Y A421E + + ND
209 G19R D70N A76Q Q78N I79V L186V K318M G336S L386P S416Y A421D + + ND
210 G19R D70N A76Q Q78N I79V L186V K318M G336S S416Y A421E ++ ++ ND
211 G19R D70N A76Q Q78N I79V L186V K318M G336S L386V S416Y A421E ++ ++ ND
212 S136A A152V V386I V390A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
213 S136A A152T V390L G19R D70N A76Q Q78N I79V K318M G336S Y297F L386I S416Y A421E ++ ++ ND
214 S136A A152V V186I A290L Y297F G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
215 S136A V186M Y297F G19R D70N A76Q Q78N I79V K318M G336S L386V S416Y A421E ++ ++ ND
216 S136A A152V G19R D70N A76Q Q78N I79V K318M G336S Y297F L386I S416Y A421E ++ ++ ND
217 G19R D70N A76Q Q78N I79V K318M G336S Y297F L386I S416Y A421E ++ ++ ND
218 V186I V390A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386I S416Y A421E ++ ++ ND
219 S136A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
220 S136G A152V V186I G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
221 V186I G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
222 S136A A290L V390L G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
223 S136A V186A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
224 S136A V186M G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
225 S136A V186M A290L G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
226 S136G V186I G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
227 S136A A152V A290L G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
228 S136G V186I G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
229 S136G V186M G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
230 S136A V186A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
231 S136G V186M G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
232 S136A A152V G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
233 S136A G19R D70N A76Q Q78N I79V K318M G336S Y297F L386V S416Y A421E ++ ++ ND
실시예 4. 6- 아미노카프로익산 ( 6ACA )에 대해 활성을 가진 CAR 상동체의 동정
CAR을 코딩하는 유전자를 메타게놈 라이브러리 및 공공 데이터베이스에서 BLAST (basic local alignment search tool)을 이용해 생물정보학적으로 동정하였다 (표 8). 각 CAR을 코딩하는 유전자를 합성 및 발현시키고, 6-아미노카프로익산 (6ACA) 및 헥사노에이트 (GABA)에 대한 촉매 활성을 효소-연계 분석으로 평가하였다.
간략하게는, 카르복시산 리덕타제 (CAR) 후보 및 변이체를 평가하기 위해, CAR 플라스미드를 가진 포스포판테테인 트랜스퍼라제 통합 E. coli 균주를 구축하였다. 균주는 카르베니실린 (100 ㎍/mL)이 첨가된 LB에 접종하여 교반 배양기에서 밤새 37℃에서 배양하였다. 밤새 배양물을 카르베니실린 (100 ㎍/mL), IPTG (0.5 mM) 및 쿠메이트 (0.2 mM)가 첨가된 신선한 LB로 희석하고, 밤새 27℃에서 교반 배양기에서 배양하였다. 이를 원심분리하여 세포를 수집하고, 분석 당일까지 -20℃에서 냉동시켰다.
시험관내 세포용해물 분석을 위해, 세포 펠릿을 해동하고, 0.1 M Tris-HCl, pH 7.0 완충제에 재현탁하였다. 세포 현탁물의 OD600을 측정하고, 각 후보물질을 OD 4에 대해 정규화하였다. 원심분리하여 펠릿을 준비하고, 이를 뉴클레아제 및 리소자임이 첨가된 화학적 세포용해 시약을 실온에서 30분간 처리하여 세포용해 처리하였다. 세포용해물을 이용해 CAR 활성을 측정하였으며, 분석은 다음과 같이 수행하였다: CAR 세포용해물 조산물 분액, 바람직한 산 기질 (헥사노에이트, 6-아미노카프로익산, 부티레이트 및 4-아미노부티르산), 1 mM ATP, 0.3 mM NADPH 및 10 mM MgCl2를 0.1 M Tris-HCl, pH 7.4 완충제 0.04 mL 중에 혼합하였다. NADPH 산화로 반응물의 카이네틱스를 형광 또는 흡광을 통해 모니터링하였다. CAR 활성 비율을 진행 곡선 (progress curve)으로부터 결정하였다.
표 8은 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264에 해당하는 CAR 상동체들은 모두 6ACA, 헥사노에이트 또는 이 둘다에 대해 활성을 나타냄을 보여준다.
표 8. CAR 상동체
상동 체 # 유기체 서열번호 등재 번호 활성 6ACA 활성 헥사노에이트 생체내 HMD 생산
1 마이콜리시박테리움 스메그마티스 MC2 155 150 WP_011728718.1 + +
2 마이콜리시박테리움 스메그마티스 MC2 155 151 AFP42026.1 + +
3 마이코박테리움 아비움 152 WP_003872682.1 + +
4 마이코박테리움 아비움 153 WP_003872682.1 + +++ +
5 마이코박테리움 마리눔 M 154 WP_012393886.1 + +
6 마이코박테리움 리플란디이 128FXT 155 ACC41375.1 + +
7 마이코박테리움 투베르쿨로시스 변종 보비스 BCG 156 WP_011799278.1 + +
8 스트렙토마이세스 그리세우스 아종 그리세우스 NBRC 13350 157 WP_012382217.1 + +
9 사카로마이세스 세레비지애 S288C 158 NP_009673.1 + +
10 시아노비움 sp. PCC 7001 159 EDY38441.1 + +
11 뉴로스포라 크라사 160 XP_955820.1 ND ND
12 스트렙토마이세스 프라디에 161 ASW31113.1 + +
13 마이코박테리움 리플란디이 128FXT 162 AXN44890.1 + +
14 마이코박테로이데스 앱세수스 163 CPX02987.1 ND ND
15 마이콜리시박테리움 박케 ATCC 25954 164 EJZ09834.1 - +
16 소란기움 셀룰로숨 165 KYF89500.1 - +
17 마이코박테로이데스 앱세수스 아종 마실리엔스 166 SLB41318.1 - -
18 쿠르토박테리움 sp. MCSS17_007 167 WP_028185036.1 - -
19 노카르디아 브라실리엔시스 ATCC 700358 168 WP_029900022.1
20 알로쿠츠네리아 알바타 169 WP_030430720.1 - +
21 마이콜리시박테리움 반바알레니이 PYR-1 170 WP_042264421.1 + -
22 노카르디아 불네리스 171 KIA63422.1 - ++
23 마이콜리시박테리움 콘플루엔티스 172 WP_045824606.1 - -
24 마이콜리시박터 아루펜시스 173 WP_046295775.1 - ++
25 마이코박테리움 시미에 174 WP_047542266.1 + +
26 스트렙토마이세스 sp. TSRI0395 175 WP_050362911.1 + +
27 노카르디아 세리올레 176 WP_051178149.1 - +
28 아카로마이세스 인골디이 177 WP_051297098.1 + +
29 로도코커스 sp. Leaf247 178 WP_056069829.1 + +
30 스트렙토마이세스 sp. Root1310 179 WP_057605035.1 - -
31 스핑고비움 sp. MI1205 180 WP_062112979.1 + +
32 스트렙토마이세스 윤나넨시스 181 WP_062207887.1 - -
33 마이코박테리움 sp. KMS 182 WP_064915933.1 - -
34 마이코박테리움 인트라셀룰라레 ATCC 13950 183 WP_064939119.1 - +
35 마이콜리시박테리움 셀레리플라붐 184 WP_067216488.1 - +
36 마이콜리시박테리움 팔락스 185 WP_067876059.1 + +
37 노카르디아 테르페니카 186 WP_067585591.1 - -
38 마이콜리시박테리움 페레그리눔 187 WP_067973901.1 - ++
39 마이코박테리움 sp. E1386 188 WP_068119938.1 - +
40 마이코박테로이데스 앱세수스 아종 앱세수스 189 WP_052544110 - -
41 마이코박테리움 sp. SWH-M1 190 WP_073684817.1 - ++
42 마이코박테로이데스 앱세수스 아종 볼레티이 191 WP_074248349.1 - +++
43 큐르토박테리움 sp. MCBA15_012 192 WP_071245982.1 ND ND
44 마이코박테로이데스 앱세수스 아종 앱세수스 193 WP_074331300.1
45 마이코박테리움 콜롬비엔스 194 WP_076102317.1 - -
46 윌리암시아 스테르쿨리에 195 WP_076478068.1 + +
47 마이코박테로이데스 켈로에 196 WP_078287768.1 - -
48 마이코박테리움 sp. AT1 197 WP_079921768.1 - -
49 브레비박테리움 카세이 198 WP_082829042.1 + ++
50 마이코박테리움 노비오마겐스 199 WP_083087901.1 + +
51 마이콜리시박테리움 페레그리눔 200 OBB89769.1 ++ ++
52 슈도노카르디아 sp. SCN 73-27 201 ODU29987.1 - -
53 클로로플렉시 박테리움 HGW-클로로플렉시-5 202 PKN69095.1 - +
54 마이콜리시박테리움 투시애 203 WP_083123568.1 + ++
55 마이콜리시박테리움 구디이 204 WP_100516314.1 + ++
56 프란키아 sp. EUN1h 205 WP_007506938.1 ++ ++
57 마이코박테리움 sp. JS623 206 WP_015306631.1
58 레지오넬라 모라비카 207 WP_028384907.1
59 슈도모나스 sp. 43NM1 208 WP_101209428.1 ++ ++
60 마이코박테리움 sp. EPG1 209 WP_104865516.1 ++ ++
61 아파노테세 cf. 미누티시마 CCALA 015 210 WP_106220800.1 + -
62 로도코커스 sp. AG1013 211 WP_114723703.1 - +
63 로도코커스 sp. AG1013 212 WP_114723596.1 + +
64 마이크로박테리움 sp. AG157 213 WP_116239091.1 ++ ++
65 노카르디아 sp. YIM PH 21724 214 WP_120042211.1 + +
66 마이셀리게네란스 크실리고우엔스 215 WP_123814706.1 + +
67 슈도노카르디알레스 박테리움 216 WP_132386047.1
68 스트렙토마이세스 스카브리스포루스 217 WP_126639580.1 - -
69 마이코박테리움 [투베라쿨로시스] TKK-01-0051 218 WP_133895376.1 - +
70 마이콜리시박테리움 라체렌스 219 WP_133759136.1 + ++
71 로도코커스 sp. 06-469-3-2 220 WP_094685926.1 - -
72 고르도니아 스푸티 NBRC 100414 221 WP_005206594.1
73 마이코박테로이데스 앱세수스 아종 앱세수스 222 SHU01071.1 ++ ++
74 마이코박테리움 sp. 223 PJE23808.1 ++ ++
75 마이코박테리움 데시피엔스 224 WP_104061604.1 ++ ++
76 마이코박테로이데스 앱세수스 아종 볼레티이 225 WP_100483059.1 - +
77 슈도모나스 프라기 226 WP_095030548.1 - +
78 로도코커스 sp. 15-1154-1 227 WP_094713117.1 - +
79 로도코커스 sp. 05-340-1 228 WP_037189966.1 + +
80 마이코박테리움 다이옥사노트로피쿠스 229 WP_087077450.1 - +
81 마이코박테리움 쿠비캐 230 ORV97129.1 + +
82 마이코박테리움 콜롬비엔스 231 OBK63104.1 - -
83 마이코박테리움 아바지컴 232 WP_096287632.1
84 마이코박테리움 콜롬비엔스 233 WP_065073482.1 - +
85 클라비박터 미키가넨시스 아종 미키가넨시스 NCPPB 382 234 CAN00144.1
86 마이코박테로이데스 앱세수스 아종 볼레티이 50594 235 WP_134080798.1 + -
87 마이콜리시박테리움 로데시애 JS60 236 EHB47859.1
88 마이코박테로이데스 이뮤노게눔 237 WP_064629783.1 - +
89 마이코박테로이데스 사오파울렌스 238 WP_070909839.1 - +
90 로도코커스 sp. 06-412-2C 239 WP_057479409.1 - -
91 마이코박테리움 sp. 1482292.6 240 WP_066859835.1 - -
92 로도코커스 sp. PBTS 2 241 AMY55468.1 + +
93 마이콜리시박테리움 스메그마티스 242 WP_058127019.1 - +
94 마이코박테로이데스 sp. H092 243 WP_070928686.1 - +
95 마이코박테리움 콜롬비엔스 244 WP_064951073.1 + +
96 마이코박테리움 sp. TKK-01-0059 245 OBH69834.1 - -
97 마이코박테리움 아바지컴 246 SOX51546.1
98 마이코박테리움 플로렌티넘 247 WP_085225350.1 - +
99 마이코박테리움 유로파움 248 ORV62949.1
100 마이코박테리움 sp. E1319 249 OBH23094.1 - ++
101 마이코박테리움 아로시엔스 ATCC BAA-1401 = DSM 45069 250 ORA19103.1 - -
102 마이콜리시박테리움 리트오랄 251 AQT80557.1 - +
103 마이코박테리움 sp. JS623 252 WP_015304658.1
104 칸디다 알비칸스 SC5314 253 KGU19302.1 - -
105 마이코박테리움 sp. JS623 254 WP_015306631.1 ++ ++
106 노카르디아 브라실리엔시스 ATCC 700358 255 AFU02004.1 + -
107 세그닐리파루스 루고수스 ATCC BAA-974 256 WP_007468889.1 - +
108 노카르디아 sp. Y48 257 AHH98121.1
109 마이콜리시박테리움 반바알레니이 PYR-1 258 WP_042264421.1 + -
110 마이콜리시박테리움 팔락스 259 WP_067876059.1 + +
111 브레비박테리움 카세이 260 WP_082829042.1 + ++
112 마이셀리게네란스 크실리고우엔스 261 WP_123814706.1 + +
113 마이콜리시박테리움 라체렌스 262 WP_133759136.1 + ++
114 로도코커스 파시안스 D188 263 AMY55468.1 + ++
115 마이코박테로이데스 앱세수스 아종 앱세수스 264 WP_005082584.1
활성 범례
　 ΔF/분
- 활성이 전혀 내지 거의 없음
+ 활성; 0.1-1
++ 활성; 1-100
+++ 활성; 100-500
++++ 활성; > 500
ND 검출 안함
실시예 5. CAR 상동체에 대한 생체내 분석.
생체내 CAR 상동체들의 활성을 검사하기 위해, 선택한 CAR 상동체를 코딩하는 유전자들을, 1) 3-옥소아디필-CoA 티올라제 (Thl), 2) 3-옥소아디필-CoA 데하이드로게나제 (Hbd), 3) 3-옥소아디필-CoA 데하이드라타제 ("크로토나제" 또는 Crt), 4) 5-카르복시-2-펜테노일-CoA 리덕타제 (Ter); 및 5) 알데하이드 데하이드로게나제 (Ald), 6) 6ACA 트랜스아미나제 (TA), 및 7) HMD-트랜스아미나제 (TA2)를 코딩하는 도입된 유전자를 또한 포함하는 E. coli 균주에 형질전환하였다. Thl, Hbd, Crt, Ter, Ald 유전자들은 US 8,377,680 (예, 실시예 8, 그 전체가 원용에 의해 본 명세서에 포함됨)에 언급되어 있다. 이들 유전자는 CAR 효소를 제외한 HMD 생산에 필수적인 경로 효소들을 모두 함유한 E. coli 균주에 도입된다.
CAR 유전자를 발현하는 벡터를 Thl/Hbd/Crt/Ter/Ald/TA/TA2 E. coli 균주에 형질전환하였으며, 형질전환체를 HMD 생산에 대해 검사하였다. 조작된 E. coli 세포에는 최소 배지 하에 2% 글루코스를 제공하였으며, 35℃에서 18시간 동안 인큐베이션한 다음 세포를 회수하고, 상층액을 분석용 HPLC 또는 표준 LC/MS 분석 방법을 통해 HMD 생산을 평가하였다. 표 8 및 표 9에 나타낸 바와 같이, Thl, Hbd, Crt, Ter, Ald, TA 및 TA2 유전자를 가진 E. coli에서 CAR 효소를 코딩하는 유전자의 발현으로, 이들 균주에서 HMD 생산이 달성되었다.
실시예 6. CAR 변이체.
단백질의 결정 구조를 조사함으로써, CAR 상동체 4 (서열번호 153) 및 CAR 상동체 105 (서열번호 254)에서, 아미노산의 돌연변이 위치를 동정하였으며, 서열번호 153 및 254를 코딩하는 유전자에 대해 선택 아미노산 위치에서 포화 돌연변이 유발을 수행하였다. 수득한 변이체들을 대상으로 실시예 4에 기술한 바와 같이 세포용해물 분석으로 활성을 검사하였다. 기질 8종에 대한 CAR 서열번호 153의 결과를 도 11에 나타낸다.
CAR 효소 (서열번호 153 및 254)를 코딩하는 유전자를 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929 아미노산 위치에서 돌연변이 유발하여 변이체를 구축하였다. 돌연변이는 단독으로, 그리고 다른 아미노산 위치에서의 돌연변이와 조합하여 수행하였다. 아미노산 위치들에서 돌연변이는 축중 프라이머 서열 및 PCR을 이용해 수행하였으며, 변이된 유전자 서열 혼합물을 E. coli에 형질전환하였다. 형질전환체는 실시예 4에 기술된 바와 같이 세포용해물 분석으로 검사하였다. 분석에서 활성이 확인된 세포용해물의 기원 클론에 대해 트리플리케이트 세포용해물 분석으로 다시 검사하였다. 활성이 계속 검증된 클론들은 함유된 CAR 유전자의 서열을 분석하기 위해 준비하였다.
표 9 및 도 12는 활성 클론들의 변이체 CAR 유전자 서열에서 발견된 돌연변이들을 나타낸다. 야생형 활성보다 높은 것으로 확인된 변이체들은 CAR 유전자 내 단일 돌연변이 및 조합 (다중) 돌연변이를 포함하였다. 표 9는, 변이체의 기원이 되는 야생형 CAR에 비해 활성이 우수한 복수의 변이체를 생성하는, 아미노산 위치 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929 (위치는 서열번호 152를 기준으로 식별)에 돌연변이가 존재하는, 야생형 CAR (서열번호 152)보다 활성이 우수한 것으로 입증된 복수의 변이체들을 나타낸다.
표 9. CAR 변이체
상동체 4 (서열번호 153)에 대한 변이체들
변이체 # 상동체 4 대비 아미노산 치환 활성 6ACA 생체내 HMD 생산
없음 ++ +
1 N335E +++ +
2 N335D +++ +
3 S274D ++ +
4 S274E ++
5 K275D ++
6 K275E ++
7 S299D ++++ +
8 S299E +++
9 M389D ++++ +
10 M389E +++
11 G414D +++ +
12 G414E +++ +
13 G421D ++
14 G421E ++
15 M422D +++ +
16 M422E ++
17 F425D ++
18 F425E ++
19 N335D A282P +++
20 N335D A282V +++
21 N335D A283C ++++
22 N335D A283C F929L +++
23 N335D A283C G636D +++
24 N335D A283G +++
25 N335D F278A ++++
26 N335D F278C +++
27 N335D F278S ++++
28 N335D F278V ++++
29 N335D G279V +++
30 N335D I247M ++++
31 N335D I247Q +++
32 N335D I247T ++++
33 N335D I247V +++
34 N335D I300C +++
35 N335D I300G +++
36 N335D I300M +++
37 N335D I300M +++
38 N335D I300Y +++
39 N335D K275A +++
40 N335D K275D +++
41 N335D K275D +++
42 N335D K275E +++
43 N335D K275M +++
44 N335D K275N ++++
45 N335D K275S +++
46 N335D K275T +++
47 N335D K275V +++
48 N335D K275W +++
49 N335D L245C +++
50 N335D L245G +++
51 N335D L245S +++
52 N335D L245T ++++
53 N335D L245V ++++
54 N335D M389I +++
55 N335D M389W +++
56 N335D M422D +++
57 N335D N276S +++
58 N335D N279 INSERT +++
59 N335D P141G +++
60 N335D S299D ++++
61 N335D S299E +++
62 N335D S391G +++
63 N335D W270M +++
64 K275D N276S F278S A283C N335D ++++
65 L245V K275D N276S F278S A283C N335D ++++
66 I247M K275D N276S F278A A283C N335D ++++
67 L245V K275T N276S F278S A283C N335D ++++
68 I247M K275T N276S F278S A283C N335D ++++
69 K275D N276S F278S A283C I300G N335D ++++ +
70 L245T K275D N276S F278A A283C N335D ++++
71 K275N F278S A283C S299D N335D ++++
72 I247M K275N N276S F278S A283C N335D ++++
73 K275N F278S A283C I300G N335D ++++
74 K275N N276S F278S A283C I300G N335D ++++
75 I247M K275T F278S A283C N335D ++++
76 L245V K275D N276S F278A A283C N335D ++++
77 K275N F278S A283C I300G N335D ++++
78 K275N F278A A283C S299D N335D ++++
79 K275N N276S F278A A283C N335D ++++
80 L245V K275N N276S F278S A283C I300G N335D ++++
81 L245T K275N N276S F278S A283C I300G N335D ++++
82 K275N F278A S299D N335D ++++
83 I247M K275N F278A A283C I300Y N335D ++++
84 I247M K275N F278A A283C N335D ++++
85 K275D N276S F278A N335D ++++
86 K275T F278A A283C S299D N335D ++++
87 F278A A282P N335D ++++
88 F278A A283C N335D ++++
89 K275N S299D N335D ++++
90 L245T S299D N335D ++++
91 K275D S299D N335D ++++
92 K275N F278S N335D ++++
93 S299D M389W N335D ++++
94 G279V S299D N335D ++++
95 F278A S283C N335D ++++
96 K275D N276S N335D ++++
97 G279V S299E N335D ++++
98 I247M S299D N335D ++++
99 P141G A282P N335D ++++
100 L245T A282P N335D ++++
101 F278S A283C N335D ++++
102 K275D S284I S299D N335D ++++
103 I247M I282P N335D ++++
104 I247V K275D N276S F278S A283C I300G N335D ++++
105 K275D S274C N276S F278S A283C I300G N335D ++++
106 K275D S274A N276S F278S A283C I300G N335D ++++
107 K275D S274P N276S F278S A283C I300G N335D ++++
108 K275D N276S F278S A282F A283C I300G N335D ++++
109 K275D N276S F278S A282P A283C I300G N335D ++++
110 K275D N276S F278S A283C S299I I300G N335D ++++
111 K275D N276S F278S A283C I300G N335D M389C ++++
112 K275D N276S F278S A283C I300G N335D M389Y ++++
113 K275D N276S F278S A283C I300G N335D M389S ++++
상동체 105에 대한 변이체
변이체 # 상동체 105 대비 돌연변이 활성 6ACA 생체내 HMD 생산
없음 ++ +
114 S336E +++ +
115 S336D +++ +
표 10은 상동체 4의 245, 247, 274, 275, 276, 278, 282, 283, 299, 300 및 389번 위치들에서 돌연변이들의 조합으로, 고유한 조합 총 165,888개를 생성할 수 있음을 보여준다. 조합 돌연변이들은 상동체 4의 N335D에 추가된다.
표 10. 상동체 4 (서열번호 153)의 CAR 변이체들의 조합 돌연변이
위치 # 위치 WT 돌연변이 총
1 245 L T, V 3
2 247 I M, T, V 4
3 274 S C, A, P 4
4 275 K D, N, T 4
5 276 N S 2
6 278 F S, A 3
7 282 A F, P 3
8 283 A C 2
9 299 S D, I 2
10 300 I G, Y 3
11 389 M C, Y, S 4
고유한 조합 총수 　 　 　 165,888
실시예 7. 6- 아미노카프로에이트 세미알데하이드에 대해 활성을 가진 TA2 트랜스아미나제의 동정
실시예 1에 기술된 바와 같이, TA2 트랜스아미나제를 코딩하는 유전자를 동정하여 검사하였다.
표 11은 서열번호 265 및 267-296을 가진 TA2 상동체들은 6-아미노카프로에이트 세미알데하이드를 HMD로 변환하는 활성을 발휘함을 보여준다.
표 11. TA2 상동체
Figure pct00001
실시예 8. 아디필 - CoA에 대한 활성에 대해 다양한 미생물 소스로부터 알데하이드 데하이드로게나제 스크리닝
다양한 종으로부터 알데하이드 데하이드로게나제 (ALD)를 코딩하는 유전자를 복수의 종들의 게놈에서 생물정보학적 방식으로 동정하였다 (표 4). 각 알데하이드 데하이드로게나제를 코딩하는 유전자를 합성하여 E. coli에서 발현시킨 후 ALD 활성에 대해 평가하였다.
표 12의 ALD 효소 후보를 코딩하는 유전자들을 저 카피수 벡터에 구성적 프로모터 하에 클로닝하고, 구조체를 표준 기법을 이용해 E. coli에 형질전환하였다. 형질전환체를 항생제 존재 하에 LB 배지에서 밤새 35℃에서 배양한 다음 세포를 15,000 rpm으로 실온에서 회수하였다. 세포용해물을 제조하기 위해, 세포를 리소자임, 뉴클레아제 및 10 mM DTT가 함유된 화학적 세포용해 용액에 재현탁하여, 실온에서 적어도 30분간 인큐베이션하였다. 수득한 세포용해물을 이용해 알데하이드 데하이드로게나제 활성을 검사하였다.
세포용해물 (5 ㎕)을 분석 혼합물에 첨가하여, 최종 농도 0.1 M Tris-HCl, pH 7.5, 2.5 mM 아디필-CoA (AdCoA) 및 0.5 mM NADH 또는 0.5 mM NADPH의 총 부피 20 ㎕를 수득하였다.
본 분석을 이용해 다양한 종들의 ALD 효소를 스크리닝하였다. 일부 ALD 후보 역시 기질로서 숙시닐-CoA (SuCoA) 또는 아세틸-CoA (AcCoA)를 이용해 분석하였다. AdCoA, SuCoA 및 AcCoA는 시판 공급처로부터 입수하였다. CoA 기질 존재 하에 NADH 또는 NADPH의 선형적인 형광 감소에 의해 활성을 모니터링하였다. NADH 또는 NADPH 이용시 아디필-CoA에 대한 활성이 현저한 ALD는 표 4에 양성 (+)으로 표시하고, 활성이 거의 내지 전혀 없는 것은 음성 (-)으로 표시하였다.
SEQUENCE LISTING <110> GENOMATICA, INC. <120> ENGINEERED ENZYMES AND METHODS OF MAKING AND USING <130> 14620-492-228 <140> <141> <150> US 63/015,428 <151> 2020-04-24 <160> 370 <170> PatentIn version 3.5 <210> 1 <211> 421 <212> PRT <213> Artificial Sequence <220> <223> Achromobacter xylosoxidans <400> 1 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Asn Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Ile Lys Ala Ala 50 55 60 Val Ala Ala Gln Leu Asp Asn Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Val Ser Leu Ala Glu Arg Ile Asn Arg Leu Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Ser Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ala Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Thr Gln Ser 165 170 175 Ile Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Cys 180 185 190 Asp Ile Asp Pro Lys Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ala Met Glu His His 245 250 255 Ser Val Gln Ala Asp Leu Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Val Val Gly Arg Ala Asp Val Met Asp Ala Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Asp Ala Leu Gly Asp Lys Leu Arg Ala His Leu Glu Gly 325 330 335 Leu Arg Ala Lys Val Pro Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Pro Ala Thr Gly Lys Pro Asp Ala 355 360 365 Glu Ala Val Lys Arg Val Gln Ala Arg Ala Ile Glu Lys Gly Leu Ile 370 375 380 Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro 385 390 395 400 Leu Thr Ile Pro Asp Ala Gln Phe Asp Arg Ala Leu Ala Ile Leu Ser 405 410 415 Glu Ala Leu Ala Ala 420 <210> 2 <400> 2 000 <210> 3 <211> 426 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 3 Met Phe Ile Glu Ala Glu Met Lys Asn Gln Asp Leu Asn Thr Arg Arg 1 5 10 15 Ser Leu Ala Thr Pro Arg Gly Val Gly Val Met Cys Asp Phe Tyr Ala 20 25 30 Val Arg Ala Glu Asn Ala Thr Leu Trp Asp Ala Asn Gly Lys Glu Tyr 35 40 45 Ile Asp Phe Ala Gly Gly Ile Ala Val Leu Asn Thr Gly His Leu His 50 55 60 Pro Lys Val Lys Ala Ala Val Ala Ala Gln Leu Asp Asn Phe Thr His 65 70 75 80 Thr Ala Tyr Gln Ile Val Pro Tyr Glu Ser Tyr Ile Ser Leu Ala Glu 85 90 95 Arg Ile Asn Arg Leu Ala Pro Ile Asp Gly Leu Lys Lys Thr Ala Phe 100 105 110 Phe Thr Thr Gly Val Glu Ala Val Glu Asn Ala Ile Lys Ile Ala Arg 115 120 125 Ser Ser Thr Gly Arg Ser Gly Val Ile Ala Phe Ser Gly Ser Phe His 130 135 140 Gly Arg Thr Met Leu Gly Met Ala Leu Thr Gly Lys Val Ala Pro Tyr 145 150 155 160 Lys Leu Ser Phe Gly Pro Met Pro Gly Asp Ile Tyr His Val Pro Phe 165 170 175 Pro Asn Ala Thr Gln Ala Ile Ser Val Ala Asp Ser Leu Lys Ala Leu 180 185 190 Asp Leu Leu Phe Lys Cys Asp Ile Asp Pro Lys Arg Val Ala Ala Ile 195 200 205 Ile Ile Glu Pro Val Gln Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro 210 215 220 Glu Leu Met Thr Ala Leu Arg Lys Ile Cys Asp Glu His Gly Ile Leu 225 230 235 240 Leu Ile Ala Asp Glu Val Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu 245 250 255 Tyr Ala Met Glu His His Ser Val Gln Ala Asp Leu Ile Thr Met Ala 260 265 270 Lys Ser Leu Gly Gly Gly Phe Pro Ile Ser Gly Val Val Gly Arg Ala 275 280 285 Asp Val Met Asp Gly Pro Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala 290 295 300 Gly Asn Pro Leu Ala Val Ala Ala Ala His Ala Val Leu Asp Val Ile 305 310 315 320 Ala Glu Glu Lys Leu Cys Asp Arg Ala Asn Val Leu Gly Glu Lys Leu 325 330 335 Arg Ala His Leu Glu Gly Leu Arg Ala Lys Val Pro Gly Ile Ala Asp 340 345 350 Val Arg Gly Leu Gly Ser Met Val Ala Leu Glu Leu Asn Asp Ala Ser 355 360 365 Gly Lys Pro Asp Ala Glu Ala Val Lys Arg Val Gln Ala Arg Ala Leu 370 375 380 Glu Gln Gly Leu Ile Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Leu 385 390 395 400 Arg Phe Leu Tyr Pro Leu Thr Ile Pro Asp Ala Gln Phe Asp Arg Ala 405 410 415 Leu Ala Ile Leu Ser Asp Ala Leu Ala Ala 420 425 <210> 4 <211> 446 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 4 Met Val His Leu Arg Ala Ala Thr Arg Thr Ser Cys Thr Pro Val Leu 1 5 10 15 Thr Pro Ser Leu Thr Trp Arg Ser Ala Met Lys Asn Met Asp Leu Asp 20 25 30 Thr Arg Arg Ser Leu Ala Thr Pro Arg Gly Val Gly Val Ala Tyr Ser 35 40 45 Val Tyr Ala Val Arg Ala Glu Asn Ala Thr Ile Trp Asp Ala Asp Gly 50 55 60 Lys Glu Tyr Ile Asp Phe Ala Gly Gly Ile Ala Val Leu Asn Thr Gly 65 70 75 80 His Arg His Pro Lys Val Lys Ala Ala Ile Ala Ala Gln Leu Glu Cys 85 90 95 Phe Thr His Thr Ala Tyr Gln Ile Ile Pro Tyr Glu Pro Tyr Val Ala 100 105 110 Leu Ala Glu Arg Leu Asn Lys Ile Ala Pro Ile Asp Gly Leu Lys Lys 115 120 125 Thr Ala Phe Phe Thr Thr Gly Ala Glu Ala Val Glu Asn Ala Ile Lys 130 135 140 Ile Ala Arg Ala Tyr Thr Lys Arg Thr Gly Val Ile Ala Phe Ser Gly 145 150 155 160 Ala Phe His Gly Arg Thr Leu Leu Gly Met Ala Leu Thr Gly Lys Val 165 170 175 Ala Pro Tyr Lys Val Asp Phe Gly Ala Met Pro Pro Asp Ile Phe His 180 185 190 Ala Pro Phe Pro Asn Thr Thr Gln Asp Ile Ser Val Ala Asp Ala Leu 195 200 205 Lys His Leu Glu Leu Leu Phe Lys Val Asp Ile Asp Pro Lys Arg Val 210 215 220 Ala Ala Ile Ile Ile Glu Pro Val Gln Gly Glu Gly Gly Phe Asn Pro 225 230 235 240 Ala Pro Ala Glu Leu Met Thr Ala Leu Arg Arg Ile Cys Asp Glu His 245 250 255 Gly Ile Val Leu Ile Ala Asp Glu Val Gln Thr Gly Phe Ala Arg Thr 260 265 270 Gly Lys Leu Phe Ala Met Gln His Tyr Asp Val Gln Pro Asp Met Met 275 280 285 Thr Val Ala Lys Ser Leu Ala Gly Gly Met Pro Leu Ser Gly Val Ile 290 295 300 Gly Arg Ala Glu Ile Met Asp Ala Pro Asn Pro Gly Gly Leu Gly Gly 305 310 315 320 Thr Tyr Ala Gly Asn Ala Leu Ala Leu Ala Ser Ala His Ala Val Leu 325 330 335 Asp Val Ile Glu Glu Glu Gln Leu Cys Ala Arg Ala Glu Thr Leu Gly 340 345 350 Gln Arg Leu Arg Asp Arg Leu Thr Ala Leu Lys Gly Thr Val Pro Ala 355 360 365 Leu Gly Glu Val Arg Gly Pro Gly Ser Met Val Ala Val Glu Met Asn 370 375 380 Asp Pro Ala Thr Gly Lys Pro Asp Ala Glu Ala Val Lys Arg Val Gln 385 390 395 400 Ala Arg Ala Leu Ala Gln Gly Leu Ile Leu Ile Thr Cys Gly Val Tyr 405 410 415 Gly Asn Val Leu Arg Phe Leu Tyr Pro Leu Thr Ile Pro Asp Ala Gln 420 425 430 Phe Asp Arg Ala Leu Asp Ile Leu Ala Asp Ala Ile Thr Ala 435 440 445 <210> 5 <211> 456 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 5 Met Thr Thr Thr Ala Ala Asp Ile Thr Tyr Arg Leu Glu Gln Lys Arg 1 5 10 15 Arg Val Gln Ala Asp Phe Pro Gly Pro Lys Ser Val Ala Leu Thr Glu 20 25 30 Arg Arg Lys Ser Val Val Ala Ala Gly Val Ala Ser Ser Val Pro Val 35 40 45 Tyr Val Ala Asp Ala Asp Gly Gly Ile Ile Gln Asp Val Asp Gly Asn 50 55 60 Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala 65 70 75 80 Ser Asp Pro Ala Val Val Gly Ala Val Lys Glu Ala Val Glu His Phe 85 90 95 Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala Val 100 105 110 Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Glu Lys Arg Thr 115 120 125 Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val Lys Val 130 135 140 Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His Ala 145 150 155 160 Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala Met 165 170 175 Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg Met 180 185 190 Pro Met Ser Tyr Pro Tyr Arg Glu Glu Asn Pro Ser Ile Thr Gly Ala 195 200 205 Glu Ala Ala Lys Arg Ala Ile Thr Ala Ile Glu Lys Gln Ile Gly Gly 210 215 220 Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly Gly 225 230 235 240 Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ala Ala Trp Ala 245 250 255 Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly Phe 260 265 270 Cys Arg Thr Gly Glu Trp Phe Ala Val Asn His Glu Gly Val Ile Pro 275 280 285 Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Met Pro Leu Ser 290 295 300 Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly Gly 305 310 315 320 Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu 325 330 335 Ala Ser Ile Gly Ser Met Glu Glu Tyr Gly Leu Asn Ala Arg Ala Lys 340 345 350 His Ile Glu Glu Leu Ala Thr Thr Arg Leu Ser Ala Leu Gln Glu Glu 355 360 365 Leu Ala Gly Ala Gly Ser Ala Val Ile Gly Asp Ile Arg Gly Arg Gly 370 375 380 Ala Met Leu Ala Ile Glu Leu Val His Ala Gly Ser Lys Glu Pro Asn 385 390 395 400 Pro Glu Leu Thr Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val 405 410 415 Ile Ile Leu Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro 420 425 430 Pro Leu Val Ile Thr Asp Glu Leu Leu Asn Asp Gly Leu Asp Val Leu 435 440 445 Ala Ala Ala Ile Lys Ala Asn Ala 450 455 <210> 6 <400> 6 000 <210> 7 <400> 7 000 <210> 8 <400> 8 000 <210> 9 <211> 451 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 9 Met Thr Thr Thr Ala Asn Glu Leu Ser Tyr Arg Ile Glu Gln Lys Arg 1 5 10 15 Asn Ile Asn Gly Ala Phe Pro Gly Pro Lys Ser Gln Ala Leu Ala Glu 20 25 30 Arg Arg Ala Ala Val Val Ala Ala Gly Val Ala Ser Gly Val Pro Val 35 40 45 Tyr Val Glu Asp Ala Asp Gly Gly Ile Val Arg Asp Val Asp Gly Asn 50 55 60 Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala 65 70 75 80 Ser Asp Pro Ala Val Val Ala Ala Val Gln Glu Ala Ala Ala His Phe 85 90 95 Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala Val 100 105 110 Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Ala Lys Arg Thr 115 120 125 Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val Lys Val 130 135 140 Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His Ala 145 150 155 160 Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala Met 165 170 175 Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg Met 180 185 190 Pro Met Ser Tyr Pro Phe Arg Glu Glu Asn Pro Glu Ile Thr Gly Ala 195 200 205 Glu Ala Ala Lys Arg Ala Ile Thr Met Ile Glu Lys Gln Ile Gly Gly 210 215 220 Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly Gly 225 230 235 240 Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ser Ala Trp Ala 245 250 255 Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly Phe 260 265 270 Cys Arg Thr Gly Glu Trp Phe Ala Val Asp His Glu Gly Val Val Pro 275 280 285 Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Leu Pro Leu Ser 290 295 300 Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly Gly 305 310 315 320 Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu 325 330 335 Ala Ala Ile Asp Thr Met Glu Gln His Asp Leu Asn Gly Arg Ala Arg 340 345 350 His Ile Glu Glu Leu Ala Leu Gly Lys Leu Arg Glu Leu Ala Asp Glu 355 360 365 Val Ser Val Val Gly Asp Ile Arg Gly His Gly Ala Met Leu Ala Ile 370 375 380 Glu Leu Val Gln Ser Gly Ser Lys Glu Pro Asn Ala Glu Leu Thr Lys 385 390 395 400 Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val Ile Ile Leu Thr Cys 405 410 415 Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro Pro Leu Val Ile Ser 420 425 430 Asp Glu Leu Leu Ile Asp Gly Leu Glu Val Leu Ala Ala Ala Ile Lys 435 440 445 Ala His Ala 450 <210> 10 <400> 10 000 <210> 11 <400> 11 000 <210> 12 <211> 456 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 12 Met Thr Ala Thr Ala Ser Glu Ile Thr Tyr Arg Leu Glu Gln Lys Arg 1 5 10 15 Arg Val Gln Ala Asp Phe Pro Gly Pro Lys Ser Ala Ala Leu Thr Glu 20 25 30 Arg Arg Lys Ser Val Val Ala Ala Gly Val Ala Ser Ser Val Pro Val 35 40 45 Tyr Val Ala Asp Ala Asp Gly Gly Ile Ile His Asp Val Asp Gly Asn 50 55 60 Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala 65 70 75 80 Ser Asp Pro Ala Val Val Gly Ala Val Lys Glu Ala Val Glu His Phe 85 90 95 Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala Val 100 105 110 Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Glu Lys Arg Thr 115 120 125 Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Ile Lys Val 130 135 140 Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His Ala 145 150 155 160 Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala Met 165 170 175 Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg Met 180 185 190 Pro Met Ser Tyr Pro Tyr Arg Glu Glu Asn Pro Ala Ile Thr Gly Ala 195 200 205 Glu Ala Ala Lys Arg Ala Ile Thr Met Ile Glu Lys Gln Ile Gly Gly 210 215 220 Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly Gly 225 230 235 240 Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ala Ala Trp Ala 245 250 255 Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly Phe 260 265 270 Cys Arg Thr Gly Glu Trp Phe Ala Val Asn His Glu Gly Ile Val Pro 275 280 285 Asp Ile Met Thr Met Ala Lys Gly Ile Ala Gly Gly Met Pro Leu Ser 290 295 300 Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly Gly 305 310 315 320 Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu 325 330 335 Ala Ser Ile Gly Ser Met Glu Glu Tyr Asp Leu Ala Gly Arg Ala Arg 340 345 350 His Ile Glu Ala Leu Ala Thr Gly Arg Leu Arg Glu Leu Gln Ala Glu 355 360 365 Leu Ala Asp Ala Gly Thr Ala Val Ile Gly Asp Val Arg Gly Arg Gly 370 375 380 Ala Met Leu Ala Ile Glu Leu Val Gln Ala Gly Ser Lys Glu Pro Asn 385 390 395 400 Pro Glu Leu Thr Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val 405 410 415 Ile Ile Leu Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro 420 425 430 Pro Leu Val Ile Thr Asp Glu Leu Leu Asn Asp Gly Leu Asp Val Leu 435 440 445 Ala Ala Ala Ile Lys Ala Asn Ala 450 455 <210> 13 <211> 456 <212> PRT <213> Artificial Sequence <220> <223> Paenarthrobacter aurescens TC1 <400> 13 Met Thr Thr Thr Ala Asn Glu Leu Ser Tyr Arg Ile Glu Gln Lys Arg 1 5 10 15 Asn Ile Asn Gly Ala Phe Pro Gly Pro Lys Ser Gln Ala Leu Ala Glu 20 25 30 Arg Arg Ser Ala Val Val Ala Ala Gly Val Ala Ser Gly Val Pro Val 35 40 45 Tyr Val Glu Asp Ala Asp Gly Gly Ile Ile Arg Asp Val Asp Gly Asn 50 55 60 Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala 65 70 75 80 Ser Asp Pro Ala Val Val Ala Ala Val Gln Glu Ala Ala Ala His Phe 85 90 95 Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala Val 100 105 110 Thr Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Ala Lys Arg Thr 115 120 125 Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val Lys Val 130 135 140 Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His Ala 145 150 155 160 Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala Met 165 170 175 Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg Met 180 185 190 Pro Met Ser Tyr Pro Phe Arg Glu Glu Asn Pro Glu Ile Thr Gly Ala 195 200 205 Glu Ala Ala Lys Arg Ala Ile Thr Met Ile Glu Lys Gln Ile Gly Gly 210 215 220 Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly Gly 225 230 235 240 Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ser Glu Trp Ala 245 250 255 Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly Phe 260 265 270 Cys Arg Thr Gly Glu Trp Phe Ala Val Asp His Glu Gly Val Val Pro 275 280 285 Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Leu Pro Leu Ser 290 295 300 Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly Gly 305 310 315 320 Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu 325 330 335 Ala Ala Ile Asp Thr Met Glu Gln His Asp Leu Asn Gly Arg Ala Arg 340 345 350 His Ile Glu Glu Leu Ala Leu Gly Lys Leu Arg Glu Leu Ala Ala Glu 355 360 365 Leu Ser Ala Gly Gly Gly Ser Val Val Gly Asp Ile Arg Gly Arg Gly 370 375 380 Ala Met Leu Ala Ile Glu Leu Val Gln Pro Gly Ser Lys Glu Pro Asn 385 390 395 400 Ala Glu Leu Thr Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val 405 410 415 Ile Ile Leu Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro 420 425 430 Pro Leu Val Ile Ser Asp Glu Leu Leu Ile Asp Gly Leu Glu Val Leu 435 440 445 Ala Ala Ala Ile Lys Ala His Ala 450 455 <210> 14 <400> 14 000 <210> 15 <211> 425 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 15 Met Ser Lys Thr Asn Ala Ser Leu Met Lys Arg Arg Glu Ala Ala Val 1 5 10 15 Pro Arg Gly Val Gly Gln Ile His Pro Ile Phe Ala Glu Ser Ala Lys 20 25 30 Asn Ala Thr Val Thr Asp Val Glu Gly Arg Glu Phe Ile Asp Phe Ala 35 40 45 Gly Gly Ile Ala Val Leu Asn Thr Gly His Val His Pro Lys Ile Ile 50 55 60 Ala Ala Val Thr Glu Gln Leu Asn Lys Leu Thr His Thr Cys Phe Gln 65 70 75 80 Val Leu Ala Tyr Glu Pro Tyr Val Glu Val Cys Glu Lys Ile Asn Ala 85 90 95 Lys Val Pro Gly Asp Phe Ala Lys Lys Thr Leu Leu Val Thr Thr Gly 100 105 110 Ser Glu Ala Val Glu Asn Ser Ile Lys Ile Ala Arg Ala Ala Thr Gly 115 120 125 Arg Ala Gly Val Ile Ala Phe Thr Gly Ala Tyr His Gly Arg Thr Met 130 135 140 Met Thr Leu Gly Leu Thr Gly Lys Val Val Pro Tyr Ser Ala Gly Met 145 150 155 160 Gly Leu Met Pro Gly Gly Ile Phe Arg Ala Leu Tyr Pro Asn Glu Leu 165 170 175 His Gly Val Ser Ile Asp Asp Ser Ile Ala Ser Ile Glu Arg Ile Phe 180 185 190 Lys Asn Asp Ala Glu Pro Arg Asp Ile Ala Ala Ile Ile Ile Glu Pro 195 200 205 Val Gln Gly Glu Gly Gly Phe Tyr Val Ala Pro Lys Glu Phe Met Lys 210 215 220 Arg Leu Arg Ala Leu Cys Asp Gln His Gly Ile Leu Leu Ile Ala Asp 225 230 235 240 Glu Val Gln Thr Gly Ala Gly Arg Thr Gly Thr Phe Phe Ala Met Glu 245 250 255 Gln Met Gly Val Ala Ala Asp Leu Thr Thr Phe Ala Lys Ser Ile Ala 260 265 270 Gly Gly Phe Pro Leu Ala Gly Val Cys Gly Lys Ala Glu Tyr Met Asp 275 280 285 Ala Ile Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Ser Pro Ile 290 295 300 Ala Cys Ala Ala Ala Leu Ala Val Met Glu Val Phe Glu Glu Glu His 305 310 315 320 Leu Leu Asp Arg Cys Lys Ala Val Gly Glu Arg Leu Val Thr Gly Leu 325 330 335 Lys Ala Ile Gln Ala Lys Tyr Pro Val Ile Gly Glu Val Arg Ala Leu 340 345 350 Gly Ala Met Ile Ala Val Glu Leu Phe Val Asp Gly Asp Ser His Lys 355 360 365 Pro Asn Ala Pro Ala Val Ala Ala Val Val Ala Lys Ala Arg Asp Lys 370 375 380 Gly Leu Ile Leu Leu Ser Cys Gly Thr Tyr Gly Asn Val Leu Arg Val 385 390 395 400 Leu Val Pro Leu Thr Ser Pro Asp Glu Gln Leu Asp Lys Gly Leu Ala 405 410 415 Ile Ile Glu Glu Cys Phe Ser Glu Leu 420 425 <210> 16 <400> 16 000 <210> 17 <400> 17 000 <210> 18 <400> 18 000 <210> 19 <400> 19 000 <210> 20 <400> 20 000 <210> 21 <400> 21 000 <210> 22 <400> 22 000 <210> 23 <400> 23 000 <210> 24 <400> 24 000 <210> 25 <400> 25 000 <210> 26 <211> 421 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 26 Val Asn Asn His Glu Leu Asn Glu Arg Arg Leu Gln Ala Thr Pro Arg 1 5 10 15 Gly Ile Gly Val Met Cys Gly Phe Tyr Ala Asp Lys Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ile Glu Gly Asn Glu Val Ile Asp Phe Ala Ala Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Arg His Pro Lys Val Ile Ala Ala 50 55 60 Ile Glu Lys Gln Leu Gln Ser Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Ile Ala Leu Ala Glu Arg Ile Asn Ala Arg Val 85 90 95 Pro Ile Glu Gly Pro Ala Lys Thr Ala Phe Phe Ser Thr Gly Ala Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ala Tyr Thr Lys Arg Pro 115 120 125 Gly Leu Ile Thr Phe Gly Gly Ala Phe His Gly Arg Thr Phe Met Thr 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Gly Phe Gly Pro 145 150 155 160 Phe Pro Gly Ser Val Tyr His Ala Gln Tyr Pro Asn Thr Leu His Gly 165 170 175 Val Ser Ser Gln Asp Ala Leu Lys Ser Leu Glu Arg Ile Phe Lys Ala 180 185 190 Asp Ile Ala Pro Asp Gln Val Ala Ala Ile Ile Leu Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Val Ala Pro Pro Asp Phe Met Gln Gly Leu 210 215 220 Arg Ala Leu Cys Asp Thr His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Ala Arg Thr Gly Lys Leu Phe Ser Met Glu His His 245 250 255 Cys Val Lys Pro Asp Leu Ile Thr Met Ala Lys Ser Leu Ala Gly Gly 260 265 270 Met Pro Leu Ser Ala Val Ser Gly Arg Ala Glu Val Met Asp Ala Pro 275 280 285 Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Ile 290 295 300 Ala Ala Ala Leu Ala Val Leu Asp Val Ile Asp Glu Glu Asp Leu Cys 305 310 315 320 Ala Arg Ala Ser His Leu Gly His His Leu Val Glu Val Leu Ser Lys 325 330 335 Ala Lys Ser Gly Cys Pro Tyr Ile Ala Asp Ile Arg Ala Gln Gly Ser 340 345 350 Met Val Ala Val Glu Phe Asn Asp Pro Glu Thr Gly Gln Pro Ser Pro 355 360 365 Glu Phe Thr Arg Gln Val Gln Glu Arg Ala Leu Ala Glu Gly Leu Leu 370 375 380 Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Ile Arg Phe Leu Tyr Pro 385 390 395 400 Leu Thr Ile Pro Asp Ala Gln Phe Arg Lys Ala Leu Asp Ile Ile Ser 405 410 415 Ala Ser Leu Thr Arg 420 <210> 27 <211> 457 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 27 Met Thr Ile Leu Glu His Gly Thr Glu Thr Cys Ile Gly Gly Pro Thr 1 5 10 15 Leu Pro Gln Ile Arg Arg Leu Val Thr Glu Val Pro Gly Pro Asn Ser 20 25 30 Arg Ala Leu Ala Lys Arg Arg Ser Ala Ala Leu Pro Ala Gly Leu Thr 35 40 45 Ser Gly Ser Ser Ile Tyr Val Ala Ala Ala Gly Gly Gly Val Val Val 50 55 60 Asp Val Asp Asp Asn Ser Phe Ile Asp Phe Gly Ser Gly Ile Ala Val 65 70 75 80 Thr Thr Val Gly Asn Ser Ala Pro Arg Val Val Glu Arg Thr Thr Arg 85 90 95 Gln Leu Gly Gln Phe Thr His Thr Cys Phe Leu Ala Asn Pro Tyr Glu 100 105 110 Gly Tyr Leu Glu Val Cys Glu Ala Leu Asn Arg Leu Thr Pro Gly Asp 115 120 125 His Glu Lys Arg Thr Ala Leu Phe Asn Thr Gly Ser Glu Ala Leu Glu 130 135 140 Asn Ala Val Lys Tyr Ala Arg Ala Ala Thr Gly Arg Pro Ala Val Val 145 150 155 160 Val Phe Asp His Ala Phe His Gly Arg Thr Leu Met Thr Met Thr Met 165 170 175 Thr Ala Lys Asn Gln Pro Tyr Lys Ala Thr Phe Gly Pro Phe Ala Pro 180 185 190 Glu Val Tyr Arg Val Pro Met Ala Tyr Pro Tyr Arg Trp Pro Ser Gly 195 200 205 Pro Glu Asn Ala Ala Asp Glu Ala Phe Ala Gln Phe Arg Leu Ala Ile 210 215 220 Asp Thr Gln Ile Gly Ala Glu Ser Val Ala Ala Val Val Val Glu Pro 225 230 235 240 Ile Gln Gly Glu Gly Gly Phe Ile Val Pro Ala Pro Gly Phe Leu Lys 245 250 255 Arg Ile Ser Glu Phe Cys Arg Glu Arg Gly Ile Leu Val Val Ala Asp 260 265 270 Glu Val Gln Thr Gly Ile Ala Arg Thr Gly Ser Trp Phe Ala Ser Glu 275 280 285 Ser Glu Asp Phe Val Pro Asp Ile Ile Thr Thr Ala Lys Gly Leu Ala 290 295 300 Gly Gly Met Pro Leu Ala Ala Val Thr Gly Arg Ala Asp Val Met Asp 305 310 315 320 Ala Ala His Pro Gly Gly Ile Gly Gly Thr Tyr Ser Gly Asn Pro Val 325 330 335 Ala Cys Glu Ala Ala Leu Ala Val Phe Glu Thr Ile Glu Met Glu Gly 340 345 350 Leu Leu Asp Arg Ala Lys Asp Ile Gly Asp Ile Leu Thr Thr Gly Leu 355 360 365 Ser Glu Ile Ala Ser Glu Thr Asp Ile Ile Gly Asp Ile Arg Gly Arg 370 375 380 Gly Ala Met Ile Ala Ile Glu Leu Val His Asp Glu Asp Lys Ala Pro 385 390 395 400 Asn Arg Glu Ala Val Ala Gln Ile Val Ser Tyr Ala His Thr His Gly 405 410 415 Leu Leu Leu Leu Thr Ala Gly Thr Tyr Gly Asn Val Val Arg Phe Leu 420 425 430 Pro Pro Leu Ser Ile Ser Asp Glu Leu Leu Thr Glu Gly Leu Gly Ile 435 440 445 Leu Arg Asp Ala Val Ala Ala Val Arg 450 455 <210> 28 <400> 28 000 <210> 29 <400> 29 000 <210> 30 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 30 Met Arg Ser Ala Ser Ala Pro Pro Val Arg Ile Ser Gln Lys Gly Asn 1 5 10 15 His Pro Met Thr Thr Thr Ala Asn Glu Leu Ser Tyr Arg Ile Glu Gln 20 25 30 Lys Arg Asn Ile Asn Gly Ala Phe Pro Gly Pro Lys Ser Gln Ala Leu 35 40 45 Ala Glu Arg Arg Ser Ala Val Val Ala Ala Gly Val Ala Ser Gly Val 50 55 60 Pro Val Tyr Val Glu Asp Ala Asp Gly Gly Ile Ile Arg Asp Val Asp 65 70 75 80 Gly Asn Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val 85 90 95 Gly Ala Ser Asp Pro Ala Val Val Ala Ala Val Gln Glu Ala Ala Ala 100 105 110 His Phe Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val 115 120 125 Ala Val Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Ala Lys 130 135 140 Arg Thr Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val 145 150 155 160 Lys Val Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp 165 170 175 His Ala Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys 180 185 190 Ala Met Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr 195 200 205 Arg Met Pro Met Ser Tyr Pro Phe Arg Glu Glu Asn Pro Glu Ile Thr 210 215 220 Gly Ala Glu Ala Ala Lys Arg Ala Ile Thr Met Ile Glu Lys Gln Ile 225 230 235 240 Gly Gly Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu 245 250 255 Gly Gly Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ser Glu 260 265 270 Trp Ala Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser 275 280 285 Gly Phe Cys Arg Thr Gly Glu Trp Phe Ala Val Asp His Glu Gly Val 290 295 300 Val Pro Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Leu Pro 305 310 315 320 Leu Ser Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro 325 330 335 Gly Gly Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala 340 345 350 Ala Leu Ala Ala Ile Asp Thr Met Glu Gln His Asp Leu Asn Gly Arg 355 360 365 Ala Arg His Ile Glu Glu Leu Ala Leu Gly Lys Leu Arg Glu Leu Ala 370 375 380 Gly Glu Val Ser Val Val Gly Asp Ile Arg Gly Arg Gly Ala Met Leu 385 390 395 400 Ala Ile Glu Leu Val Gln Ser Gly Ser Lys Glu Pro Asn Ala Glu Leu 405 410 415 Thr Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val Ile Ile Leu 420 425 430 Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro Pro Leu Val 435 440 445 Ile Ser Asp Glu Leu Leu Ile Asp Gly Leu Glu Val Leu Ala Ala Ala 450 455 460 Ile Lys Ala His Ala 465 <210> 31 <211> 421 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 31 Met Gln Asn Pro Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Met Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ser Thr Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Arg His Pro Lys Ile Lys Ala Ala 50 55 60 Val Ala Glu Gln Leu Glu Ala Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Ser Tyr Val Ala Leu Ala Glu Arg Ile Asn Gly Leu Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Thr Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ala His Thr Gly Arg Ser 115 120 125 Gly Val Val Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ala Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Gly Thr Gln Asp 165 170 175 Ile Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Ser 180 185 190 Asp Ile Asp Pro Arg Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Ile Cys Asp Glu Tyr Gly Ile Met Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Ala Arg Thr Gly Lys Leu Tyr Ala Met Gln His His 245 250 255 Asp Val Gln Ala Asp Leu Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Val Val Gly Arg Ala Glu Val Met Asp Gly Pro 275 280 285 Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Glu Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Ala Glu Leu Gly Gln Arg Leu Gln Glu Arg Leu Asn Gly 325 330 335 Leu Arg Pro Gln Cys Pro Ala Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Arg Asp Pro Ala Thr Gly Gln Pro Asp Ala 355 360 365 Ala Ala Val Lys Arg Val Gln Asp Ala Ala Ile Glu Arg Gly Leu Ile 370 375 380 Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro 385 390 395 400 Leu Thr Ile Pro Asp Glu Gln Phe Ala Arg Ala Leu Asp Ile Leu Ser 405 410 415 Asp Ile Leu Thr Ala 420 <210> 32 <400> 32 000 <210> 33 <400> 33 000 <210> 34 <400> 34 000 <210> 35 <400> 35 000 <210> 36 <211> 425 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 36 Met Ser Lys Thr Asn Ala Ser Leu Met Lys Arg Arg Glu Ala Ala Val 1 5 10 15 Pro Arg Gly Val Gly Gln Ile His Pro Ile Phe Ala Glu Ser Ala Lys 20 25 30 Asn Ala Thr Val Thr Asp Val Glu Gly Arg Glu Phe Ile Asp Phe Ala 35 40 45 Gly Gly Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Ile Ile 50 55 60 Ala Ala Val Thr Glu Gln Leu Asn Lys Leu Thr His Thr Cys Phe Gln 65 70 75 80 Val Leu Ala Tyr Glu Pro Tyr Val Glu Leu Cys Glu Lys Ile Asn Ala 85 90 95 Lys Val Pro Gly Asp Phe Ala Lys Lys Thr Leu Leu Val Thr Thr Gly 100 105 110 Ser Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ala Ala Thr Gly 115 120 125 Arg Ala Gly Val Ile Ala Phe Thr Gly Ala Tyr His Gly Arg Thr Met 130 135 140 Met Thr Leu Gly Leu Thr Gly Lys Val Val Pro Tyr Ser Ala Gly Met 145 150 155 160 Gly Leu Met Pro Gly Gly Val Phe Arg Ala Leu Tyr Pro Asn Glu Leu 165 170 175 His Gly Val Ser Val Asp Asp Ser Ile Ala Ser Ile Glu Arg Ile Phe 180 185 190 Lys Asn Asp Ala Glu Pro Arg Asp Ile Ala Ala Ile Ile Ile Glu Pro 195 200 205 Val Gln Gly Glu Gly Gly Phe Tyr Val Ala Pro Lys Glu Phe Met Lys 210 215 220 Arg Leu Arg Ala Leu Cys Asp Gln His Gly Ile Leu Leu Ile Ala Asp 225 230 235 240 Glu Val Gln Thr Gly Ala Gly Arg Thr Gly Thr Phe Phe Ala Met Glu 245 250 255 Gln Met Gly Val Ser Ala Asp Leu Thr Thr Phe Ala Lys Ser Ile Ala 260 265 270 Gly Gly Phe Pro Leu Ala Gly Val Cys Gly Lys Ala Glu Tyr Met Asp 275 280 285 Ala Ile Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Ser Pro Ile 290 295 300 Ala Cys Ala Ala Ala Leu Ala Val Met Glu Val Phe Glu Glu Glu His 305 310 315 320 Leu Leu Asp Arg Cys Lys Ala Val Gly Glu Arg Leu Val Thr Gly Leu 325 330 335 Lys Ala Ile Gln Ser Lys Tyr Pro Val Ile Gly Glu Val Arg Ala Leu 340 345 350 Gly Ala Met Ile Ala Val Glu Leu Phe Val Asp Gly Asp Ser His Lys 355 360 365 Pro Asn Ala Ala Ala Val Ala Ser Val Val Ala Lys Ala Arg Asp Lys 370 375 380 Gly Leu Ile Leu Leu Ser Cys Gly Thr Tyr Gly Asn Val Leu Arg Val 385 390 395 400 Leu Val Pro Leu Thr Ser Pro Asp Glu Gln Leu Asp Lys Gly Leu Ala 405 410 415 Ile Ile Glu Glu Cys Phe Ser Glu Leu 420 425 <210> 37 <400> 37 000 <210> 38 <211> 456 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 38 Met Thr Thr Thr Ala Ala Asp Ile Thr Tyr Arg Leu Glu Gln Lys Arg 1 5 10 15 Arg Val Gln Ala Asp Phe Pro Gly Pro Lys Ser Val Ala Leu Thr Glu 20 25 30 Arg Arg Lys Ser Val Val Ala Ala Gly Val Ala Ser Ser Val Pro Val 35 40 45 Tyr Val Ala Asp Ala Asp Gly Gly Ile Ile Gln Asp Val Asp Gly Asn 50 55 60 Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala 65 70 75 80 Ser Asp Pro Ala Val Val Gly Ala Val Lys Glu Ala Val Glu His Phe 85 90 95 Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala Val 100 105 110 Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Glu Lys Arg Thr 115 120 125 Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val Lys Val 130 135 140 Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His Ala 145 150 155 160 Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala Met 165 170 175 Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg Met 180 185 190 Pro Met Ser Tyr Pro Tyr Arg Glu Glu Asn Pro Ser Ile Thr Gly Ala 195 200 205 Glu Ala Ala Lys Arg Ala Ile Thr Ala Ile Glu Lys Gln Ile Gly Gly 210 215 220 Asp Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly Gly 225 230 235 240 Phe Ile Val Pro Ala Glu Gly Phe Leu Pro Ala Leu Ala Ala Trp Ala 245 250 255 Lys Asp Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly Phe 260 265 270 Cys Arg Thr Gly Glu Trp Phe Ala Val Asn His Glu Gly Val Val Pro 275 280 285 Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Met Pro Leu Ser 290 295 300 Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly Gly 305 310 315 320 Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu 325 330 335 Ala Ser Ile Gly Ser Met Glu Glu Tyr Gly Leu Asn Ala Arg Ala Lys 340 345 350 His Ile Glu Glu Leu Ala Thr Thr Arg Leu Ser Ala Leu Gln Glu Glu 355 360 365 Leu Ala Gly Ala Gly Ser Ala Val Ile Gly Asp Ile Arg Gly Arg Gly 370 375 380 Ala Met Leu Ala Ile Glu Leu Val Gln Ala Gly Ser Lys Glu Pro Asn 385 390 395 400 Pro Glu Leu Thr Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val 405 410 415 Ile Ile Leu Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro 420 425 430 Pro Leu Val Ile Thr Asp Glu Leu Leu Asn Asp Gly Leu Asp Val Leu 435 440 445 Ala Ala Ala Ile Lys Ala Asn Ala 450 455 <210> 39 <400> 39 000 <210> 40 <400> 40 000 <210> 41 <400> 41 000 <210> 42 <400> 42 000 <210> 43 <400> 43 000 <210> 44 <400> 44 000 <210> 45 <400> 45 000 <210> 46 <400> 46 000 <210> 47 <400> 47 000 <210> 48 <400> 48 000 <210> 49 <400> 49 000 <210> 50 <211> 420 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 50 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Glu Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Val Lys Ala Ala 50 55 60 Val Ala Ala Gln Leu Asp Asn Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Ile Ser Leu Ala Glu Arg Ile Asn Arg Leu Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Thr Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ser Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Thr Gln Ser 165 170 175 Ile Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Val 180 185 190 Asp Ile Asp Pro Lys Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ala Met Glu His His 245 250 255 Gly Val Gln Ala Asp Ile Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Ile Val Gly Arg Ala Asp Val Met Asp Gly Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Ala Gln Leu Gly Glu Lys Leu Arg Ala His Leu Glu Gly 325 330 335 Leu Arg Ala Lys Val Pro Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Ala Ala Gly Lys Pro Asp Ala Glu 355 360 365 Ala Val Lys Arg Val Gln Gln Arg Ala Leu Asp Ala Gly Leu Ile Leu 370 375 380 Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro Leu 385 390 395 400 Thr Ile Pro Asp Ala Gln Phe Ala Arg Ala Leu Asp Ile Leu Ser Glu 405 410 415 Ala Leu Ala Ala 420 <210> 51 <400> 51 000 <210> 52 <211> 429 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 52 Met Leu Thr Gln Val Thr Thr Asn Ala Ser Leu Gln Ala Arg Lys Asn 1 5 10 15 Ala Ala Cys Ala Gln Gly Ile Gly Thr Leu Thr Pro His Phe Thr Ala 20 25 30 Arg Ala Asp Asn Ala Glu Leu Trp Asp Val Glu Gly Arg Arg Phe Val 35 40 45 Asp Phe Ala Ser Gly Ile Ala Thr Leu Ala Thr Gly His Arg His Pro 50 55 60 Arg Ile Val Ala Ala Val Arg Ala Gln Leu Asp Asp Phe His His Thr 65 70 75 80 Cys Phe His Val Thr Pro Tyr Glu Glu Tyr Val Ala Leu Cys Glu Gln 85 90 95 Leu Asn Arg Val Val Pro Gly Pro Ser Ala Lys Lys Ser Ala Leu Phe 100 105 110 Thr Thr Gly Ala Glu Ala Ile Glu Asn Ala Met Lys Val Ala Arg Ala 115 120 125 Ala Thr Gly Arg Ser Gly Val Val Ala Phe Ser Gly Ala Phe His Gly 130 135 140 Arg Thr Phe Met Gly Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys 145 150 155 160 Ala Gly Phe Gly Pro Met Pro Gly Asp Val Trp His Val Pro Phe Pro 165 170 175 Ala Ala Pro Leu Gly Val Thr Val Asp Asp Ser Ile Ala Ala Leu Asp 180 185 190 Arg Leu Phe Lys Thr Asp Val Asp Pro Gln Arg Val Ala Ala Ile Val 195 200 205 Ile Glu Leu Val Gln Gly Glu Gly Gly Phe Tyr Val Ala Pro Pro Ala 210 215 220 Leu Met Glu Tyr Leu Arg Ala Glu Cys Asp Arg His Gly Ile Leu Leu 225 230 235 240 Val Val Asp Glu Ile Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe 245 250 255 Ala Leu Glu His Tyr Gly Ile Glu Ala Asp Leu Val Thr Thr Ala Lys 260 265 270 Ser Leu Ala Gly Gly Phe Pro Leu Ser Ala Leu Thr Gly Arg Ala Glu 275 280 285 Leu Met Asp Ala Thr Arg Val Gly Ser Leu Gly Gly Thr Tyr Ala Gly 290 295 300 Asn Pro Leu Ala Val Ala Ala Ala Leu Glu Thr Met Arg Val Ile Glu 305 310 315 320 Asp Glu Gly Leu Val Ala Arg Ala Arg Met Leu Gly Glu Arg Leu Thr 325 330 335 Ala Cys Leu Ala Ala Leu Arg Thr Glu Val Pro Arg Ile Cys Asp Val 340 345 350 Arg Gly Leu Gly Ala Met Val Ala Val Glu Phe Arg Asp Pro His Ser 355 360 365 Gly Glu Pro Asp Ala Glu Phe Thr Lys Arg Val His Ala Ala Gly Leu 370 375 380 Glu Arg Gly Leu Leu Leu Leu Thr Cys Gly Val His Gly Asn Val Val 385 390 395 400 Arg Phe Leu Phe Pro Leu Thr Ile Pro Glu Ala Val Tyr Glu Glu Gly 405 410 415 Leu Gly Leu Leu Ala Glu Ser Ile Arg Ala Ala Asn Val 420 425 <210> 53 <400> 53 000 <210> 54 <400> 54 000 <210> 55 <400> 55 000 <210> 56 <211> 425 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 56 Met Ser Lys Thr Asn Ala Ser Leu Met Lys Arg Arg Glu Ala Ala Val 1 5 10 15 Pro Arg Gly Val Gly Gln Ile His Pro Ile Phe Ala Glu Ser Ala Lys 20 25 30 Asn Ala Thr Val Thr Asp Val Glu Gly Arg Glu Phe Ile Asp Phe Ala 35 40 45 Gly Gly Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Ile Ile 50 55 60 Ala Ala Val Thr Ala Gln Leu Asn Lys Leu Thr His Thr Cys Phe Gln 65 70 75 80 Val Leu Ala Tyr Glu Pro Tyr Val Glu Leu Cys Glu Lys Ile Asn Ala 85 90 95 Lys Val Pro Gly Asp Phe Ala Lys Lys Thr Leu Leu Val Thr Thr Gly 100 105 110 Ser Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ala Ala Thr Gly 115 120 125 Arg Ala Gly Val Ile Ala Phe Thr Gly Ala Tyr His Gly Arg Thr Met 130 135 140 Met Thr Leu Gly Leu Thr Gly Lys Val Val Pro Tyr Ser Ala Gly Met 145 150 155 160 Gly Leu Met Pro Gly Gly Ile Phe Arg Ala Leu Tyr Pro Asn Glu Leu 165 170 175 His Gly Val Ser Ile Asp Asp Ser Ile Ala Ser Ile Glu Arg Ile Phe 180 185 190 Lys Asn Asp Ala Glu Pro Arg Asp Ile Ala Ala Ile Ile Ile Glu Pro 195 200 205 Val Gln Gly Glu Gly Gly Phe Tyr Val Ala Pro Lys Glu Phe Met Lys 210 215 220 Arg Leu Arg Ala Leu Cys Asp Gln His Gly Ile Leu Leu Ile Ala Asp 225 230 235 240 Glu Val Gln Thr Gly Ala Gly Arg Thr Gly Thr Phe Phe Ala Met Glu 245 250 255 Gln Met Gly Val Ala Ala Asp Leu Thr Thr Phe Ala Lys Ser Ile Ala 260 265 270 Gly Gly Phe Pro Leu Ala Gly Val Cys Gly Lys Ala Glu Tyr Met Asp 275 280 285 Ala Ile Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Ser Pro Ile 290 295 300 Ala Cys Ala Ala Ala Leu Ala Val Met Glu Val Phe Glu Glu Glu His 305 310 315 320 Leu Leu Asp Arg Cys Lys Ala Val Gly Glu Arg Leu Val Thr Gly Leu 325 330 335 Lys Ala Ile Gln Ala Lys Tyr Pro Val Ile Gly Glu Val Arg Ala Leu 340 345 350 Gly Ala Met Ile Ala Val Glu Leu Phe Val Asp Gly Asp Ser His Lys 355 360 365 Pro Asn Ala Pro Ala Val Ala Ala Val Val Ala Lys Ala Arg Asp Lys 370 375 380 Gly Leu Ile Leu Leu Ser Cys Gly Thr Tyr Gly Asn Val Leu Arg Val 385 390 395 400 Leu Val Pro Leu Thr Ser Pro Asp Glu Gln Leu Asp Lys Gly Leu Ala 405 410 415 Ile Ile Glu Glu Cys Phe Ala Glu Leu 420 425 <210> 57 <400> 57 000 <210> 58 <400> 58 000 <210> 59 <400> 59 000 <210> 60 <400> 60 000 <210> 61 <400> 61 000 <210> 62 <400> 62 000 <210> 63 <400> 63 000 <210> 64 <211> 455 <212> PRT <213> Artificial Sequence <220> <223> Arthrobacter sp. Edens01 <400> 64 Met Thr Phe Thr Ala Ser Glu Ala Thr Leu Pro Gln Thr Arg His Leu 1 5 10 15 Ala Thr Ala Val Pro Gly Pro Arg Ser Arg Glu Leu His Ala Glu Arg 20 25 30 Arg Gln Gln Val Ser Ser Gly Phe Gly Thr Val Leu Pro Val Phe Ile 35 40 45 Glu Arg Ala Glu Gly Gly Ile Leu Gln Asp Val Asp Gly Asn Arg Phe 50 55 60 Ile Asp Phe Ala Ser Gly Ile Ala Val Thr Ser Val Gly Ala Ser Asn 65 70 75 80 Ala Arg Val Arg Glu Arg Val Ala Ala Gln Leu Glu Arg Phe Thr His 85 90 95 Thr Cys Phe Met Val Thr Glu Tyr Glu Ser Phe Thr Gln Val Cys Arg 100 105 110 Trp Leu Asn Glu His Thr Pro Gly Thr Phe Glu Lys Arg Thr Ala Leu 115 120 125 Phe Ser Thr Gly Ala Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg 130 135 140 Ala Ala Thr Gly Arg Pro Asn Val Leu Val Phe Asp Glu Ala Tyr His 145 150 155 160 Gly Arg Ser Leu Leu Thr Met Ala Met Thr Ala Lys Glu Asn Pro Tyr 165 170 175 Arg Leu Asn Phe Gly Pro Leu Pro Gly Glu Val Leu Arg Ala Pro Ser 180 185 190 Ala Asn Pro Leu Arg Pro Ser Arg Ala Ser Val Pro Gly Ala Asp Pro 195 200 205 Ala Ala Ala Ala Leu Ala Gly Val Glu Glu Leu Leu Ser Glu His Gly 210 215 220 Ala Gly Ser Phe Ala Ala Met Val Ile Glu Pro Ile Gln Gly Glu Gly 225 230 235 240 Gly Phe Val Val Pro Ala Pro Gly Phe Leu Gln Gly Leu Arg Ser Leu 245 250 255 Ala Asp Gln His Gly Ile Val Leu Val Ile Asp Glu Ile Gln Ala Gly 260 265 270 Met Gly Arg Thr Gly Thr Leu Tyr Ala Ser Glu His Glu Gly Val Ala 275 280 285 Gly Asp Ile Thr Leu Ser Ala Lys Ala Leu Ala Gly Gly Leu Pro Leu 290 295 300 Ser Ala Val Thr Gly Arg Ala Asp Leu Met Asp Ala Val His Thr Gly 305 310 315 320 Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Cys Glu Ala Ala 325 330 335 Leu Ala Val Phe Glu Glu Phe Glu Asp Gly Thr Leu Leu Ala Asn Ala 340 345 350 Arg Ala Ile Glu Glu Thr Val Arg Glu Val Leu Glu Pro Leu Val Ala 355 360 365 Gln Val Pro Ala Val Ala Glu Phe Arg Gly Arg Gly Ala Met Leu Ala 370 375 380 Leu Glu Phe Ala Asp Pro Glu Thr Leu Glu Pro Arg Ala Asp Leu Ala 385 390 395 400 Gln Ala Ala Ser Ala Ala Cys His Ala Gln Gly Val Leu Thr Leu Thr 405 410 415 Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro Pro Leu Val Ile 420 425 430 Pro Arg Asp Leu Leu Leu Asp Gly Leu His Val Leu Arg Ser Ala Ile 435 440 445 Leu Glu Ala Ala Ala Asn Ser 450 455 <210> 65 <400> 65 000 <210> 66 <400> 66 000 <210> 67 <400> 67 000 <210> 68 <400> 68 000 <210> 69 <400> 69 000 <210> 70 <400> 70 000 <210> 71 <400> 71 000 <210> 72 <400> 72 000 <210> 73 <400> 73 000 <210> 74 <211> 421 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 74 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Asp Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Ile Lys Ala Ala 50 55 60 Val Ser Ala Gln Leu Asp Asn Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Val Ser Leu Ala Glu Arg Ile Asn Arg Leu Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Ser Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ser Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Thr Gln Ser 165 170 175 Ile Thr Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Cys 180 185 190 Asp Ile Asp Pro Lys Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ala Met Glu His His 245 250 255 Ser Val Gln Ala Asp Leu Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Val Val Gly Arg Ala Glu Ile Met Asp Gly Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Val Ala Leu Gly Asp Lys Leu Arg Ala His Leu Glu Gly 325 330 335 Leu Arg Ala Lys Val Pro Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Pro Ala Thr Gly Lys Pro Asp Ala 355 360 365 Glu Ala Val Lys Arg Val Gln Ala Arg Ala Ile Glu Lys Gly Leu Ile 370 375 380 Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro 385 390 395 400 Leu Thr Ile Pro Asp Ala Gln Phe Asp Arg Ala Leu Ala Ile Leu Ser 405 410 415 Glu Val Leu Ala Ala 420 <210> 75 <400> 75 000 <210> 76 <400> 76 000 <210> 77 <211> 420 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 77 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Glu Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Val Lys Ala Ala 50 55 60 Val Thr Ala Gln Leu Asp Asn Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Ile Ser Leu Ala Glu Arg Ile Asn Arg Val Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Thr Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ala Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Thr Gln Ser 165 170 175 Ile Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Val 180 185 190 Asp Ile Asp Pro Lys Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ala Met Glu His His 245 250 255 Thr Val Gln Ala Asp Ile Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Ile Val Gly Arg Ala Glu Ile Met Asp Gly Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Thr Gln Leu Gly Asp Lys Leu Arg Ala His Leu Glu Gly 325 330 335 Leu Arg Gly Lys Val Pro Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Ala Ala Gly Lys Pro Asp Ala Glu 355 360 365 Ala Val Lys Arg Val Gln Lys Arg Ala Leu Asp Ala Gly Leu Ile Leu 370 375 380 Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro Leu 385 390 395 400 Thr Ile Pro Asp Ala Gln Phe Ala Arg Ala Leu Asp Ile Leu Ser Glu 405 410 415 Ala Leu Ala Ala 420 <210> 78 <211> 422 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 78 Met Thr Ser Leu Thr Asp Arg Lys Asn Ala Ala Ile Ser Arg Gly Val 1 5 10 15 Gly Met Thr Thr Gln Ile Tyr Ala Glu Arg Ala Glu Asn Ala Glu Ile 20 25 30 Trp Asp Lys Asp Gly Asn Arg Tyr Ile Asp Phe Ala Ala Gly Ile Ala 35 40 45 Val Val Asn Thr Gly His Arg His Pro Arg Val Val Glu Ala Val Lys 50 55 60 Ala Gln Leu Asp Arg Phe Thr His Thr Cys His Gln Val Val Pro Tyr 65 70 75 80 Glu Asn Tyr Val Ala Leu Ala Glu Arg Leu Asn Arg Leu Val Pro Gly 85 90 95 Asn Gly Pro Lys Lys Thr Ala Phe Tyr Thr Thr Gly Ala Glu Ala Val 100 105 110 Glu Asn Ala Val Lys Ile Ala Arg His His Thr Gly Arg Ala Gly Ile 115 120 125 Ile Ala Phe Ala Gly Gly Phe His Gly Arg Thr Phe Leu Gly Met Ser 130 135 140 Leu Thr Gly Lys Val Gln Pro Tyr Lys Ala Gly Phe Gly Pro Met Met 145 150 155 160 Asn Asp Ile Trp His Leu Pro Phe Pro Asn Ala Leu His Gly Val Thr 165 170 175 Ala Asp Glu Ala Leu Ala Ala Leu Asp Arg Leu Phe Lys Ala Asp Ile 180 185 190 Asp Pro Ser Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln Gly Glu 195 200 205 Gly Gly Phe Tyr Glu Ala Pro Pro Gly Phe Met Gln Arg Leu Arg Gln 210 215 220 Ile Cys Asp Gln Tyr Ser Ile Leu Leu Ile Ala Asp Glu Val Gln Thr 225 230 235 240 Gly Phe Ala Arg Thr Gly Lys Leu Phe Ala Met Glu His His Gly Val 245 250 255 Ala Ala Asp Leu Thr Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro 260 265 270 Ile Ser Ala Val Thr Gly Arg Ala Asp Val Met Asp Ser Pro Ala Pro 275 280 285 Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val Ala Ala 290 295 300 Ala His Ala Val Leu Asp Val Ile Glu Asp Glu Gly Leu Cys Glu Arg 305 310 315 320 Ala Thr Arg Leu Gly Gln Arg Leu Lys Gln Arg Leu Ala Gly Ile Ala 325 330 335 Glu Thr Val Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Phe Met Asn 340 345 350 Ala Val Glu Phe Asn Thr Ala Gly Ser Asp Lys Pro Ser Ala Asp Phe 355 360 365 Ala Asn Arg Val Arg Glu Glu Ala Leu Lys Arg Asn Leu Ile Leu Leu 370 375 380 Thr Cys Gly Val His Gly Asn Val Ile Arg Phe Leu Ala Pro Leu Thr 385 390 395 400 Ile Gln Asp Thr Val Phe Asp Glu Ala Leu Asp Ile Leu Glu Asp Ser 405 410 415 Ile Gln Ala Ala Arg Asn 420 <210> 79 <211> 421 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 79 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Glu Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Val Lys Ala Ala 50 55 60 Val Ala Ala Gln Leu Asp Ala Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Val Thr Leu Ala Glu Arg Ile Asn Arg Val Ala 85 90 95 Pro Ile Ala Gly Leu Lys Lys Ser Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ala Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Ala Gln Ser 165 170 175 Val Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Cys 180 185 190 Asp Ile Asp Pro Arg Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Ala Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ala Met Glu His His 245 250 255 Ala Val Gln Ala Asp Leu Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Val Val Gly Arg Ala Glu Ile Met Asp Ala Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Ala Leu Leu Gly Glu Lys Leu Arg Thr His Leu Glu Gly 325 330 335 Leu Arg Ala Thr Val Pro Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Ala Ala Ser Gly Lys Pro Asp Ala 355 360 365 Glu Ala Val Lys Arg Val Gln Ala Arg Ala Leu Glu Arg Gly Leu Ile 370 375 380 Leu Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro 385 390 395 400 Leu Thr Ile Pro Asp Ala Gln Phe Asp Arg Ala Leu Ala Ile Leu Ser 405 410 415 Glu Val Leu Ala Thr 420 <210> 80 <400> 80 000 <210> 81 <211> 422 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 81 Met Thr Thr Met Thr Asp Arg Lys Asn Ala Ala Ile Ser Arg Gly Val 1 5 10 15 Gly Met Thr Thr Gln Ile Tyr Ala Glu Arg Ala Glu Asn Ala Glu Ile 20 25 30 Trp Asp Arg Glu Gly Arg Arg Tyr Ile Asp Phe Ala Ala Gly Ile Ala 35 40 45 Val Val Asn Thr Gly His Arg His Pro Lys Val Val Gln Ala Val Lys 50 55 60 Asp Gln Leu Asp Arg Phe Thr His Thr Cys His Gln Val Val Pro Tyr 65 70 75 80 Glu Asn Tyr Val Ala Leu Ala Glu Arg Leu Asn Asp Leu Val Pro Gly 85 90 95 Asp Phe Glu Lys Lys Thr Ile Phe Ala Thr Thr Gly Ala Glu Ala Val 100 105 110 Glu Asn Ala Val Lys Ile Ala Arg Phe Ala Thr Gly Arg Ser Ala Ile 115 120 125 Ile Ala Phe Thr Gly Ala Phe His Gly Arg Thr Phe Met Gly Met Thr 130 135 140 Leu Thr Gly Lys Val Gln Pro Tyr Lys Ala Gly Phe Gly Ala Met Met 145 150 155 160 Pro Asp Val Phe His Leu Pro Phe Pro Asn Glu Leu His Gly Val Ser 165 170 175 Gln Asp Asp Ala Leu Ala Ala Leu Asp Lys Leu Phe Lys Ala Asp Val 180 185 190 Asp Pro Ala Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln Gly Glu 195 200 205 Gly Gly Phe Tyr Pro Val Pro Ser Gly Phe Met Gln Lys Leu Arg Ser 210 215 220 Leu Cys Asp Asp Asn Gly Ile Leu Leu Ile Ala Asp Glu Val Gln Thr 225 230 235 240 Gly Phe Ala Arg Thr Gly Arg Leu Phe Ala Met Glu Leu His Gly Val 245 250 255 Ser Ala Asp Ile Thr Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro 260 265 270 Ile Ser Ala Val Thr Gly Arg Ala Glu Ile Met Asp Ala Pro Asn Pro 275 280 285 Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Gly Val Ala Ala 290 295 300 Ala His Ala Val Leu Asp Ile Ile Glu Glu Glu Gly Leu Cys Asp Arg 305 310 315 320 Ala Glu Arg Leu Gly Gln Arg Leu Lys Gln Arg Leu Ala Ser Leu Arg 325 330 335 Asp Asp Val Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Leu Met Asn 340 345 350 Ala Val Glu Phe Asn Val Ala Gly Ser Asp Arg Pro Asn Pro Glu Met 355 360 365 Thr Asn Arg Val Arg Glu Glu Ala Leu Glu Arg Gly Leu Ile Leu Leu 370 375 380 Thr Cys Gly Val Tyr Gly Asn Val Ile Arg Phe Leu Pro Pro Leu Thr 385 390 395 400 Val Pro Asp Ala Val Phe Asp Glu Ala Leu Gly Ile Leu Glu Asp Ser 405 410 415 Ile Arg Ala Ala Arg Gly 420 <210> 82 <400> 82 000 <210> 83 <211> 422 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 83 Met Met Gln Arg Arg Val Ala Ala Val Pro Arg Gly Val Gly Gln Ile 1 5 10 15 His Pro Ile Phe Ala Asp His Ala Lys Asn Ser Ser Val Val Asp Val 20 25 30 Glu Gly Arg Glu Phe Ile Asp Phe Ala Gly Gly Ile Ala Val Leu Asn 35 40 45 Thr Gly His Leu His Pro Lys Ile Val Lys Ala Val Glu Glu Gln Leu 50 55 60 His Lys Leu Thr His Thr Cys Phe Gln Val Leu Ala Tyr Glu Pro Tyr 65 70 75 80 Ile Ala Leu Cys Glu Ala Ile Ala Lys Arg Val Pro Gly Asp Phe Ala 85 90 95 Lys Lys Thr Leu Leu Val Thr Ser Gly Ser Glu Ala Val Glu Asn Ala 100 105 110 Val Lys Ile Ala Arg Ala Ala Thr Gly Arg Ala Gly Val Ile Ala Phe 115 120 125 Thr Gly Ala Tyr His Gly Arg Thr Met Met Thr Leu Ser Leu Thr Gly 130 135 140 Lys Val Val Pro Tyr Ser Ala Gly Met Gly Leu Met Pro Gly Gly Val 145 150 155 160 Phe Arg Ala Leu Ala Pro Cys Pro Leu His Gly Ile Ser Glu Asp Asp 165 170 175 Ala Ile Ala Ser Ile Glu Arg Val Phe Lys Asn Asp Ala Gln Pro Arg 180 185 190 Asp Ile Ala Ala Ile Ile Ile Glu Pro Val Gln Gly Glu Gly Gly Phe 195 200 205 Tyr Val Asn Ser Pro Ala Phe Met Gln Arg Leu Arg Ala Leu Cys Asp 210 215 220 Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val Gln Thr Gly Ala Gly 225 230 235 240 Arg Thr Gly Thr Phe Phe Ala Cys Glu Gln Leu Gly Ile Val Pro Asp 245 250 255 Leu Thr Thr Phe Ala Lys Ser Val Gly Gly Gly Phe Pro Ile Ser Gly 260 265 270 Val Cys Gly Lys Ala Glu Ile Met Asp Val Ile Ala Pro Gly Gly Leu 275 280 285 Gly Gly Thr Tyr Ala Gly Ser Pro Ile Ala Cys Ala Ala Ala Leu Ala 290 295 300 Val Met Glu Val Phe Glu Glu Glu Lys Leu Leu Glu Arg Ser Gln Ala 305 310 315 320 Val Gly Glu Lys Leu Lys Ala Gly Leu Asn Ala Ile Ala Ala Arg His 325 330 335 Lys Val Ile Gly Asp Val Arg Gly Leu Gly Ser Met Val Ala Ile Glu 340 345 350 Leu Phe Glu Gly Gly Asp His Ser Lys Pro Ala Ala Glu Leu Val Gly 355 360 365 Arg Ile Val Ala Arg Ala Arg Asp Lys Gly Leu Leu Leu Leu Ser Cys 370 375 380 Gly Thr Tyr Tyr Asn Val Ile Arg Phe Leu Met Pro Leu Thr Ile Pro 385 390 395 400 Asp Ala Gln Leu Glu Arg Gly Leu Ala Ile Val Ala Glu Cys Phe Asp 405 410 415 Glu Leu Ala Ser Glu Gln 420 <210> 84 <400> 84 000 <210> 85 <400> 85 000 <210> 86 <400> 86 000 <210> 87 <400> 87 000 <210> 88 <400> 88 000 <210> 89 <400> 89 000 <210> 90 <400> 90 000 <210> 91 <211> 422 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 91 Met Thr Thr Met Thr Asp Arg Lys Asn Ala Ala Ile Ser Arg Gly Val 1 5 10 15 Gly Met Thr Thr Gln Ile Tyr Ala Glu Arg Ala Glu Asn Ala Glu Ile 20 25 30 Trp Asp Arg Glu Gly Arg Arg Tyr Ile Asp Phe Ala Ala Gly Ile Ala 35 40 45 Val Val Asn Thr Gly His Arg His Pro Lys Val Val Gln Ala Val Lys 50 55 60 Asp Gln Leu Asp Arg Phe Thr His Thr Cys His Gln Val Val Pro Tyr 65 70 75 80 Glu Asn Tyr Val Ala Leu Ala Glu Arg Leu Asn Asp Leu Val Pro Gly 85 90 95 Asp Phe Glu Lys Lys Thr Ile Phe Ala Thr Thr Gly Ala Glu Ala Val 100 105 110 Glu Asn Ala Val Lys Ile Ala Arg Phe Ala Thr Gly Arg Ser Ala Ile 115 120 125 Ile Ala Phe Thr Gly Ala Phe His Gly Arg Thr Phe Met Gly Met Thr 130 135 140 Leu Thr Gly Lys Val Gln Pro Tyr Lys Ala Gly Phe Gly Ala Met Met 145 150 155 160 Pro Asp Val Phe His Leu Pro Phe Pro Asn Glu Leu His Gly Val Ser 165 170 175 Gln Asp Asp Ala Leu Ala Ala Leu Asp Lys Leu Phe Lys Ala Asp Val 180 185 190 Asp Pro Ala Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln Gly Glu 195 200 205 Gly Gly Phe Tyr Pro Val Pro Ser Gly Phe Met Gln Lys Leu Arg Ala 210 215 220 Ile Cys Asp Asp Asn Gly Ile Leu Leu Ile Ala Asp Glu Val Gln Thr 225 230 235 240 Gly Phe Ala Arg Thr Gly Arg Leu Phe Ala Met Glu His His Gly Val 245 250 255 Ser Ala Asp Ile Thr Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro 260 265 270 Ile Ser Ala Val Thr Gly Arg Ala Glu Ile Met Asp Ala Pro Asn Pro 275 280 285 Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Gly Val Ala Ala 290 295 300 Ala His Ala Val Leu Asp Ile Ile Glu Glu Glu Gly Leu Cys Asp Arg 305 310 315 320 Ala Glu Arg Leu Gly Gln Arg Leu Lys Gln Arg Leu Ala Ser Leu Arg 325 330 335 Asp Asp Val Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Leu Met Asn 340 345 350 Ala Val Glu Phe Asn Val Ala Gly Ser Asp Arg Pro Asn Pro Glu Met 355 360 365 Thr Asn Arg Val Arg Glu Gln Ala Leu Lys Arg Gly Leu Ile Leu Leu 370 375 380 Thr Cys Gly Val His Gly Asn Val Ile Arg Phe Leu Pro Pro Leu Thr 385 390 395 400 Val Pro Asp Ala Val Phe Asp Glu Ala Leu Gly Ile Leu Glu Asp Ser 405 410 415 Ile Arg Ala Ala Arg Gly 420 <210> 92 <400> 92 000 <210> 93 <400> 93 000 <210> 94 <400> 94 000 <210> 95 <400> 95 000 <210> 96 <400> 96 000 <210> 97 <400> 97 000 <210> 98 <400> 98 000 <210> 99 <400> 99 000 <210> 100 <400> 100 000 <210> 101 <400> 101 000 <210> 102 <400> 102 000 <210> 103 <400> 103 000 <210> 104 <400> 104 000 <210> 105 <400> 105 000 <210> 106 <211> 422 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 106 Met Thr Thr Met Thr Asp Arg Lys Asn Ala Ala Ile Ser Arg Gly Val 1 5 10 15 Gly Met Thr Thr Gln Ile Tyr Ala Glu Arg Ala Glu Asn Ala Glu Ile 20 25 30 Trp Asp Arg Glu Gly Arg Arg Tyr Ile Asp Phe Ala Ala Gly Ile Ala 35 40 45 Val Val Asn Thr Gly His Arg His Pro Lys Val Val Gln Ala Val Lys 50 55 60 Asp Gln Leu Asp Arg Phe Thr His Thr Cys His Gln Val Val Pro Tyr 65 70 75 80 Glu Asn Tyr Val Ser Leu Ala Glu Arg Leu Asn Glu Leu Val Pro Gly 85 90 95 Asp Phe Glu Lys Lys Thr Ile Phe Ala Thr Thr Gly Ala Glu Ala Val 100 105 110 Glu Asn Ala Val Lys Ile Ala Arg Phe Ala Thr Gly Arg Ser Ala Ile 115 120 125 Ile Ala Phe Thr Gly Ala Phe His Gly Arg Thr Phe Met Gly Met Thr 130 135 140 Leu Thr Gly Lys Val Gln Pro Tyr Lys Ala Gly Phe Gly Ala Met Met 145 150 155 160 Pro Asp Val Phe His Leu Pro Phe Pro Asn Glu Leu His Gly Val Ser 165 170 175 Gln Asp Asp Ala Leu Ala Ala Leu Asp Lys Leu Phe Lys Ala Asp Val 180 185 190 Asp Pro Ala Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln Gly Glu 195 200 205 Gly Gly Phe Tyr Pro Val Pro Ser Gly Phe Met Gln Lys Leu Arg Ala 210 215 220 Leu Cys Asp Asp Asn Gly Ile Leu Leu Ile Ala Asp Glu Val Gln Thr 225 230 235 240 Gly Phe Ala Arg Thr Gly Arg Leu Phe Ala Met Glu Leu His Gly Val 245 250 255 Ala Ala Asp Ile Thr Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro 260 265 270 Ile Ser Ala Val Thr Gly Arg Ala Glu Ile Met Asp Ala Pro Asn Pro 275 280 285 Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Gly Val Ala Ala 290 295 300 Ala His Ala Val Leu Asp Ile Ile Glu Glu Glu Gly Leu Cys Asp Arg 305 310 315 320 Ala Glu Arg Leu Gly Gln Arg Leu Lys Gln Arg Leu Ala Ser Leu Arg 325 330 335 Asp Asp Val Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Leu Met Asn 340 345 350 Ala Val Glu Phe Asn Val Ala Gly Ser Asp Arg Pro Asn Pro Glu Met 355 360 365 Thr Asn Arg Val Arg Glu Glu Ala Leu Glu Arg Gly Leu Ile Leu Leu 370 375 380 Thr Cys Gly Val Tyr Gly Asn Val Ile Arg Phe Leu Pro Pro Leu Thr 385 390 395 400 Val Pro Asp Ala Val Phe Asp Glu Ala Leu Gly Ile Leu Glu Asp Ser 405 410 415 Ile Arg Ala Ala Arg Gly 420 <210> 107 <400> 107 000 <210> 108 <211> 420 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 108 Met Lys Asn Gln Asp Leu Asn Thr Arg Arg Ser Leu Ala Thr Pro Arg 1 5 10 15 Gly Val Gly Val Met Cys Asp Phe Tyr Ala Val Arg Ala Glu Asn Ala 20 25 30 Thr Leu Trp Asp Ala Glu Gly Lys Glu Tyr Ile Asp Phe Ala Gly Gly 35 40 45 Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Val Lys Ala Ala 50 55 60 Val Thr Ala Gln Leu Asp Asn Phe Thr His Thr Ala Tyr Gln Ile Val 65 70 75 80 Pro Tyr Glu Gly Tyr Ile Ser Leu Ala Glu Arg Ile Asn Arg Val Ala 85 90 95 Pro Ile Asp Gly Leu Lys Lys Thr Ala Phe Phe Thr Thr Gly Val Glu 100 105 110 Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ser Ala Thr Gly Arg Ser 115 120 125 Gly Val Ile Ala Phe Ser Gly Ser Phe His Gly Arg Thr Met Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Ala Pro Tyr Lys Leu Ser Phe Gly Pro 145 150 155 160 Met Pro Gly Asp Ile Tyr His Val Pro Phe Pro Asn Ala Thr Gln Ser 165 170 175 Ile Ser Val Ala Asp Ser Leu Lys Ala Leu Asp Leu Leu Phe Lys Val 180 185 190 Asp Ile Asp Pro Lys Arg Val Ala Ala Ile Ile Ile Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Asn Ile Thr Pro Pro Glu Leu Met Thr Ala Leu 210 215 220 Arg Lys Val Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Ser Met Glu His His 245 250 255 Ser Val Gln Ala Asp Ile Ile Thr Met Ala Lys Ser Leu Gly Gly Gly 260 265 270 Phe Pro Ile Ser Gly Val Val Gly Arg Ala Glu Ile Met Asp Gly Pro 275 280 285 Ala Ala Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Ala Val 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Ala Glu Glu Lys Leu Cys 305 310 315 320 Glu Arg Ala Ala Glu Leu Gly Asp Lys Leu Arg Ala His Leu Glu Gly 325 330 335 Leu Arg Gly Lys Val Ala Gly Ile Ala Asp Val Arg Gly Leu Gly Ser 340 345 350 Met Val Ala Leu Glu Leu Asn Asp Ala Ala Gly Lys Pro Asp Ala Glu 355 360 365 Ala Val Lys Arg Val Gln Lys Arg Ala Leu Asp Ala Gly Leu Ile Leu 370 375 380 Leu Ser Cys Gly Val Tyr Gly Asn Val Leu Arg Phe Leu Tyr Pro Leu 385 390 395 400 Thr Ile Pro Asp Ala Gln Phe Ala Arg Ala Leu Asp Ile Leu Ser Glu 405 410 415 Ala Leu Ala Ala 420 <210> 109 <400> 109 000 <210> 110 <400> 110 000 <210> 111 <400> 111 000 <210> 112 <211> 419 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 112 Met Thr Asp Arg Lys Asn Ala Ala Ile Ser Arg Gly Val Gly Met Thr 1 5 10 15 Thr Gln Ile Tyr Ala Glu Arg Ala Glu Asn Ala Glu Ile Trp Asp Arg 20 25 30 Glu Gly Arg Arg Tyr Ile Asp Phe Ala Ala Gly Ile Ala Val Val Asn 35 40 45 Thr Gly His Arg His Pro Lys Val Val Gln Ala Val Lys Asp Gln Leu 50 55 60 Asp Arg Phe Thr His Thr Cys His Gln Val Val Pro Tyr Glu Asn Tyr 65 70 75 80 Val Ala Leu Ala Glu Arg Leu Asn Asp Leu Val Pro Gly Asp Phe Glu 85 90 95 Lys Lys Thr Ile Phe Ala Thr Thr Gly Ala Glu Ala Val Glu Asn Ala 100 105 110 Val Lys Ile Ala Arg Phe Ala Thr Gly Arg Ser Ala Ile Ile Ala Phe 115 120 125 Thr Gly Ala Phe His Gly Arg Thr Phe Met Gly Met Thr Leu Thr Gly 130 135 140 Lys Val Gln Pro Tyr Lys Ala Gly Phe Gly Ala Met Met Pro Asp Val 145 150 155 160 Phe His Leu Pro Phe Pro Asn Glu Leu His Gly Val Ser Gln Asp Asp 165 170 175 Ala Leu Ala Ala Leu Asp Lys Leu Phe Lys Ala Asp Val Asp Pro Ala 180 185 190 Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln Gly Glu Gly Gly Phe 195 200 205 Tyr Pro Val Pro Ser Gly Phe Met Gln Lys Leu Arg Ala Leu Cys Asp 210 215 220 Asp Asn Gly Ile Leu Leu Ile Ala Asp Glu Val Gln Thr Gly Phe Ala 225 230 235 240 Arg Thr Gly Arg Leu Phe Ala Met Glu Leu His Gly Val Ser Ala Asp 245 250 255 Ile Thr Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro Ile Ser Ala 260 265 270 Val Thr Gly Arg Ala Glu Ile Met Asp Ala Pro Asn Pro Gly Gly Leu 275 280 285 Gly Gly Thr Tyr Ala Gly Asn Pro Leu Gly Val Ala Ala Ala His Ala 290 295 300 Val Leu Asp Ile Ile Glu Glu Glu Gly Leu Cys Asp Arg Ala Glu Arg 305 310 315 320 Leu Gly Gln Arg Leu Lys Gln Arg Leu Ala Ser Leu Arg Asp Asp Val 325 330 335 Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Leu Met Asn Ala Val Glu 340 345 350 Phe Asn Val Ala Gly Ser Asp Arg Pro Asn Pro Glu Met Thr Asn Arg 355 360 365 Val Arg Glu Glu Ala Leu Lys Arg Gly Leu Ile Leu Leu Thr Cys Gly 370 375 380 Val Tyr Gly Asn Val Val Arg Phe Leu Pro Pro Leu Thr Val Pro Asp 385 390 395 400 Ala Val Phe Asp Glu Ala Leu Gly Ile Leu Glu Asp Ser Ile Arg Ala 405 410 415 Ala Arg Gly <210> 113 <400> 113 000 <210> 114 <400> 114 000 <210> 115 <400> 115 000 <210> 116 <211> 424 <212> PRT <213> Artificial Sequence <220> <223> Metagenomic <400> 116 Met Lys Asn Asp Ala Ile Ser Asp Arg Lys Asn Ala Ala Ile Ser Arg 1 5 10 15 Gly Val Gly Met Thr Thr Gln Ile Tyr Ala Asp Arg Ala Glu Asn Ser 20 25 30 Glu Ile Trp Asp Val Glu Gly Arg Arg Tyr Ile Asp Phe Ser Ser Gly 35 40 45 Ile Ala Val Val Asn Thr Gly His Arg His Pro Lys Val Ile Ala Ala 50 55 60 Val Lys Glu Gln Leu Asp Arg Phe Thr His Thr Cys His Gln Val Val 65 70 75 80 Pro Tyr Glu Asn Tyr Val His Leu Ala Glu Arg Leu Asn Ser Met Leu 85 90 95 Pro Gly Lys Phe Glu Lys Lys Thr Val Phe Val Thr Thr Gly Ala Glu 100 105 110 Ala Val Glu Asn Ala Ile Lys Ile Ala Arg Ala Ala Thr Gly Arg Gln 115 120 125 Ala Ile Val Ser Phe Ser Gly Ala Phe His Gly Arg Thr Leu Leu Gly 130 135 140 Met Ala Leu Thr Gly Lys Val Val Pro Tyr Lys Val Gly Phe Gly Ala 145 150 155 160 Met Pro Gly Asp Val Phe His Val Pro Phe Pro Val Pro Leu His Gly 165 170 175 Val Ser Val Ala Asp Ser Leu Ala Ala Leu Asp Arg Leu Phe Lys Ala 180 185 190 Asp Val Asp Pro Asn Arg Val Ala Ala Ile Ile Val Glu Pro Val Gln 195 200 205 Gly Glu Gly Gly Phe Tyr Glu Ala Pro Arg Glu Leu Thr Thr Ala Leu 210 215 220 Arg Arg Ile Cys Asp Gln His Gly Ile Leu Leu Ile Ala Asp Glu Val 225 230 235 240 Gln Thr Gly Phe Ala Arg Thr Gly Lys Met Phe Ala Met Glu His His 245 250 255 Asp Ala Ala Pro Asp Leu Thr Thr Met Ala Lys Ser Leu Ala Gly Gly 260 265 270 Phe Pro Leu Ser Ala Val Thr Gly Arg Ala Glu Leu Met Asp Ala Pro 275 280 285 Gly Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Asn Pro Leu Gly Ile 290 295 300 Ala Ala Ala His Ala Val Leu Asp Val Ile Glu Glu Glu Lys Leu Cys 305 310 315 320 Asp Arg Ala Asn Thr Leu Gly Asn Arg Leu Lys Gln Arg Leu Glu Ser 325 330 335 Leu Arg Asp Asp Val Pro Glu Ile Val Asp Ile Arg Gly Pro Gly Phe 340 345 350 Met Asn Ala Ile Glu Phe Asn Asp Val Ala Lys Gly Leu Pro Ser Ala 355 360 365 Glu Ile Ala Asn Ala Ile Arg Leu Lys Ala Leu Asp Lys Gly Leu Ile 370 375 380 Leu Leu Thr Cys Gly Val Tyr Gly Asn Val Ile Arg Phe Leu Ala Pro 385 390 395 400 Ile Thr Ile Gln Asp Asn Val Met Asn Glu Ala Leu Asp Ile Leu Glu 405 410 415 Ser Ser Ile Arg Glu Ala Gln Ala 420 <210> 117 <400> 117 000 <210> 118 <400> 118 000 <210> 119 <400> 119 000 <210> 120 <400> 120 000 <210> 121 <400> 121 000 <210> 122 <400> 122 000 <210> 123 <400> 123 000 <210> 124 <400> 124 000 <210> 125 <400> 125 000 <210> 126 <400> 126 000 <210> 127 <400> 127 000 <210> 128 <400> 128 000 <210> 129 <400> 129 000 <210> 130 <400> 130 000 <210> 131 <400> 131 000 <210> 132 <400> 132 000 <210> 133 <211> 471 <212> PRT <213> Artificial Sequence <220> <223> Saccharomyces cerevisiae <400> 133 Met Ser Ile Cys Glu Gln Tyr Tyr Pro Glu Glu Pro Thr Lys Pro Thr 1 5 10 15 Val Lys Thr Glu Ser Ile Pro Gly Pro Glu Ser Gln Lys Gln Leu Lys 20 25 30 Glu Leu Gly Glu Val Phe Asp Thr Arg Pro Ala Tyr Phe Leu Ala Asp 35 40 45 Tyr Glu Lys Ser Leu Gly Asn Tyr Ile Thr Asp Val Asp Gly Asn Thr 50 55 60 Tyr Leu Asp Leu Tyr Ala Gln Ile Ser Ser Ile Ala Leu Gly Tyr Asn 65 70 75 80 Asn Pro Ala Leu Ile Lys Ala Ala Gln Ser Pro Glu Met Ile Arg Ala 85 90 95 Leu Val Asp Arg Pro Ala Leu Gly Asn Phe Pro Ser Lys Asp Leu Asp 100 105 110 Lys Ile Leu Lys Gln Ile Leu Lys Ser Ala Pro Lys Gly Gln Asp His 115 120 125 Val Trp Ser Gly Leu Ser Gly Ala Asp Ala Asn Glu Leu Ala Phe Lys 130 135 140 Ala Ala Phe Ile Tyr Tyr Arg Ala Lys Gln Arg Gly Tyr Asp Ala Asp 145 150 155 160 Phe Ser Glu Lys Glu Asn Leu Ser Val Met Asp Asn Asp Ala Pro Gly 165 170 175 Ala Pro His Leu Ala Val Leu Ser Phe Lys Arg Ala Phe His Gly Arg 180 185 190 Leu Phe Ala Ser Gly Ser Thr Thr Cys Ser Lys Pro Ile His Lys Leu 195 200 205 Asp Phe Pro Ala Phe His Trp Pro His Ala Glu Tyr Pro Ser Tyr Gln 210 215 220 Tyr Pro Leu Asp Glu Asn Ser Asp Ala Asn Arg Lys Glu Asp Asp His 225 230 235 240 Cys Leu Ala Ile Val Glu Glu Leu Ile Lys Thr Trp Ser Ile Pro Val 245 250 255 Ala Ala Leu Ile Ile Glu Pro Ile Gln Ser Glu Gly Gly Asp Asn His 260 265 270 Ala Ser Lys Tyr Phe Leu Gln Lys Leu Arg Asp Ile Thr Leu Lys Tyr 275 280 285 Asn Val Val Tyr Ile Ile Asp Glu Val Gln Thr Gly Val Gly Ala Thr 290 295 300 Gly Lys Leu Trp Cys His Glu Tyr Ala Asp Ile Gln Pro Pro Val Asp 305 310 315 320 Leu Val Thr Phe Ser Lys Lys Phe Gln Ser Ala Gly Tyr Phe Phe His 325 330 335 Asp Pro Lys Phe Ile Pro Asn Lys Pro Tyr Arg Gln Phe Asn Thr Trp 340 345 350 Cys Gly Glu Pro Ala Arg Met Ile Ile Ala Gly Ala Ile Gly Gln Glu 355 360 365 Ile Ser Asp Lys Lys Leu Thr Glu Gln Cys Ser Arg Val Gly Asp Tyr 370 375 380 Leu Phe Lys Lys Leu Glu Gly Leu Gln Lys Lys Tyr Pro Glu Asn Phe 385 390 395 400 Gln Asn Leu Arg Gly Lys Gly Arg Gly Thr Phe Ile Ala Trp Asp Leu 405 410 415 Pro Thr Gly Glu Lys Arg Asp Leu Leu Leu Lys Lys Leu Lys Leu Asn 420 425 430 Gly Cys Asn Val Gly Gly Cys Ala Val His Ala Val Arg Leu Arg Pro 435 440 445 Ser Leu Thr Phe Glu Glu Lys His Ala Asp Ile Phe Ile Glu Ala Leu 450 455 460 Ala Lys Ser Val Asn Glu Leu 465 470 <210> 134 <211> 450 <212> PRT <213> Artificial Sequence <220> <223> Clostridium viride <400> 134 Met Leu Lys Asn Ala Leu Pro Lys Ile Val Thr Glu Ser Leu Pro Gly 1 5 10 15 Pro Lys Ala Lys Ala Ile Ile Asp Arg Arg Ala Asn Ala Ile Pro Ser 20 25 30 Ala Ile Arg Cys Val Tyr Pro Val Val Ile Asp Arg Gly Glu Gly Ala 35 40 45 Met Val Glu Asp Val Asp Gly Asn His Phe Leu Asp Trp Ile Gly Gly 50 55 60 Val Gly Val Leu Asn Ile Gly Tyr Ser His Pro Glu Val Val Asp Ala 65 70 75 80 Val Lys Lys Gln Thr Glu Arg Tyr Phe His Gly Met Phe Asn Ile Val 85 90 95 Thr His Glu Gly Tyr Val Ala Leu Ala Glu Lys Leu Ser Thr Leu Ala 100 105 110 Pro Val Leu Gly Lys Glu Lys Lys Ala Phe Phe Ala Asn Ser Gly Ala 115 120 125 Glu Ala Asn Glu Asn Ala Ile Lys Ile Ala Lys Ala Tyr Thr Lys Arg 130 135 140 Pro Asn Ile Ile Val Phe Ser Gly Ala Phe His Gly Arg Thr Met Leu 145 150 155 160 Thr Met Ser Met Thr Ser Lys Lys Ala Tyr Ala Asn Gly Met Gly Pro 165 170 175 Phe Pro Asp Gly Val Tyr Arg Ala Lys Phe Pro Tyr Tyr Tyr Arg Asn 180 185 190 Pro Val Gly Leu Pro Gln Glu Glu Ala Val Asn Tyr Tyr Ile Glu Ser 195 200 205 Ile Lys Ser Val Phe Glu Glu Ala Ser Pro Pro Glu His Val Ala Ala 210 215 220 Ile Val Val Glu Pro Leu Gln Gly Glu Gly Gly Phe Ile Pro Ala Pro 225 230 235 240 Ile Glu Trp Val Lys Ala Val Arg Gln Leu Cys Asp Gln His Gly Ile 245 250 255 Leu Leu Ile Ala Asp Glu Val Gln Thr Gly Phe Cys Arg Ala Gly Lys 260 265 270 Met Phe Ala Ser Glu Tyr Trp Gln Gly Ala Gly Ala Ser Pro Asp Ile 275 280 285 Leu Thr Thr Ala Lys Ser Ile Ala Ala Gly Val Pro Ile Ser Ala Ile 290 295 300 Val Ala Arg Asn Glu Ile Met Asp Ala Val Pro Ala Gly Ile Ile Gly 305 310 315 320 Gly Thr Tyr Cys Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Lys Val 325 330 335 Ile Glu Val Met Glu Arg Asp Lys Phe Ala Gln Arg Ser Thr Glu Ile 340 345 350 Gly Lys Ile Ala Met Glu Arg Phe Gln Gln Phe Lys Gln Asn Tyr Pro 355 360 365 Val Val Gly Asp Val Arg Gly Leu Gly Ser Met Ile Gly Leu Glu Phe 370 375 380 Val Lys Asp Pro Val Ser Lys Glu Pro Asn Ala Pro Phe Val Asn Ala 385 390 395 400 Leu Val Gln Glu Ala Val Lys Arg Gly Leu Met Ile Glu Asn Ala Gly 405 410 415 Thr Tyr Gly Asn Val Ile Arg Phe Leu Ala Pro Leu Thr Ile Thr Asp 420 425 430 Glu Gln Leu Tyr Ala Gly Leu Asp Ile Met Glu Glu Ser Ile Lys Ala 435 440 445 Leu Leu 450 <210> 135 <211> 441 <212> PRT <213> Artificial Sequence <220> <223> Gulosibacter molinativorax <400> 135 Met Glu Phe Arg Leu Glu Gln Gln Arg Lys Ile Val Thr Glu Ile Pro 1 5 10 15 Gly Pro Lys Ser Glu Glu Leu Leu Lys Arg Arg Gln Gln Tyr Val Ser 20 25 30 Ser Ser Ile Gly Ser Ser Leu Pro Val Tyr Ile Gly Glu Ala Asp Gly 35 40 45 Ala Ile Leu Arg Asp Val Asp Gly Asn Gln Phe Ile Asp Phe Gly Ser 50 55 60 Gly Ile Gly Val Thr Thr Val Gly Asn Ala Asn Pro Lys Val Val Lys 65 70 75 80 Ala Ile Gln Asp Ala Ala Ala Ala Ser Thr His Leu Gln Ile Asn Thr 85 90 95 Ala Pro Tyr Gly Ser Tyr Val Asp Leu Cys Gln Lys Leu Thr Glu Leu 100 105 110 Thr Pro Gly Asp Phe Pro Lys Lys Ala Ala Leu Phe Asn Ser Gly Ala 115 120 125 Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg Lys Tyr Thr Gly Arg 130 135 140 Asp Ala Val Ile Val Phe Asp His Ala Phe His Gly Arg Thr Asn Leu 145 150 155 160 Thr Met Ala Met Thr Ser Lys Ser Met Pro Tyr Lys Asp Gly Phe Gly 165 170 175 Pro Phe Ala Pro Glu Val Tyr Arg Ala Pro Leu Ser Tyr Pro Phe Arg 180 185 190 Asp Glu Leu Ser Gly Pro Glu Ala Ala Ala Arg Thr Ile Asp Val Ile 195 200 205 Asp Lys Gln Val Gly Ala Lys Asn Val Ala Ala Ile Ile Ile Glu Pro 210 215 220 Ile Val Gly Glu Gly Gly Phe Ile Val Pro Ala Glu Gly Phe Leu Pro 225 230 235 240 Ala Leu Val Glu Tyr Ala Asn Glu Asn Gly Ile Val Phe Val Ala Asp 245 250 255 Glu Val Gln Ala Gly Met Ser Arg Thr Gly Lys Trp Phe Cys Ser Glu 260 265 270 Trp Glu Gly Ile Glu Pro Asp Leu Val Thr Ser Ala Lys Gly Ile Ala 275 280 285 Gly Gly Met Pro Leu Ser Ala Val Val Gly Arg Ala Glu Ile Met Asp 290 295 300 Ala Pro His Thr Gly Gly Ile Gly Gly Thr Tyr Ala Gly Asn Pro Val 305 310 315 320 Ala Asn Ala Ala Ala Leu Ala Thr Ile Ala Ser Tyr Glu Glu Asp Gly 325 330 335 Leu Gln Glu Ala Ala Leu Arg Ile Glu Lys Thr Ile Arg Gly Val Leu 340 345 350 Glu Pro Leu Val Asp Glu Leu Asp Val Val Gly Glu Val Arg Gly Arg 355 360 365 Gly Ala Met Leu Ala Ile Glu Leu Val Thr Gly Ala Asp Lys Thr Pro 370 375 380 Asn Pro Glu Leu Val Lys Thr Val Val Ala Glu Ala Gln Ala Gln Gly 385 390 395 400 Val Val Phe Leu Thr Cys Gly Thr Tyr Gly Asn Val Ile Arg Phe Leu 405 410 415 Pro Pro Leu Val Ile Thr Asp Glu Leu Leu Thr Asp Gly Leu Asn Val 420 425 430 Leu Val Asp Ala Ile Arg Lys Asn Ala 435 440 <210> 136 <211> 447 <212> PRT <213> Artificial Sequence <220> <223> Kocuria rhizophila <400> 136 Met Ala Glu Ile Glu Tyr Arg Leu Pro Gln Lys Arg Glu Leu Val Thr 1 5 10 15 Ser Ile Pro Gly Pro Lys Ser Gln Ser Leu Ala Glu Arg Arg Ala Gln 20 25 30 Thr Val Ala Ala Gly Val Ala Ser Ser Leu Pro Val Phe Ala Asp Glu 35 40 45 Leu Asp Gly Gly Val Ile Lys Asp Val Asp Gly Asn Gln Met Val Asp 50 55 60 Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly Ala Ser Asn Pro Lys 65 70 75 80 Val Val Ala Arg Val Gln Asp Ala Val Ala Lys Phe Thr His Thr Cys 85 90 95 Phe Met Val Thr Pro Tyr Glu Asp Tyr Val Ala Val Gly Glu Lys Met 100 105 110 Ala Gln Leu Thr Pro Gly Ser Phe Asp Lys Arg Thr Ala Leu Phe Thr 115 120 125 Ser Gly Ser Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg Val Arg 130 135 140 Thr Lys Arg Gln Ala Val Val Val Phe Asp His Ala Tyr His Gly Arg 145 150 155 160 Thr Asn Leu Thr Met Ala Met Thr Ala Lys Val Met Pro Tyr Lys Gln 165 170 175 Gly Phe Gly Pro Phe Ala Asn Glu Val Tyr Arg Val Pro Met Ser Tyr 180 185 190 Pro Phe Arg Asp Pro Glu Gly Met Thr Gly Thr Glu Ala Ala Lys Arg 195 200 205 Ala Leu Thr Met Val Glu Lys Gln Val Gly Ala Glu Asn Val Ala Ala 210 215 220 Val Val Ile Glu Pro Ile Gln Gly Glu Gly Gly Phe Ile Val Pro Ala 225 230 235 240 Glu Gly Phe Leu Pro Ala Leu Ser Ser Trp Cys Arg Glu Asn Gly Ala 245 250 255 Val Phe Val Ala Asp Glu Val Gln Ala Gly Ile Ala Arg Thr Gly Ala 260 265 270 Trp Phe Ala Ser Glu His Glu Gly Val Glu Pro Asp Leu Val Thr Phe 275 280 285 Ala Lys Gly Ile Ala Gly Gly Met Pro Leu Ser Gly Val Val Gly Arg 290 295 300 Ala Glu Ile Met Asp Ala Val His Pro Gly Gly Leu Gly Gly Thr Tyr 305 310 315 320 Gly Gly Asn Pro Val Ala Cys Ala Ala Ala Leu Gly Ala Leu Glu Ala 325 330 335 Ile Glu Glu Trp Asp Leu Val Ala Arg Ala Gln Glu Ile Glu Lys Val 340 345 350 Ile Arg Glu Glu Leu Gly Ser Val Ala Glu Ser Ser Pro Val Val Gly 355 360 365 Asp Leu Arg Gly Arg Gly Ala Met Ile Ala Leu Glu Phe Val Lys Pro 370 375 380 Gly Thr Thr Glu Pro Asn Pro Asp Ala Ala Lys Gln Ile Ala Ala Arg 385 390 395 400 Cys Leu Glu Gln Gly Val Ala Ile Leu Thr Cys Gly Thr Tyr Gly Asn 405 410 415 Ile Val Arg Leu Leu Pro Pro Leu Val Ile Asp Met Asp Leu Leu Arg 420 425 430 Asp Ala Leu Gly Val Phe Ala Ala Ala Ile Gln Glu Val Gly Ala 435 440 445 <210> 137 <211> 468 <212> PRT <213> Artificial Sequence <220> <223> Arthrobacter sp. FB24 <400> 137 Met Val Glu Leu Val Glu Thr Arg Thr Gly Thr His Gln Lys Gly Ile 1 5 10 15 Pro Met Thr Ala Thr Ala Pro Asp Ile Thr Tyr Arg Leu Glu Gln Lys 20 25 30 Arg Arg Val Gln Ala Asp Phe Pro Gly Pro Lys Ser Val Ala Leu Thr 35 40 45 Glu Arg Arg Lys Ala Val Val Ala Ala Gly Val Ala Ser Ser Val Pro 50 55 60 Val Phe Val Ser Asp Ala Asp Gly Gly Ile Ile His Asp Val Asp Gly 65 70 75 80 Asn Ser Phe Ile Asp Leu Gly Ser Gly Ile Ala Val Thr Ser Val Gly 85 90 95 Ala Ser Asp Pro Ala Val Val Gly Ala Val Lys Glu Ala Val Glu His 100 105 110 Phe Thr His Thr Cys Phe Met Val Thr Pro Tyr Glu Gly Tyr Val Ala 115 120 125 Val Ala Glu Gln Leu Asn Arg Leu Thr Pro Gly Asp His Glu Lys Arg 130 135 140 Thr Val Leu Phe Asn Ser Gly Ala Glu Ala Val Glu Asn Ala Val Lys 145 150 155 160 Val Ala Arg Leu Ala Thr Gly Arg Asp Ala Val Val Ala Phe Asp His 165 170 175 Ala Tyr His Gly Arg Thr Asn Leu Thr Met Ala Leu Thr Ala Lys Ala 180 185 190 Met Pro Tyr Lys Thr Asn Phe Gly Pro Phe Ala Pro Glu Val Tyr Arg 195 200 205 Met Pro Met Ser Tyr Pro Phe Arg Glu Glu Asn Pro Ala Ile Thr Gly 210 215 220 Ala Glu Ala Ala Lys Arg Ala Ile Thr Ala Ile Glu Lys Gln Ile Gly 225 230 235 240 Gly Glu Gln Val Ala Ala Ile Ile Ile Glu Pro Ile Gln Gly Glu Gly 245 250 255 Gly Phe Ile Val Pro Ala Asp Gly Phe Leu Pro Ala Leu Ala Ala Trp 260 265 270 Ala Lys Glu Lys Gly Ile Val Phe Ile Ala Asp Glu Val Gln Ser Gly 275 280 285 Phe Cys Arg Thr Gly Glu Trp Phe Ala Val Asn His Glu Gly Val Val 290 295 300 Pro Asp Ile Ile Thr Met Ala Lys Gly Ile Ala Gly Gly Met Pro Leu 305 310 315 320 Ser Ala Ile Thr Gly Arg Ala Asp Leu Leu Asp Ala Val His Pro Gly 325 330 335 Gly Leu Gly Gly Thr Tyr Gly Gly Asn Pro Val Ala Cys Ala Ala Ala 340 345 350 Leu Ala Ser Ile Gly Ser Met Glu Glu Tyr Asp Leu Asn Ala Arg Ala 355 360 365 Lys His Ile Glu Glu Leu Ala Thr Gly Arg Leu Arg Glu Leu Gln Gly 370 375 380 Glu Val Ser Val Ile Gly Asp Ile Arg Gly Arg Gly Ala Met Leu Ala 385 390 395 400 Ile Glu Leu Val Gln Ala Gly Ser Lys Glu Pro Asn Pro Glu Leu Thr 405 410 415 Lys Ala Val Ala Ala Ala Cys Leu Lys Glu Gly Val Ile Ile Leu Thr 420 425 430 Cys Gly Thr Tyr Gly Asn Val Ile Arg Leu Leu Pro Pro Leu Val Ile 435 440 445 Gly Asp Glu Leu Leu Leu Asp Gly Leu Glu Val Leu Ala Ala Ala Ile 450 455 460 Lys Ala His Ala 465 <210> 138 <211> 426 <212> PRT <213> Artificial Sequence <220> <223> Pseudomonas sp. AAC <400> 138 Met Ser Lys Thr Asn Glu Ser Leu Leu Gln Arg Arg Gln Ala Ala Val 1 5 10 15 Pro Arg Gly Val Gly Gln Ile His Pro Val Val Ala Glu Arg Ala Glu 20 25 30 Asn Ala Thr Val Trp Asp Val Glu Gly Arg Glu Tyr Ile Asp Phe Ala 35 40 45 Gly Gly Ile Ala Val Leu Asn Thr Gly His Leu His Pro Lys Val Val 50 55 60 Ala Ala Val Gln Glu Gln Leu Thr Lys Leu Ser His Thr Cys Phe Gln 65 70 75 80 Val Leu Ala Tyr Glu Pro Tyr Ile Glu Leu Ala Glu Glu Ile Ala Lys 85 90 95 Arg Val Pro Gly Asn Phe Pro Lys Lys Thr Leu Leu Val Thr Ser Gly 100 105 110 Ser Glu Ala Val Glu Asn Ala Val Lys Ile Ala Arg Ala Ala Thr Gly 115 120 125 Arg Ala Gly Val Ile Ala Phe Thr Gly Ala Tyr His Gly Arg Thr Met 130 135 140 Met Thr Leu Gly Leu Thr Gly Lys Val Val Pro Tyr Ser Ala Gly Met 145 150 155 160 Gly Leu Met Pro Gly Gly Ile Phe Arg Ala Leu Ala Pro Cys Glu Leu 165 170 175 His Gly Ile Ser Glu Asp Glu Ser Ile Ala Ser Ile Glu Arg Ile Phe 180 185 190 Lys Asn Asp Ala Gln Pro Arg Asp Ile Ala Ala Ile Ile Ile Glu Pro 195 200 205 Val Gln Gly Glu Gly Gly Phe Tyr Val Asn Ser Lys Pro Phe Met Gln 210 215 220 Arg Leu Arg Ala Leu Cys Asp Glu His Gly Ile Leu Leu Ile Ala Asp 225 230 235 240 Glu Val Gln Thr Gly Ala Gly Arg Thr Gly Thr Phe Phe Ala Thr Glu 245 250 255 Gln Leu Gly Ile Val Pro Asp Leu Thr Thr Phe Ala Lys Ser Val Gly 260 265 270 Gly Gly Phe Pro Ile Ser Gly Val Val Gly Lys Ala Glu Ile Met Asp 275 280 285 Ala Ile Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Ser Pro Ile 290 295 300 Ala Cys Ala Ala Ala Leu Ala Val Leu Lys Val Phe Asp Glu Glu Lys 305 310 315 320 Leu Leu Glu Arg Ser Gln Ala Val Gly Glu Thr Leu Lys Ala Gly Leu 325 330 335 Arg Glu Ile Gln Ala Lys His Lys Val Ile Gly Asp Val Arg Gly Leu 340 345 350 Gly Ser Met Val Ala Ile Glu Leu Phe Glu Gly Gly Asp Val Asn Lys 355 360 365 Pro Ala Ala Glu Leu Val Ser Lys Ile Val Val Arg Ala Arg Glu Lys 370 375 380 Gly Leu Ile Leu Leu Ser Cys Gly Thr Tyr Tyr Asn Val Ile Arg Phe 385 390 395 400 Leu Met Pro Val Thr Ile Pro Asp Ala Gln Leu Lys Gln Gly Leu Ala 405 410 415 Ile Leu Ala Glu Cys Phe Asp Glu Leu Ala 420 425 <210> 139 <211> 426 <212> PRT <213> Artificial Sequence <220> <223> Pseudomonas putida KG-4 <400> 139 Met Ser Lys Thr Asn Glu Ser Leu Met Gln Arg Arg Val Ala Ala Val 1 5 10 15 Pro Arg Gly Val Gly Gln Ile His Pro Ile Phe Ala Glu Ser Ala Arg 20 25 30 Asn Ala Thr Val Thr Asp Val Glu Gly Arg Glu Phe Ile Asp Phe Ala 35 40 45 Gly Gly Ile Ala Val Leu Asn Thr Gly His Val His Pro Lys Ile Ile 50 55 60 Ala Ala Val Glu Ala Gln Leu His Lys Leu Thr His Thr Cys Phe Gln 65 70 75 80 Val Leu Ala Tyr Glu Pro Tyr Val Glu Val Cys Glu Lys Ile Asn Ala 85 90 95 Leu Ile Pro Gly Asp Phe Ala Lys Lys Thr Leu Leu Val Thr Thr Gly 100 105 110 Ser Glu Ala Val Glu Asn Ala Ile Lys Ile Ala Arg Ala Ala Thr Gly 115 120 125 Arg Ala Gly Val Ile Ala Phe Thr Gly Ala Tyr His Gly Arg Thr Met 130 135 140 Met Thr Leu Gly Leu Thr Gly Lys Val Val Pro Tyr Ser Ala Gly Met 145 150 155 160 Gly Leu Met Pro Gly Gly Ile Phe Arg Ala Ile Tyr Pro Asn Glu Leu 165 170 175 His Gly Val Ser Ile Asp Asp Ser Ile Ala Ser Ile Glu Arg Ile Phe 180 185 190 Lys Asn Asp Ala Glu Ala Lys Asp Ile Ala Ala Ile Ile Leu Glu Pro 195 200 205 Val Gln Gly Glu Gly Gly Phe Tyr Val Ala Pro Lys Glu Phe Met Lys 210 215 220 Arg Leu Arg Ala Leu Cys Asp Gln His Gly Ile Leu Leu Ile Ala Asp 225 230 235 240 Glu Val Gln Thr Gly Ala Gly Arg Thr Gly Thr Phe Phe Ala Met Glu 245 250 255 Gln Met Gly Val Ala Pro Asp Leu Thr Thr Phe Ala Lys Ser Ile Ala 260 265 270 Gly Gly Phe Pro Leu Ala Gly Val Cys Gly Lys Ala Glu Tyr Met Asp 275 280 285 Ala Ile Ala Pro Gly Gly Leu Gly Gly Thr Tyr Ala Gly Ser Pro Ile 290 295 300 Ala Cys Ala Ala Ala Leu Ala Val Met Glu Val Phe Glu Glu Glu Lys 305 310 315 320 Leu Leu Asp Arg Ser Lys Ala Val Gly Glu Arg Leu Val Thr Gly Leu 325 330 335 Arg Lys Ile Gln Asp Lys His Pro Ile Ile Gly Asp Val Arg Ala Leu 340 345 350 Gly Ser Met Ile Ala Val Glu Val Phe Asp Lys Ala Gly Ser His Thr 355 360 365 Pro Asn Pro Thr Ala Val Ala Ala Val Val Ala Lys Ala Arg Asp Lys 370 375 380 Gly Leu Ile Leu Leu Ser Cys Gly Thr Tyr Gly Asn Val Leu Arg Ile 385 390 395 400 Leu Val Pro Leu Thr Ser Pro Asp Glu Gln Leu Asp Lys Gly Leu Ala 405 410 415 Ile Ile Glu Glu Cys Phe Ala Glu Leu Ala 420 425 <210> 140 <211> 442 <212> PRT <213> Artificial Sequence <220> <223> Alcaligenes A. faecalis <400> 140 Met Ser Lys Asp Lys Ala Met Leu Asn Ala Phe Asp Pro Ala Ala Ala 1 5 10 15 Asp Ser Leu Pro Ala Ala Glu Arg Ala Leu Ile Glu Arg Arg Gln Arg 20 25 30 Val Leu Gly Thr Ala Tyr Arg Leu Phe Tyr Asp Asn Pro Leu His Ile 35 40 45 Val Arg Gly Glu Gly Val Trp Leu Tyr Asp Ala Ala Gly Glu Arg Tyr 50 55 60 Leu Asp Ala Tyr Asn Asn Val Ala Ser Val Gly His Ser His Pro Arg 65 70 75 80 Val Val Ala Ala Ile Ala Glu Gln Ala Ala Ile Leu Asn Thr His Thr 85 90 95 Arg Tyr Leu His Asp Gly Val Val Glu Tyr Ala Glu Arg Leu Val Ala 100 105 110 Thr Phe Pro Ser Ala Leu Ser Gln Ala Met Phe Thr Cys Thr Gly Ser 115 120 125 Glu Ala Asn Asp Leu Ala Leu Arg Ile Ala Arg Ser His Thr Gly Ala 130 135 140 Ser Gly Val Ile Val Thr Glu Leu Ala Tyr His Gly Val Thr Ala Ala 145 150 155 160 Val Ala Ala Val Ser Pro Ser Leu Gly Lys Thr Val Pro Leu Gly Val 165 170 175 Asp Val Arg Ala Val Ser Ala Pro Asp Thr Tyr Arg His Asp Pro Ala 180 185 190 Thr Ile Gly Val Trp Phe Ala Ala Arg Val Gln Glu Ala Ile Asp Asp 195 200 205 Met Leu Arg His Gly Ile Arg Pro Ala Ala Leu Leu Val Asp Thr Val 210 215 220 Phe Ser Ser Asp Gly Val Tyr Thr Asp Pro Ala Pro Phe Leu Ala Pro 225 230 235 240 Ala Val Glu Ala Ile Arg Ala Ala Gly Gly Leu Phe Ile Ala Asp Glu 245 250 255 Val Gln Ala Gly Phe Ala Arg Thr Gly Ser Cys Met Trp Gly Phe Gln 260 265 270 Arg His Gly Leu Val Pro Asp Ile Val Thr Met Gly Lys Pro Met Gly 275 280 285 Asn Gly His Pro Ile Ala Gly Val Val Ala Arg Pro Glu Ile Phe Glu 290 295 300 Arg Phe Gly Arg Asp Ala Arg Tyr Phe Asn Thr Phe Gly Gly Asn Pro 305 310 315 320 Val Ser Cys Ala Ala Ala Leu Ala Thr Leu Asp Val Ile Gln Asp Glu 325 330 335 Gly Leu Gln Ala Asn Ala Ala Arg Thr Gly Ala Tyr Leu Arg Asp Lys 340 345 350 Phe Arg Glu Met Ala Arg Lys His Ser Trp Ile Gly Asp Val Arg Gly 355 360 365 Asp Gly Leu Phe Met Gly Ile Glu Leu Val Lys Asp Gln Ala Ala Lys 370 375 380 Thr Pro Ala Thr Glu Glu Thr His Arg Phe Val Asn Leu Met Arg Glu 385 390 395 400 His Arg Val Leu Leu Ser Ala Thr Gly Leu Arg Gly Asn Val Ile Lys 405 410 415 Leu Arg Pro Gln Leu Pro Phe Ser Leu Glu Asn Ala Asp Gln Leu Met 420 425 430 Gln Ala Ala Asp Glu Val Phe Ala Lys Leu 435 440 <210> 141 <211> 453 <212> PRT <213> Artificial Sequence <220> <223> Clostridium kluyveri DSM555 <400> 141 Met Ser Asn Glu Val Ser Ile Lys Glu Leu Ile Glu Lys Ala Lys Val 1 5 10 15 Ala Gln Lys Lys Leu Glu Ala Tyr Ser Gln Glu Gln Val Asp Val Leu 20 25 30 Val Lys Ala Leu Gly Lys Val Val Tyr Asp Asn Ala Glu Met Phe Ala 35 40 45 Lys Glu Ala Val Glu Glu Thr Glu Met Gly Val Tyr Glu Asp Lys Val 50 55 60 Ala Lys Cys His Leu Lys Ser Gly Ala Ile Trp Asn His Ile Lys Asp 65 70 75 80 Lys Lys Thr Val Gly Ile Ile Lys Glu Glu Pro Glu Arg Ala Leu Val 85 90 95 Tyr Val Ala Lys Pro Lys Gly Val Val Ala Ala Thr Thr Pro Ile Thr 100 105 110 Asn Pro Val Val Thr Pro Met Cys Asn Ala Met Ala Ala Ile Lys Gly 115 120 125 Arg Asn Thr Ile Ile Val Ala Pro His Pro Lys Ala Lys Lys Val Ser 130 135 140 Ala His Thr Val Glu Leu Met Asn Ala Glu Leu Lys Lys Leu Gly Ala 145 150 155 160 Pro Glu Asn Ile Ile Gln Ile Val Glu Ala Pro Ser Arg Glu Ala Ala 165 170 175 Lys Glu Leu Met Glu Ser Ala Asp Val Val Ile Ala Thr Gly Gly Ala 180 185 190 Gly Arg Val Lys Ala Ala Tyr Ser Ser Gly Arg Pro Ala Tyr Gly Val 195 200 205 Gly Pro Gly Asn Ser Gln Val Ile Val Asp Lys Gly Tyr Asp Tyr Asn 210 215 220 Lys Ala Ala Gln Asp Ile Ile Thr Gly Arg Lys Tyr Asp Asn Gly Ile 225 230 235 240 Ile Cys Ser Ser Glu Gln Ser Val Ile Ala Pro Ala Glu Asp Tyr Asp 245 250 255 Lys Val Ile Ala Ala Phe Val Glu Asn Gly Ala Phe Tyr Val Glu Asp 260 265 270 Glu Glu Thr Val Glu Lys Phe Arg Ser Thr Leu Phe Lys Asp Gly Lys 275 280 285 Ile Asn Ser Lys Ile Ile Gly Lys Ser Val Gln Ile Ile Ala Asp Leu 290 295 300 Ala Gly Val Lys Val Pro Glu Gly Thr Lys Val Ile Val Leu Lys Gly 305 310 315 320 Lys Gly Ala Gly Glu Lys Asp Val Leu Cys Lys Glu Lys Met Cys Pro 325 330 335 Val Leu Val Ala Leu Lys Tyr Asp Thr Phe Glu Glu Ala Val Glu Ile 340 345 350 Ala Met Ala Asn Tyr Met Tyr Glu Gly Ala Gly His Thr Ala Gly Ile 355 360 365 His Ser Asp Asn Asp Glu Asn Ile Arg Tyr Ala Gly Thr Val Leu Pro 370 375 380 Ile Ser Arg Leu Val Val Asn Gln Pro Ala Thr Thr Ala Gly Gly Ser 385 390 395 400 Phe Asn Asn Gly Phe Asn Pro Thr Thr Thr Leu Gly Cys Gly Ser Trp 405 410 415 Gly Arg Asn Ser Ile Ser Glu Asn Leu Thr Tyr Glu His Leu Ile Asn 420 425 430 Val Ser Arg Ile Gly Tyr Phe Asn Lys Glu Ala Lys Val Pro Ser Tyr 435 440 445 Glu Glu Ile Trp Gly 450 <210> 142 <211> 451 <212> PRT <213> Artificial Sequence <220> <223> Porphyromonas gingivalis W83 <400> 142 Met Glu Ile Lys Glu Met Val Ser Leu Ala Arg Lys Ala Gln Lys Glu 1 5 10 15 Tyr Gln Ala Thr His Asn Gln Glu Ala Val Asp Asn Ile Cys Arg Ala 20 25 30 Ala Ala Lys Val Ile Tyr Glu Asn Ala Ala Ile Leu Ala Arg Glu Ala 35 40 45 Val Asp Glu Thr Gly Met Gly Val Tyr Glu His Lys Val Ala Lys Asn 50 55 60 Gln Gly Lys Ser Lys Gly Val Trp Tyr Asn Leu His Asn Lys Lys Ser 65 70 75 80 Ile Gly Ile Leu Asn Ile Asp Glu Arg Thr Gly Met Ile Glu Ile Ala 85 90 95 Lys Pro Ile Gly Val Val Gly Ala Val Thr Pro Thr Thr Asn Pro Ile 100 105 110 Val Thr Pro Met Ser Asn Ile Ile Phe Ala Leu Lys Thr Cys Asn Ala 115 120 125 Ile Ile Ile Ala Pro His Pro Arg Ser Lys Lys Cys Ser Ala His Ala 130 135 140 Val Arg Leu Ile Lys Glu Ala Ile Ala Pro Phe Asn Val Pro Glu Gly 145 150 155 160 Met Val Gln Ile Ile Glu Glu Pro Ser Ile Glu Lys Thr Gln Glu Leu 165 170 175 Met Gly Ala Val Asp Val Val Val Ala Thr Gly Gly Met Gly Met Val 180 185 190 Lys Ser Ala Tyr Ser Ser Gly Lys Pro Ser Phe Gly Val Gly Ala Gly 195 200 205 Asn Val Gln Val Ile Val Asp Ser Asn Ile Asp Phe Glu Ala Ala Ala 210 215 220 Glu Lys Ile Ile Thr Gly Arg Ala Phe Asp Asn Gly Ile Ile Cys Ser 225 230 235 240 Gly Glu Gln Ser Ile Ile Tyr Asn Glu Ala Asp Lys Glu Ala Val Phe 245 250 255 Thr Ala Phe Arg Asn His Gly Ala Tyr Phe Cys Asp Glu Ala Glu Gly 260 265 270 Asp Arg Ala Arg Ala Ala Ile Phe Glu Asn Gly Ala Ile Ala Lys Asp 275 280 285 Val Val Gly Gln Ser Val Ala Phe Ile Ala Lys Lys Ala Asn Ile Asn 290 295 300 Ile Pro Glu Gly Thr Arg Ile Leu Val Val Glu Ala Arg Gly Val Gly 305 310 315 320 Ala Glu Asp Val Ile Cys Lys Glu Lys Met Cys Pro Val Met Cys Ala 325 330 335 Leu Ser Tyr Lys His Phe Glu Glu Gly Val Glu Ile Ala Arg Thr Asn 340 345 350 Leu Ala Asn Glu Gly Asn Gly His Thr Cys Ala Ile His Ser Asn Asn 355 360 365 Gln Ala His Ile Ile Leu Ala Gly Ser Glu Leu Thr Val Ser Arg Ile 370 375 380 Val Val Asn Ala Pro Ser Ala Thr Thr Ala Gly Gly His Ile Gln Asn 385 390 395 400 Gly Leu Ala Val Thr Asn Thr Leu Gly Cys Gly Ser Trp Gly Asn Asn 405 410 415 Ser Ile Ser Glu Asn Phe Thr Tyr Lys His Leu Leu Asn Ile Ser Arg 420 425 430 Ile Ala Pro Leu Asn Ser Ser Ile His Ile Pro Asp Asp Lys Glu Ile 435 440 445 Trp Glu Leu 450 <210> 143 <211> 463 <212> PRT <213> Artificial Sequence <220> <223> Clostridium difficile 630 <400> 143 Met Glu Lys Ala Val Glu Asn Phe Glu Asp Leu Ser Lys Glu Tyr Ile 1 5 10 15 Asn Gly Tyr Ile Glu Arg Ala Arg Lys Ala Gln Arg Glu Phe Glu Cys 20 25 30 Tyr Thr Gln Glu Gln Val Asp Lys Ile Val Lys Ile Val Gly Lys Val 35 40 45 Val Tyr Tyr Asn Ala Glu Tyr Leu Ala Lys Leu Ala Val Glu Glu Thr 50 55 60 Gly Met Gly Val Tyr Glu Asp Lys Val Ala Lys Asn Lys Ser Lys Ala 65 70 75 80 Lys Val Ile Tyr Asn Asn Leu Lys Asp Lys Lys Ser Val Gly Ile Ile 85 90 95 Asp Ile Asp Arg Glu Thr Gly Ile Thr Lys Val Ala Lys Pro Val Gly 100 105 110 Val Val Ala Ala Ile Thr Pro Cys Thr Asn Pro Ile Val Thr Pro Met 115 120 125 Ser Asn Ala Met Phe Ala Leu Lys Gly Arg Asn Ala Ile Ile Ile Thr 130 135 140 Pro His His Lys Ala Ile Gly Cys Ser Thr Lys Thr Val Glu Met Ile 145 150 155 160 Asn Glu Glu Leu Glu Lys Ile Gly Ala Pro Glu Asn Leu Ile Gln Ile 165 170 175 Leu Asp Gln Gln Ser Arg Glu Asn Thr Arg Asn Leu Ile Ser Ser Ala 180 185 190 Asp Val Val Ile Ala Thr Gly Gly Met Gly Met Val Lys Ala Ala Tyr 195 200 205 Ser Ser Gly Lys Pro Ala Leu Gly Val Gly Ala Gly Asn Val Gln Cys 210 215 220 Ile Ile Asp Arg Asp Val Asp Ile Lys Glu Ala Val Pro Lys Ile Ile 225 230 235 240 Ala Gly Arg Ile Phe Asp Asn Gly Ile Ile Cys Ser Gly Glu Gln Ser 245 250 255 Val Ile Val Ala Glu Glu Met Phe Asp Lys Ile Met Asp Glu Phe Lys 260 265 270 Asn Asn Lys Gly Phe Ile Val Arg Asp Lys Val Gln Lys Glu Ala Phe 275 280 285 Arg Asn Ala Met Phe Val Asn Lys Ser Met Asn Lys Asp Ala Val Gly 290 295 300 Gln Ser Val His Thr Ile Ala Lys Ile Ala Gly Val Glu Ile Pro Glu 305 310 315 320 Asp Thr Lys Ile Ile Val Ile Glu Ala Asp Gly Pro Gly Glu Glu Asp 325 330 335 Ile Ile Ala Lys Glu Lys Met Cys Pro Val Ile Ser Ala Tyr Lys Tyr 340 345 350 Lys Ser Phe Glu Glu Gly Val Ala Ile Ala Lys Ala Asn Leu Asn Val 355 360 365 Glu Gly Lys Gly His Ser Val Ser Ile His Ser Asn Thr Val Lys Asn 370 375 380 Ile Glu Tyr Ala Gly Glu Asn Ile Glu Val Ser Arg Phe Val Ile Asn 385 390 395 400 Gln Cys Cys Ala Thr Ser Ala Gly Gly Ser Phe Phe Asn Gly Leu Ala 405 410 415 Pro Thr Asn Thr Leu Gly Cys Gly Ser Trp Gly Asn Asn Ser Ile Ser 420 425 430 Glu Asn Leu Asp Tyr Lys His Leu Ile Asn Ile Ser Arg Ile Ala Tyr 435 440 445 Tyr Met Pro Glu Asn Glu Val Pro Thr Asp Glu Glu Leu Trp Gly 450 455 460 <210> 144 <211> 364 <212> PRT <213> Artificial Sequence <220> <223> Candida tropicalis <400> 144 Met Ile Thr Ala Gln Ala Val Leu Tyr Thr Gln His Gly Glu Pro Lys 1 5 10 15 Asp Val Leu Phe Thr Gln Ser Phe Glu Ile Asp Asp Asp Asn Leu Ala 20 25 30 Pro Asn Glu Val Ile Val Lys Thr Leu Gly Ser Pro Val Asn Pro Ser 35 40 45 Asp Ile Asn Gln Ile Gln Gly Val Tyr Pro Ser Lys Pro Ala Lys Thr 50 55 60 Thr Gly Phe Gly Thr Thr Glu Pro Ala Ala Pro Cys Gly Asn Glu Gly 65 70 75 80 Leu Phe Glu Val Ile Lys Val Gly Ser Asn Val Leu Ser Leu Glu Ala 85 90 95 Gly Asp Trp Val Ile Pro Ser His Val Asn Phe Gly Thr Trp Arg Thr 100 105 110 His Ala Leu Gly Asn Asp Asp Asp Phe Ile Lys Leu Pro Asn Pro Ala 115 120 125 Gln Ser Lys Ala Asn Gly Lys Pro Asn Gly Leu Thr Ile Asn Gln Gly 130 135 140 Ala Thr Ile Ser Val Asn Pro Leu Thr Ala Tyr Leu Met Leu Thr His 145 150 155 160 Tyr Val Lys Leu Thr Pro Gly Lys Asp Trp Phe Ile Gln Asn Gly Gly 165 170 175 Thr Ser Ala Val Gly Lys Tyr Ala Ser Gln Ile Gly Lys Leu Leu Asn 180 185 190 Phe Asn Ser Ile Ser Val Ile Arg Asp Arg Pro Asn Leu Asp Glu Val 195 200 205 Val Ala Ser Leu Lys Glu Leu Gly Ala Thr Gln Val Ile Thr Glu Asp 210 215 220 Gln Asn Asn Ser Arg Glu Phe Gly Pro Thr Ile Lys Glu Trp Ile Lys 225 230 235 240 Gln Ser Gly Gly Glu Ala Lys Leu Ala Leu Asn Cys Val Gly Gly Lys 245 250 255 Ser Ser Thr Gly Ile Ala Arg Lys Leu Asn Asn Asn Gly Leu Met Leu 260 265 270 Thr Tyr Gly Gly Met Ser Phe Gln Pro Val Thr Ile Pro Thr Ser Leu 275 280 285 Tyr Ile Phe Lys Asn Phe Thr Ser Ala Gly Phe Trp Val Thr Glu Leu 290 295 300 Leu Lys Asn Asn Lys Glu Leu Lys Thr Leu Thr Leu Asn Gln Ile Ile 305 310 315 320 Ala Trp Tyr Glu Glu Gly Lys Leu Thr Asp Ala Lys Ser Ile Glu Thr 325 330 335 Leu Tyr Asp Gly Thr Lys Pro Leu His Glu Leu Tyr Gln Asp Gly Val 340 345 350 Ala Asn Ser Lys Asp Gly Lys Gln Leu Ile Thr Tyr 355 360 <210> 145 <211> 340 <212> PRT <213> Artificial Sequence <220> <223> Drosophila melanogaster <400> 145 Met Met Ser Val Val Ala Lys Ser Leu Lys Tyr Thr Gln His Gly Glu 1 5 10 15 Pro Gln Glu Val Leu Gln Leu Val Glu Asp Lys Leu Pro Asp Pro Lys 20 25 30 Asp Asn Gln Val Leu Val Lys Ile Leu Ala Ala Pro Ile Asn Pro Ala 35 40 45 Asp Ile Asn Thr Ile Gln Gly Lys Tyr Pro Val Lys Pro Lys Phe Pro 50 55 60 Ala Val Gly Gly Asn Glu Cys Val Ala Glu Val Ile Cys Val Gly Asp 65 70 75 80 Lys Val Lys Gly Phe Glu Ala Gly Gln His Val Ile Pro Leu Ala Ser 85 90 95 Gly Leu Gly Thr Trp Thr Thr His Ala Val Tyr Lys Glu Asp Gln Leu 100 105 110 Leu Ile Val Ser Lys Lys Val Gly Leu Ala Glu Ala Ala Thr Ser Thr 115 120 125 Val Asn Pro Thr Thr Ala Tyr Arg Met Leu Lys Asp Phe Val Gln Leu 130 135 140 Cys Pro Gly Asp Thr Val Ile Gln Asn Gly Ala Asn Ser Ala Val Gly 145 150 155 160 Gln Ala Val His Gln Leu Cys Arg Ala Trp Gly Ile Asn Ser Val Gly 165 170 175 Ile Val Arg Asp Arg Pro Glu Ile Ala Glu Leu Lys Gln Met Leu Gln 180 185 190 Cys Leu Gly Ala Thr Glu Val Leu Thr Glu Ala Glu Ile Arg Thr Ser 195 200 205 Asp Ile Phe Lys Ser Gly Lys Leu Lys Lys Pro Arg Leu Ala Phe Asn 210 215 220 Cys Val Gly Gly Lys Ser Ala Thr Glu Val Ser Arg His Leu Asp Asn 225 230 235 240 Gly Gly Val Leu Val Thr Tyr Gly Gly Met Ser Arg Glu Pro Val Thr 245 250 255 Val Ala Thr Gly Pro Leu Ile Phe Lys Asp Ile Ala Phe Arg Gly Phe 260 265 270 Trp Met Thr Arg Trp Ser Lys Glu Asn Tyr Ser Ser Pro Glu Arg Ser 275 280 285 Lys Met Phe Lys Glu Ile Phe Glu Leu Met Glu Gln Gly Lys Phe Val 290 295 300 Ala Pro Asn His Glu Met Val Pro Leu Ala Lys Phe Lys Asp Ala Ala 305 310 315 320 Ala Ala Ala Leu Ser Phe Lys Gly Phe Thr Gly Lys Lys Tyr Ile Leu 325 330 335 Asp Met Ser Ile 340 <210> 146 <211> 1266 <212> DNA <213> Artificial Sequence <220> <223> Nucleic Acid Sequence of SEQ ID NO: 1 <400> 146 atgaagaatc aggacctgaa tacccgccgt tccctggcca cgccgcgcgg cgtcggcgtc 60 atgtgcgact tctacgcggt gcgcgccgaa aacgccaccc tgtgggacgc caatggcaag 120 gaatacatcg atttcgcagg cggcatcgcc gtcctgaaca cgggccacct gcacccgaag 180 atcaaggccg ccgttgccgc gcagctggac aacttcacgc acacggccta ccagatcgtg 240 ccgtacgaag gctatgtctc gctggccgag cgcatcaacc gcctcgcccc catcgacggc 300 ctgaagaaga gcgccttctt caccaccggc gtggaagccg tcgaaaacgc cgtcaagatc 360 gcgcgttcgg ccaccggccg ctcgggcgtc atcgccttct cgggctcgtt ccacggccgc 420 accatgctgg gcatggcgct gactggcaag gtcgccccgt acaagctgtc gttcggtccg 480 atgccgggcg acatctatca cgtgcccttc cccaacgcca cccagtccat cagcgtggcg 540 gactcgctca aggcgctgga cctgctgttc aagtgcgaca tcgatcccaa gcgcgtcgcg 600 gccatcatca tcgaaccggt gcagggtgaa ggcggcttca acatcacccc gcccgagttg 660 atgacggcgc tgcgcaaggt ctgcgacgag cacggcattc tgctgatcgc cgacgaagtc 720 cagaccggct tcggccgcac cggcaagctg ttcgccatgg agcaccactc ggtccaggcc 780 gacctgatca ccatggccaa gagcctgggc ggcggcttcc cgatatcggg cgtggtcggc 840 cgcgccgacg tcatggacgc gcccgccgcc ggcggcctgg gcggcaccta cgccggcaac 900 ccgctggcgg tcgccgcggc gcatgccgtg ctggacgtga tcgccgagga aaagctgtgc 960 gaacgcgccg acgccctggg cgacaagctg cgcgcgcatc tggaaggcct gcgcgccaag 1020 gttccgggca tcgccgacgt gcgcggcctg ggttccatgg tcgccctgga actgaacgat 1080 cccgccaccg gcaagccgga cgcggaagcg gtcaagcgcg tgcaagcccg cgccatcgaa 1140 aagggcctga ttttgctaag ctgcggtgtg tacggcaacg tcctgcgctt cctgtacccc 1200 ttgaccatcc ccgacgccca gttcgatcgc gcgctggcca tcctgtccga ggcgcttgcc 1260 gcctga 1266 <210> 147 <211> 1266 <212> DNA <213> Artificial Sequence <220> <223> Nucleic Acid Sequence of SEQ ID NO: 1-Codon Optimized <400> 147 atgaaaaatc aggatctgaa tacccgtcgt agcctggcaa caccgcgtgg tgtgggtgtt 60 atgtgtgatt tttatgcagt tcgtgcagaa aatgcaaccc tgtgggatgc aaatggcaaa 120 gaatatattg attttgccgg tggtattgcc gtgctgaata ccggtcatct gcatccgaaa 180 atcaaagcag cagttgcagc acagctggat aactttaccc ataccgcata tcagattgtt 240 ccgtatgaag gttatgttag cctggccgaa cgtattaatc gtctggcacc gattgatggt 300 ctgaaaaaat cagcattttt taccaccggt gtggaagcag ttgaaaatgc agttaaaatt 360 gcacgtagcg caaccggtcg tagcggtgtt attgcattta gcggtagctt tcatggtcgt 420 accatgctgg gtatggcact gaccggtaaa gttgcaccgt ataaactgag ctttggtccg 480 atgcctggtg atatttatca tgttccgttt ccgaatgcca cccagagcat tagcgttgca 540 gatagcctga aagcactgga tctgctgttt aaatgtgata ttgatccgaa acgtgtggca 600 gccattatta tcgaaccggt gcagggtgaa ggtggtttta acattacccc tccggaactg 660 atgaccgcac tgcgtaaagt ttgtgatgaa catggtattc tgctgattgc agatgaagtt 720 cagaccggtt ttggtcgcac cggtaaactg tttgcaatgg aacatcatag cgttcaggca 780 gatctgatta ccatggcaaa aagcctgggt ggtggttttc cgattagcgg tgtggttggt 840 cgtgcagatg ttatggatgc accggcagcg ggtggtctgg gtggtacata tgcaggtaat 900 ccgctggcag ttgccgcagc acatgcagtt ctggatgtta ttgccgaaga aaaactgtgt 960 gaacgtgccg atgcactggg cgataaactg cgtgcacatc tggaaggtct gcgtgcaaaa 1020 gttccgggta ttgcggatgt tcgcggtctg ggtagcatgg ttgcactgga actgaatgat 1080 ccggcaaccg gcaaaccgga tgccgaagca gttaaacgtg ttcaggcacg tgcgattgaa 1140 aaaggtctga ttctgctgtc atgtggtgtt tatggtaatg ttctgcgttt tctgtatccg 1200 ctgaccattc cggatgcaca gtttgatcgt gcactggcaa ttctgagcga agcactggca 1260 gcatag 1266 <210> 148 <211> 1266 <212> DNA <213> Artificial Sequence <220> <223> Nucleic Acid Sequence of SEQ ID NO: 1-Codon Optimized <400> 148 atgaaaaatc aggatctgaa tacccgtcgt agcctggcaa caccgcgtgg tgtgggtgtt 60 atgtgtgatt tttatgcagt tcgtgcagaa aatgcaaccc tgtgggatgc aaatggcaaa 120 gaatatattg attttgccgg tggtattgcc gtgctgaata ccggtcatct gcatccgaaa 180 atcaaagcag cagttgcagc acagctggat aactttaccc ataccgcata tcagattgtt 240 ccgtatgaag gttatgttag cctggccgaa cgtattaatc gtctggcacc gattgatggt 300 ctgaaaaaat cagcattttt taccaccggt gtggaagcag ttgaaaatgc agttaaaatt 360 gcacgtagcg caaccggtcg tagcggtgtt attgcattta gcggtagctt tcatggtcgt 420 accatgctgg gtatggcact gaccggtaaa gttgcaccgt ataaactgag ctttggtccg 480 atgcctggtg atatttatca tgttccgttt ccgaatgcca cccagagcat tagcgttgca 540 gatagcctga aagcactgga tctgctgttt aaatgtgata ttgatccgaa acgtgtggca 600 gccattatta tcgaaccggt gcagggtgaa ggtggtttta acattacccc tccggaactg 660 atgaccgcac tgcgtaaagt ttgtgatgaa catggtattc tgctgattgc agatgaagtt 720 cagaccggtt ttggtcgcac cggtaaactg tttgcaatgg aacatcatag cgttcaggca 780 gatctgatta ccatggcaaa aagcctgggt ggtggttttc cgattagcgg tgtggttggt 840 cgtgcagatg ttatggatgc accggcagcg ggtggtctgg gtggtacata tgcaggtaat 900 ccgctggcag ttgccgcagc acatgcagtt ctggatgtta ttgccgaaga aaaactgtgt 960 gaacgtgccg atgcactggg cgataaactg cgtgcacatc tggaaggtct gcgtgcaaaa 1020 gttccgggta ttgcggatgt tcgcggtctg ggtagcatgg ttgcactgga actgaatgat 1080 ccggcaaccg gcaaaccgga tgccgaagca gttaaacgtg ttcaggcacg tgcgattgaa 1140 aaaggtctga ttctgctgtc atgtggtgtt tatggtaatg ttctgcgttt tctgtatccg 1200 ctgaccattc cggatgcaca gtttgatcgt gcactggcaa ttctgagcga agcactggca 1260 gcataa 1266 <210> 149 <211> 1266 <212> DNA <213> Artificial Sequence <220> <223> Nucleic Acid Sequence of SEQ ID NO: 1-Codon Optimized <400> 149 atgaaaaatc aggacttaaa cacccgtcgc agcttagcca ctcctcgcgg ggtcggggtc 60 atgtgcgact tctatgcagt gcgtgccgag aacgcgacgc tgtgggatgc caacggcaaa 120 gaatatatcg attttgcggg cggtattgcc gtgttgaata cgggccacct gcatcctaag 180 ataaaggcag ctgtcgcggc gcaactggat aatttcacgc acaccgcata tcaaatcgta 240 ccatacgaag ggtacgtatc gctggccgaa agaattaacc gtttggcccc gattgacggt 300 ctaaaaaaaa gcgcgttttt cacaaccggt gtggaagcag tcgaaaacgc ggtaaaaatc 360 gcgcgtagcg ccactggccg ctccggtgtt atcgcgttca gcggaagttt ccatggccgc 420 actatgttag gcatggcgct gactgggaaa gttgcgccgt ataaactgag ctttgggccg 480 atgcctggcg atatttatca cgttccattc cctaacgcca ctcagtctat ttcagtcgcc 540 gattctttga aagcattaga cctgctgttt aaatgcgata ttgatcccaa acgcgtagca 600 gccataatta ttgagccggt tcagggagag ggcggcttca atatcacacc accggaactc 660 atgacggccc tgcgtaaggt atgcgacgaa catggtattc tcctgattgc agatgaagta 720 cagaccggat ttggccgcac cggtaaactg tttgctatgg agcaccactc tgtgcaagct 780 gatctgatca cgatggccaa aagtttaggc ggtggcttcc cgatctctgg cgtagtgggt 840 cgggcagatg tcatggatgc gcccgcagcg ggagggttag gtggtactta tgctggtaat 900 cctttggctg tagcagcagc gcacgcagtt cttgacgtga ttgcagaaga aaagttatgt 960 gaacgcgccg atgcattagg tgacaaattg cgggcacatc tggagggtct gcgcgcgaaa 1020 gttcctggca ttgcggatgt ccgcggtttg ggcagcatgg tggcactgga actgaacgac 1080 ccggctacgg gcaaacccga cgcagaagcc gtaaaacgtg ttcaggcgcg tgccattgaa 1140 aaaggcttaa ttttactgag ctgcggcgtc tacgggaatg tgttacgttt cctgtacccg 1200 ctgaccattc cggatgcgca atttgaccgg gccttagcga ttctgtctga ggccctggca 1260 gcatag 1266 <210> 150 <211> 1168 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium smegmatis MC2 155 <400> 150 Met Thr Ile Glu Thr Arg Glu Asp Arg Phe Asn Arg Arg Ile Asp His 1 5 10 15 Leu Phe Glu Thr Asp Pro Gln Phe Ala Ala Ala Arg Pro Asp Glu Ala 20 25 30 Ile Ser Ala Ala Ala Ala Asp Pro Glu Leu Arg Leu Pro Ala Ala Val 35 40 45 Lys Gln Ile Leu Ala Gly Tyr Ala Asp Arg Pro Ala Leu Gly Lys Arg 50 55 60 Ala Val Glu Phe Val Thr Asp Glu Glu Gly Arg Thr Thr Ala Lys Leu 65 70 75 80 Leu Pro Arg Phe Asp Thr Ile Thr Tyr Arg Gln Leu Ala Gly Arg Ile 85 90 95 Gln Ala Val Thr Asn Ala Trp His Asn His Pro Val Asn Ala Gly Asp 100 105 110 Arg Val Ala Ile Leu Gly Phe Thr Ser Val Asp Tyr Thr Thr Ile Asp 115 120 125 Ile Ala Leu Leu Glu Leu Gly Ala Val Ser Val Pro Leu Gln Thr Ser 130 135 140 Ala Pro Val Ala Gln Leu Gln Pro Ile Val Ala Glu Thr Glu Pro Lys 145 150 155 160 Val Ile Ala Ser Ser Val Asp Phe Leu Ala Asp Ala Val Ala Leu Val 165 170 175 Glu Ser Gly Pro Ala Pro Ser Arg Leu Val Val Phe Asp Tyr Ser His 180 185 190 Glu Val Asp Asp Gln Arg Glu Ala Phe Glu Ala Ala Lys Gly Lys Leu 195 200 205 Ala Gly Thr Gly Val Val Val Glu Thr Ile Thr Asp Ala Leu Asp Arg 210 215 220 Gly Arg Ser Leu Ala Asp Ala Pro Leu Tyr Val Pro Asp Glu Ala Asp 225 230 235 240 Pro Leu Thr Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys 245 250 255 Gly Ala Met Tyr Pro Glu Ser Lys Thr Ala Thr Met Trp Gln Ala Gly 260 265 270 Ser Lys Ala Arg Trp Asp Glu Thr Leu Gly Val Met Pro Ser Ile Thr 275 280 285 Leu Asn Phe Met Pro Met Ser His Val Met Gly Arg Gly Ile Leu Cys 290 295 300 Ser Thr Leu Ala Ser Gly Gly Thr Ala Tyr Phe Ala Ala Arg Ser Asp 305 310 315 320 Leu Ser Thr Phe Leu Glu Asp Leu Ala Leu Val Arg Pro Thr Gln Leu 325 330 335 Asn Phe Val Pro Arg Ile Trp Asp Met Leu Phe Gln Glu Tyr Gln Ser 340 345 350 Arg Leu Asp Asn Arg Arg Ala Glu Gly Ser Glu Asp Arg Ala Glu Ala 355 360 365 Ala Val Leu Glu Glu Val Arg Thr Gln Leu Leu Gly Gly Arg Phe Val 370 375 380 Ser Ala Leu Thr Gly Ser Ala Pro Ile Ser Ala Glu Met Lys Ser Trp 385 390 395 400 Val Glu Asp Leu Leu Asp Met His Leu Leu Glu Gly Tyr Gly Ser Thr 405 410 415 Glu Ala Gly Ala Val Phe Ile Asp Gly Gln Ile Gln Arg Pro Pro Val 420 425 430 Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe Ala Thr 435 440 445 Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Glu Gln Met 450 455 460 Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Ile Thr Ala Glu Met Phe Asp 465 470 475 480 Glu Asp Gly Tyr Tyr Arg Thr Gly Asp Ile Val Ala Glu Leu Gly Pro 485 490 495 Asp His Leu Glu Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Thr Val Ser Lys Leu Glu Ala Val Phe Gly Asp 515 520 525 Ser Pro Leu Val Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Leu Leu Ala Val Val Val Pro Thr Glu Glu Ala Leu Ser Arg Trp 545 550 555 560 Asp Gly Asp Glu Leu Lys Ser Arg Ile Ser Asp Ser Leu Gln Asp Ala 565 570 575 Ala Arg Ala Ala Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Leu 580 585 590 Val Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile 595 600 605 Arg Lys Leu Ala Arg Pro Lys Leu Lys Ala His Tyr Gly Glu Arg Leu 610 615 620 Glu Gln Leu Tyr Thr Asp Leu Ala Glu Gly Gln Ala Asn Glu Leu Arg 625 630 635 640 Glu Leu Arg Arg Asn Gly Ala Asp Arg Pro Val Val Glu Thr Val Ser 645 650 655 Arg Ala Ala Val Ala Leu Leu Gly Ala Ser Val Thr Asp Leu Arg Ser 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser 675 680 685 Phe Ser Asn Leu Leu His Glu Ile Phe Asp Val Asp Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Thr Asp Leu Ala Gly Val Ala Ala Tyr Ile 705 710 715 720 Glu Gly Glu Leu Arg Gly Ser Lys Arg Pro Thr Tyr Ala Ser Val His 725 730 735 Gly Arg Asp Ala Thr Glu Val Arg Ala Arg Asp Leu Ala Leu Gly Lys 740 745 750 Phe Ile Asp Ala Lys Thr Leu Ser Ala Ala Pro Gly Leu Pro Arg Ser 755 760 765 Gly Thr Glu Ile Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu 770 775 780 Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Leu Val Asp 785 790 795 800 Gly Lys Val Ile Cys Leu Val Arg Ala Arg Ser Asp Asp Glu Ala Arg 805 810 815 Ala Arg Leu Asp Ala Thr Phe Asp Thr Gly Asp Ala Thr Leu Leu Glu 820 825 830 His Tyr Arg Ala Leu Ala Ala Asp His Leu Glu Val Ile Ala Gly Asp 835 840 845 Lys Gly Glu Ala Asp Leu Gly Leu Asp His Asp Thr Trp Gln Arg Leu 850 855 860 Ala Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Ser Gln Met Phe Gly Pro Asn Ala Leu Gly Thr Ala 885 890 895 Glu Leu Ile Arg Ile Ala Leu Thr Thr Thr Ile Lys Pro Tyr Val Tyr 900 905 910 Val Ser Thr Ile Gly Val Gly Gln Gly Ile Ser Pro Glu Ala Phe Val 915 920 925 Glu Asp Ala Asp Ile Arg Glu Ile Ser Ala Thr Arg Arg Val Asp Asp 930 935 940 Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Glu Ala His Asp Trp Cys Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ser Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Gly Ser Phe Tyr Glu Leu Asp Ala Asp Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala Glu Ala 1025 1030 1035 Ile Ser Thr Ile Gly Ser Gln Val Thr Asp Gly Phe Glu Thr Phe 1040 1045 1050 His Val Met Asn Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu Tyr 1055 1060 1065 Val Asp Trp Leu Ile Glu Ala Gly Tyr Pro Val His Arg Val Asp 1070 1075 1080 Asp Tyr Ala Thr Trp Leu Ser Arg Phe Glu Thr Ala Leu Arg Ala 1085 1090 1095 Leu Pro Glu Arg Gln Arg Gln Ala Ser Leu Leu Pro Leu Leu His 1100 1105 1110 Asn Tyr Gln Gln Pro Ser Pro Pro Val Cys Gly Ala Met Ala Pro 1115 1120 1125 Thr Asp Arg Phe Arg Ala Ala Val Gln Asp Ala Lys Ile Gly Pro 1130 1135 1140 Asp Lys Asp Ile Pro His Val Thr Ala Asp Val Ile Val Lys Tyr 1145 1150 1155 Ile Ser Asn Leu Gln Met Leu Gly Leu Leu 1160 1165 <210> 151 <211> 1174 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium smegmatis MC2 155 <400> 151 Met Gly Thr Ser Asp Val His Asp Ala Thr Asp Gly Val Thr Glu Thr 1 5 10 15 Ala Leu Asp Asp Glu Gln Ser Thr Arg Arg Ile Ala Glu Leu Tyr Ala 20 25 30 Thr Asp Pro Glu Phe Ala Ala Ala Ala Pro Leu Pro Ala Val Val Asp 35 40 45 Ala Ala His Lys Pro Gly Leu Arg Leu Ala Glu Ile Leu Gln Thr Leu 50 55 60 Phe Thr Gly Tyr Gly Asp Arg Pro Ala Leu Gly Tyr Arg Ala Arg Glu 65 70 75 80 Leu Ala Thr Asp Glu Gly Gly Arg Thr Val Thr Arg Leu Leu Pro Arg 85 90 95 Phe Asp Thr Leu Thr Tyr Ala Gln Val Trp Ser Arg Val Gln Ala Val 100 105 110 Ala Ala Ala Leu Arg His Asn Phe Ala Gln Pro Ile Tyr Pro Gly Asp 115 120 125 Ala Val Ala Thr Ile Gly Phe Ala Ser Pro Asp Tyr Leu Thr Leu Asp 130 135 140 Leu Val Cys Ala Tyr Leu Gly Leu Val Ser Val Pro Leu Gln His Asn 145 150 155 160 Ala Pro Val Ser Arg Leu Ala Pro Ile Leu Ala Glu Val Glu Pro Arg 165 170 175 Ile Leu Thr Val Ser Ala Glu Tyr Leu Asp Leu Ala Val Glu Ser Val 180 185 190 Arg Asp Val Asn Ser Val Ser Gln Leu Val Val Phe Asp His His Pro 195 200 205 Glu Val Asp Asp His Arg Asp Ala Leu Ala Arg Ala Arg Glu Gln Leu 210 215 220 Ala Gly Lys Gly Ile Ala Val Thr Thr Leu Asp Ala Ile Ala Asp Glu 225 230 235 240 Gly Ala Gly Leu Pro Ala Glu Pro Ile Tyr Thr Ala Asp His Asp Gln 245 250 255 Arg Leu Ala Met Ile Leu Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 260 265 270 Gly Ala Met Tyr Thr Glu Ala Met Val Ala Arg Leu Trp Thr Met Ser 275 280 285 Phe Ile Thr Gly Asp Pro Thr Pro Val Ile Asn Val Asn Phe Met Pro 290 295 300 Leu Asn His Leu Gly Gly Arg Ile Pro Ile Ser Thr Ala Val Gln Asn 305 310 315 320 Gly Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp Met Ser Thr Leu Phe 325 330 335 Glu Asp Leu Ala Leu Val Arg Pro Thr Glu Leu Gly Leu Val Pro Arg 340 345 350 Val Ala Asp Met Leu Tyr Gln His His Leu Ala Thr Val Asp Arg Leu 355 360 365 Val Thr Gln Gly Ala Asp Glu Leu Thr Ala Glu Lys Gln Ala Gly Ala 370 375 380 Glu Leu Arg Glu Gln Val Leu Gly Gly Arg Val Ile Thr Gly Phe Val 385 390 395 400 Ser Thr Ala Pro Leu Ala Ala Glu Met Arg Ala Phe Leu Asp Ile Thr 405 410 415 Leu Gly Ala His Ile Val Asp Gly Tyr Gly Leu Thr Glu Thr Gly Ala 420 425 430 Val Thr Arg Asp Gly Val Ile Val Arg Pro Pro Val Ile Asp Tyr Lys 435 440 445 Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro Tyr 450 455 460 Pro Arg Gly Glu Leu Leu Val Arg Ser Gln Thr Leu Thr Pro Gly Tyr 465 470 475 480 Tyr Lys Arg Pro Glu Val Thr Ala Ser Val Phe Asp Arg Asp Gly Tyr 485 490 495 Tyr His Thr Gly Asp Val Met Ala Glu Thr Ala Pro Asp His Leu Val 500 505 510 Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly Glu Phe 515 520 525 Val Ala Val Ala Asn Leu Glu Ala Val Phe Ser Gly Ala Ala Leu Val 530 535 540 Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ser Phe Leu Leu Ala 545 550 555 560 Val Val Val Pro Thr Pro Glu Ala Leu Glu Gln Tyr Asp Pro Ala Ala 565 570 575 Leu Lys Ala Ala Leu Ala Asp Ser Leu Gln Arg Thr Ala Arg Asp Ala 580 585 590 Glu Leu Gln Ser Tyr Glu Val Pro Ala Asp Phe Ile Val Glu Thr Glu 595 600 605 Pro Phe Ser Ala Ala Asn Gly Leu Leu Ser Gly Val Gly Lys Leu Leu 610 615 620 Arg Pro Asn Leu Lys Asp Arg Tyr Gly Gln Arg Leu Glu Gln Met Tyr 625 630 635 640 Ala Asp Ile Ala Ala Thr Gln Ala Asn Gln Leu Arg Glu Leu Arg Arg 645 650 655 Ala Ala Ala Thr Gln Pro Val Ile Asp Thr Leu Thr Gln Ala Ala Ala 660 665 670 Thr Ile Leu Gly Thr Gly Ser Glu Val Ala Ser Asp Ala His Phe Thr 675 680 685 Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Leu Ser Asn Leu Leu 690 695 700 Ser Asp Phe Phe Gly Phe Glu Val Pro Val Gly Thr Ile Val Asn Pro 705 710 715 720 Ala Thr Asn Leu Ala Gln Leu Ala Gln His Ile Glu Ala Gln Arg Thr 725 730 735 Ala Gly Asp Arg Arg Pro Ser Phe Thr Thr Val His Gly Ala Asp Ala 740 745 750 Thr Glu Ile Arg Ala Ser Glu Leu Thr Leu Asp Lys Phe Ile Asp Ala 755 760 765 Glu Thr Leu Arg Ala Ala Pro Gly Leu Pro Lys Val Thr Thr Glu Pro 770 775 780 Arg Thr Val Leu Leu Ser Gly Ala Asn Gly Trp Leu Gly Arg Phe Leu 785 790 795 800 Thr Leu Gln Trp Leu Glu Arg Leu Ala Pro Val Gly Gly Thr Leu Ile 805 810 815 Thr Ile Val Arg Gly Arg Asp Asp Ala Ala Ala Arg Ala Arg Leu Thr 820 825 830 Gln Ala Tyr Asp Thr Asp Pro Glu Leu Ser Arg Arg Phe Ala Glu Leu 835 840 845 Ala Asp Arg His Leu Arg Val Val Ala Gly Asp Ile Gly Asp Pro Asn 850 855 860 Leu Gly Leu Thr Pro Glu Ile Trp His Arg Leu Ala Ala Glu Val Asp 865 870 875 880 Leu Val Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Arg 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Lys Leu 900 905 910 Ala Leu Thr Glu Arg Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ser 915 920 925 Val Ala Met Gly Ile Pro Asp Phe Glu Glu Asp Gly Asp Ile Arg Thr 930 935 940 Val Ser Pro Val Arg Pro Leu Asp Gly Gly Tyr Ala Asn Gly Tyr Gly 945 950 955 960 Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu 965 970 975 Cys Gly Leu Pro Val Ala Thr Phe Arg Ser Asp Met Ile Leu Ala His 980 985 990 Pro Arg Tyr Arg Gly Gln Val Asn Val Pro Asp Met Phe Thr Arg Leu 995 1000 1005 Leu Leu Ser Leu Leu Ile Thr Gly Val Ala Pro Arg Ser Phe Tyr 1010 1015 1020 Ile Gly Asp Gly Glu Arg Pro Arg Ala His Tyr Pro Gly Leu Thr 1025 1030 1035 Val Asp Phe Val Ala Glu Ala Val Thr Thr Leu Gly Ala Gln Gln 1040 1045 1050 Arg Glu Gly Tyr Val Ser Tyr Asp Val Met Asn Pro His Asp Asp 1055 1060 1065 Gly Ile Ser Leu Asp Val Phe Val Asp Trp Leu Ile Arg Ala Gly 1070 1075 1080 His Pro Ile Asp Arg Val Asp Asp Tyr Asp Asp Trp Val Arg Arg 1085 1090 1095 Phe Glu Thr Ala Leu Thr Ala Leu Pro Glu Lys Arg Arg Ala Gln 1100 1105 1110 Thr Val Leu Pro Leu Leu His Ala Phe Arg Ala Pro Gln Ala Pro 1115 1120 1125 Leu Arg Gly Ala Pro Glu Pro Thr Glu Val Phe His Ala Ala Val 1130 1135 1140 Arg Thr Ala Lys Val Gly Pro Gly Asp Ile Pro His Leu Asp Glu 1145 1150 1155 Ala Leu Ile Asp Lys Tyr Ile Arg Asp Leu Arg Glu Phe Gly Leu 1160 1165 1170 Ile <210> 152 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium avium <400> 152 Met Ser Thr Ala Thr His Asp Glu Arg Leu Asp Arg Arg Val His Glu 1 5 10 15 Leu Ile Ala Thr Asp Pro Gln Phe Ala Ala Ala Gln Pro Asp Pro Ala 20 25 30 Ile Thr Ala Ala Leu Glu Gln Pro Gly Leu Arg Leu Pro Gln Ile Ile 35 40 45 Arg Thr Val Leu Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Val Val Glu Phe Val Thr Asp Ala Lys Thr Gly Arg Thr Ser Ala Gln 65 70 75 80 Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Ser Glu Val Ala Gln Arg 85 90 95 Val Ser Ala Leu Gly Arg Ala Leu Ser Asp Asp Ala Val His Pro Gly 100 105 110 Asp Arg Val Cys Val Leu Gly Phe Asn Ser Val Asp Tyr Ala Thr Ile 115 120 125 Asp Met Ala Leu Gly Ala Ile Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Ala Ile Ser Ser Leu Gln Pro Ile Val Ala Glu Thr Glu Pro 145 150 155 160 Thr Leu Ile Ala Ser Ser Val Asn Gln Leu Ser Asp Ala Val Gln Leu 165 170 175 Ile Thr Gly Ala Glu Gln Ala Pro Thr Arg Leu Val Val Phe Asp Tyr 180 185 190 His Pro Gln Val Asp Asp Gln Arg Glu Ala Val Gln Asp Ala Ala Ala 195 200 205 Arg Leu Ser Ser Thr Gly Val Ala Val Gln Thr Leu Ala Glu Leu Leu 210 215 220 Glu Arg Gly Lys Asp Leu Pro Ala Val Ala Glu Pro Pro Ala Asp Glu 225 230 235 240 Asp Ser Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro 245 250 255 Lys Gly Ala Met Tyr Pro Gln Ser Asn Val Gly Lys Met Trp Arg Arg 260 265 270 Gly Ser Lys Asn Trp Phe Gly Glu Ser Ala Ala Ser Ile Thr Leu Asn 275 280 285 Phe Met Pro Met Ser His Val Met Gly Arg Ser Ile Leu Tyr Gly Thr 290 295 300 Leu Gly Asn Gly Gly Thr Ala Tyr Phe Ala Ala Arg Ser Asp Leu Ser 305 310 315 320 Thr Leu Leu Glu Asp Leu Glu Leu Val Arg Pro Thr Glu Leu Asn Phe 325 330 335 Val Pro Arg Ile Trp Glu Thr Leu Tyr Gly Glu Phe Gln Arg Gln Val 340 345 350 Glu Arg Arg Leu Ser Glu Ala Gly Asp Ala Gly Glu Arg Arg Ala Val 355 360 365 Glu Ala Glu Val Leu Ala Glu Gln Arg Gln Tyr Leu Leu Gly Gly Arg 370 375 380 Phe Thr Phe Ala Met Thr Gly Ser Ala Pro Ile Ser Pro Glu Leu Arg 385 390 395 400 Asn Trp Val Glu Ser Leu Leu Glu Met His Leu Met Asp Gly Tyr Gly 405 410 415 Ser Thr Glu Ala Gly Met Val Leu Phe Asp Gly Glu Ile Gln Arg Pro 420 425 430 Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe 435 440 445 Ser Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Leu Arg Thr Glu 450 455 460 Asn Met Phe Pro Gly Tyr Tyr Lys Arg Ala Glu Thr Thr Ala Gly Val 465 470 475 480 Phe Asp Glu Asp Gly Tyr Tyr Arg Thr Gly Asp Val Phe Ala Glu Ile 485 490 495 Ala Pro Asp Arg Leu Val Tyr Val Asp Arg Arg Asn Asn Val Leu Lys 500 505 510 Leu Ala Gln Gly Glu Phe Val Thr Leu Ala Lys Leu Glu Ala Val Phe 515 520 525 Gly Asn Ser Pro Leu Ile Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ala 530 535 540 Gln Pro Tyr Leu Leu Ala Val Val Val Pro Thr Glu Glu Ala Leu Ala 545 550 555 560 Ser Gly Asp Pro Glu Thr Leu Lys Pro Lys Ile Ala Asp Ser Leu Gln 565 570 575 Gln Val Ala Lys Glu Ala Gly Leu Gln Ser Tyr Glu Val Pro Arg Asp 580 585 590 Phe Ile Ile Glu Thr Thr Pro Phe Ser Leu Glu Asn Gly Leu Leu Thr 595 600 605 Gly Ile Arg Lys Leu Ala Trp Pro Lys Leu Lys Gln His Tyr Gly Glu 610 615 620 Arg Leu Glu Gln Met Tyr Ala Asp Leu Ala Ala Gly Gln Ala Asn Glu 625 630 635 640 Leu Ala Glu Leu Arg Arg Asn Gly Ala Gln Ala Pro Val Leu Gln Thr 645 650 655 Val Ser Arg Ala Ala Gly Ala Met Leu Gly Ser Ala Ala Ser Asp Leu 660 665 670 Ser Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala 675 680 685 Leu Thr Phe Gly Asn Leu Leu Arg Glu Ile Phe Asp Val Asp Val Pro 690 695 700 Val Gly Val Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Ile Ala Ser 705 710 715 720 Tyr Ile Glu Ala Glu Arg Gln Gly Ser Lys Arg Pro Thr Phe Ala Ser 725 730 735 Val His Gly Arg Asp Ala Thr Val Val Arg Ala Ala Asp Leu Thr Leu 740 745 750 Asp Lys Phe Leu Asp Ala Glu Thr Leu Ala Ala Ala Pro Asn Leu Pro 755 760 765 Lys Pro Ala Thr Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly 770 775 780 Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Met 785 790 795 800 Val Asp Gly Lys Val Ile Ala Leu Asp Ile Leu Ala Ser Asp Glu Glu 805 810 815 Ala Arg Ala Arg Leu Asp Lys Thr Phe Asp Ser Gly Asp Pro Lys Leu 820 825 830 Leu Ala His Tyr Gln Gln Leu Ala Ala Asp His Leu Glu Val Ile Ala 835 840 845 Gly Asp Lys Gly Glu Ala Asn Leu Gly Leu Gly Gln Asp Val Trp Gln 850 855 860 Arg Leu Ala Asp Thr Val Asp Val Ile Val Asp Pro Ala Ala Leu Val 865 870 875 880 Asn His Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala Leu Gly 885 890 895 Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Ser Lys Gln Lys Pro Tyr 900 905 910 Thr Tyr Val Ser Thr Ile Gly Val Gly Asp Gln Ile Glu Pro Gly Lys 915 920 925 Phe Val Glu Asn Ala Asp Ile Arg Gln Met Ser Ala Thr Arg Ala Ile 930 935 940 Asn Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val 965 970 975 Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu 980 985 990 Asn Leu Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr 995 1000 1005 Gly Ile Ala Pro Gly Ser Phe Tyr Glu Leu Asp Ala Asp Gly Asn 1010 1015 1020 Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala 1025 1030 1035 Ala Ala Ile Ser Thr Leu Gly Ser Gln Ile Thr Asp Ser Asp Thr 1040 1045 1050 Gly Phe Gln Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Val 1055 1060 1065 Gly Leu Asp Glu Tyr Val Asp Trp Leu Val Asp Ala Gly Tyr Ser 1070 1075 1080 Ile Glu Arg Ile Ala Asp Tyr Ser Glu Trp Leu Arg Arg Phe Glu 1085 1090 1095 Thr Ser Leu Arg Ala Leu Pro Asp Arg Gln Arg Gln Tyr Ser Leu 1100 1105 1110 Leu Pro Leu Leu His Asn Tyr Arg Thr Pro Glu Lys Pro Ile Asn 1115 1120 1125 Gly Ser Ile Ala Pro Thr Asp Val Phe Arg Ala Ala Val Gln Glu 1130 1135 1140 Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro His Val Ser Pro Pro 1145 1150 1155 Val Ile Val Lys Tyr Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 153 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium avium <400> 153 Met Ser Thr Ala Thr His Asp Glu Arg Leu Asp Arg Arg Val His Glu 1 5 10 15 Leu Ile Ala Thr Asp Pro Gln Phe Ala Ala Ala Gln Pro Asp Pro Ala 20 25 30 Ile Thr Ala Ala Leu Glu Gln Pro Gly Leu Arg Leu Pro Gln Ile Ile 35 40 45 Arg Thr Val Leu Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Val Val Glu Phe Val Thr Asp Ala Lys Thr Gly Arg Thr Ser Ala Gln 65 70 75 80 Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Ser Glu Val Ala Gln Arg 85 90 95 Val Ser Ala Leu Gly Arg Ala Leu Ser Asp Asp Ala Val His Pro Gly 100 105 110 Asp Arg Val Cys Val Leu Gly Phe Asn Ser Val Asp Tyr Ala Thr Ile 115 120 125 Asp Met Ala Leu Gly Ala Ile Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Ala Ile Ser Ser Leu Gln Pro Ile Val Ala Glu Thr Glu Pro 145 150 155 160 Thr Leu Ile Ala Ser Ser Val Asn Gln Leu Ser Asp Ala Val Gln Leu 165 170 175 Ile Thr Gly Ala Glu Gln Ala Pro Thr Arg Leu Val Val Phe Asp Tyr 180 185 190 His Pro Gln Val Asp Asp Gln Arg Glu Ala Val Gln Asp Ala Ala Ala 195 200 205 Arg Leu Ser Ser Thr Gly Val Ala Val Gln Thr Leu Ala Glu Leu Leu 210 215 220 Glu Arg Gly Lys Asp Leu Pro Ala Val Ala Glu Pro Pro Ala Asp Glu 225 230 235 240 Asp Ser Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro 245 250 255 Lys Gly Ala Met Tyr Pro Gln Ser Asn Val Gly Lys Met Trp Arg Arg 260 265 270 Gly Ser Lys Asn Trp Phe Gly Glu Ser Ala Ala Ser Ile Thr Leu Asn 275 280 285 Phe Met Pro Met Ser His Val Met Gly Arg Ser Ile Leu Tyr Gly Thr 290 295 300 Leu Gly Asn Gly Gly Thr Ala Tyr Phe Ala Ala Arg Ser Asp Leu Ser 305 310 315 320 Thr Leu Leu Glu Asp Leu Glu Leu Val Arg Pro Thr Glu Leu Asn Phe 325 330 335 Val Pro Arg Ile Trp Glu Thr Leu Tyr Gly Glu Phe Gln Arg Gln Val 340 345 350 Glu Arg Arg Leu Ser Glu Ala Gly Asp Ala Gly Glu Arg Arg Ala Val 355 360 365 Glu Ala Glu Val Leu Ala Glu Gln Arg Gln Tyr Leu Leu Gly Gly Arg 370 375 380 Phe Thr Phe Ala Met Thr Ser Ser Ala Pro Ile Ser Pro Glu Leu Arg 385 390 395 400 Asn Trp Val Glu Ser Leu Leu Glu Met His Leu Met Asp Gly Tyr Gly 405 410 415 Ser Thr Glu Ala Gly Met Val Leu Phe Asp Gly Glu Ile Gln Arg Pro 420 425 430 Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe 435 440 445 Ser Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Leu Arg Thr Glu 450 455 460 Asn Met Phe Pro Gly Tyr Tyr Lys Arg Ala Glu Thr Thr Ala Gly Val 465 470 475 480 Phe Asp Glu Asp Gly Tyr Tyr Arg Thr Gly Asp Val Phe Ala Glu Ile 485 490 495 Ala Pro Asp Arg Leu Val Tyr Val Asp Arg Arg Asn Asn Val Leu Lys 500 505 510 Leu Ala Gln Gly Glu Phe Val Thr Leu Ala Lys Leu Glu Ala Val Phe 515 520 525 Gly Asn Ser Pro Leu Ile Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ala 530 535 540 Gln Pro Tyr Leu Leu Ala Val Val Val Pro Thr Glu Glu Ala Leu Ala 545 550 555 560 Ser Gly Asp Pro Glu Thr Leu Lys Pro Lys Ile Ala Asp Ser Leu Gln 565 570 575 Gln Val Ala Lys Glu Ala Gly Leu Gln Ser Tyr Glu Val Pro Arg Asp 580 585 590 Phe Ile Ile Glu Thr Thr Pro Phe Ser Leu Glu Asn Gly Leu Leu Thr 595 600 605 Gly Ile Arg Lys Leu Ala Trp Pro Lys Leu Lys Gln His Tyr Gly Glu 610 615 620 Arg Leu Glu Gln Met Tyr Ala Asp Leu Ala Ala Gly Gln Ala Asn Glu 625 630 635 640 Leu Ala Glu Leu Arg Arg Asn Gly Ala Gln Ala Pro Val Leu Gln Thr 645 650 655 Val Ser Arg Ala Ala Gly Ala Met Leu Gly Ser Ala Ala Ser Asp Leu 660 665 670 Ser Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala 675 680 685 Leu Thr Phe Gly Asn Leu Leu Arg Glu Ile Phe Asp Val Asp Val Pro 690 695 700 Val Gly Val Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Ile Ala Ser 705 710 715 720 Tyr Ile Glu Ala Glu Arg Gln Gly Ser Lys Arg Pro Thr Phe Ala Ser 725 730 735 Val His Gly Arg Asp Ala Thr Val Val Arg Ala Ala Asp Leu Thr Leu 740 745 750 Asp Lys Phe Leu Asp Ala Glu Thr Leu Ala Ala Ala Pro Asn Leu Pro 755 760 765 Lys Pro Ala Thr Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly 770 775 780 Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Met 785 790 795 800 Val Asp Gly Lys Val Ile Ala Leu Val Arg Ala Arg Ser Asp Glu Glu 805 810 815 Ala Arg Ala Arg Leu Asp Lys Thr Phe Asp Ser Gly Asp Pro Lys Leu 820 825 830 Leu Ala His Tyr Gln Gln Leu Ala Ala Asp His Leu Glu Val Ile Ala 835 840 845 Gly Asp Lys Gly Glu Ala Asn Leu Gly Leu Gly Gln Asp Val Trp Gln 850 855 860 Arg Leu Ala Asp Thr Val Asp Val Ile Val Asp Pro Ala Ala Leu Val 865 870 875 880 Asn His Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala Leu Gly 885 890 895 Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Ser Lys Gln Lys Pro Tyr 900 905 910 Thr Tyr Val Ser Thr Ile Gly Val Gly Asp Gln Ile Glu Pro Gly Lys 915 920 925 Phe Val Glu Asn Ala Asp Ile Arg Gln Met Ser Ala Thr Arg Ala Ile 930 935 940 Asn Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val 965 970 975 Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu 980 985 990 Asn Leu Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr 995 1000 1005 Gly Ile Ala Pro Gly Ser Phe Tyr Glu Leu Asp Ala Asp Gly Asn 1010 1015 1020 Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala 1025 1030 1035 Ala Ala Ile Ser Thr Leu Gly Ser Gln Ile Thr Asp Ser Asp Thr 1040 1045 1050 Gly Phe Gln Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Val 1055 1060 1065 Gly Leu Asp Glu Tyr Val Asp Trp Leu Val Asp Ala Gly Tyr Ser 1070 1075 1080 Ile Glu Arg Ile Ala Asp Tyr Ser Glu Trp Leu Arg Arg Phe Glu 1085 1090 1095 Thr Ser Leu Arg Ala Leu Pro Asp Arg Gln Arg Gln Tyr Ser Leu 1100 1105 1110 Leu Pro Leu Leu His Asn Tyr Arg Thr Pro Glu Lys Pro Ile Asn 1115 1120 1125 Gly Ser Ile Ala Pro Thr Asp Val Phe Arg Ala Ala Val Gln Glu 1130 1135 1140 Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro His Val Ser Pro Pro 1145 1150 1155 Val Ile Val Lys Tyr Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 154 <211> 1174 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium marinum M <400> 154 Met Ser Pro Ile Thr Arg Glu Glu Arg Leu Glu Arg Arg Ile Gln Asp 1 5 10 15 Leu Tyr Ala Asn Asp Pro Gln Phe Ala Ala Ala Lys Pro Ala Thr Ala 20 25 30 Ile Thr Ala Ala Ile Glu Arg Pro Gly Leu Pro Leu Pro Gln Ile Ile 35 40 45 Glu Thr Val Met Thr Gly Tyr Ala Asp Arg Pro Ala Leu Ala Gln Arg 50 55 60 Ser Val Glu Phe Val Thr Asp Ala Gly Thr Gly His Thr Thr Leu Arg 65 70 75 80 Leu Leu Pro His Phe Glu Thr Ile Ser Tyr Gly Glu Leu Trp Asp Arg 85 90 95 Ile Ser Ala Leu Ala Asp Val Leu Ser Thr Glu Gln Thr Val Lys Pro 100 105 110 Gly Asp Arg Val Cys Leu Leu Gly Phe Asn Ser Val Asp Tyr Ala Thr 115 120 125 Ile Asp Met Thr Leu Ala Arg Leu Gly Ala Val Ala Val Pro Leu Gln 130 135 140 Thr Ser Ala Ala Ile Thr Gln Leu Gln Pro Ile Val Ala Glu Thr Gln 145 150 155 160 Pro Thr Met Ile Ala Ala Ser Val Asp Ala Leu Ala Asp Ala Thr Glu 165 170 175 Leu Ala Leu Ser Gly Gln Thr Ala Thr Arg Val Leu Val Phe Asp His 180 185 190 His Arg Gln Val Asp Ala His Arg Ala Ala Val Glu Ser Ala Arg Glu 195 200 205 Arg Leu Ala Gly Ser Ala Val Val Glu Thr Leu Ala Glu Ala Ile Ala 210 215 220 Arg Gly Asp Val Pro Arg Gly Ala Ser Ala Gly Ser Ala Pro Gly Thr 225 230 235 240 Asp Val Ser Asp Asp Ser Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Ala Pro Lys Gly Ala Met Tyr Pro Arg Arg Asn Val Ala Thr 260 265 270 Phe Trp Arg Lys Arg Thr Trp Phe Glu Gly Gly Tyr Glu Pro Ser Ile 275 280 285 Thr Leu Asn Phe Met Pro Met Ser His Val Met Gly Arg Gln Ile Leu 290 295 300 Tyr Gly Thr Leu Cys Asn Gly Gly Thr Ala Tyr Phe Val Ala Lys Ser 305 310 315 320 Asp Leu Ser Thr Leu Phe Glu Asp Leu Ala Leu Val Arg Pro Thr Glu 325 330 335 Leu Thr Phe Val Pro Arg Val Trp Asp Met Val Phe Asp Glu Phe Gln 340 345 350 Ser Glu Val Asp Arg Arg Leu Val Asp Gly Ala Asp Arg Val Ala Leu 355 360 365 Glu Ala Gln Val Lys Ala Glu Ile Arg Asn Asp Val Leu Gly Gly Arg 370 375 380 Tyr Thr Ser Ala Leu Thr Gly Ser Ala Pro Ile Ser Asp Glu Met Lys 385 390 395 400 Ala Trp Val Glu Glu Leu Leu Asp Met His Leu Val Glu Gly Tyr Gly 405 410 415 Ser Thr Glu Ala Gly Met Ile Leu Ile Asp Gly Ala Ile Arg Arg Pro 420 425 430 Ala Val Leu Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe 435 440 445 Leu Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Val Lys Thr Asp 450 455 460 Ser Leu Phe Pro Gly Tyr Tyr Gln Arg Ala Glu Val Thr Ala Asp Val 465 470 475 480 Phe Asp Ala Asp Gly Phe Tyr Arg Thr Gly Asp Ile Met Ala Glu Val 485 490 495 Gly Pro Glu Gln Phe Val Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys 500 505 510 Leu Ser Gln Gly Glu Phe Val Thr Val Ser Lys Leu Glu Ala Val Phe 515 520 525 Gly Asp Ser Pro Leu Val Arg Gln Ile Tyr Ile Tyr Gly Asn Ser Ala 530 535 540 Arg Ala Tyr Leu Leu Ala Val Ile Val Pro Thr Gln Glu Ala Leu Asp 545 550 555 560 Ala Val Pro Val Glu Glu Leu Lys Ala Arg Leu Gly Asp Ser Leu Gln 565 570 575 Glu Val Ala Lys Ala Ala Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp 580 585 590 Phe Ile Ile Glu Thr Thr Pro Trp Thr Leu Glu Asn Gly Leu Leu Thr 595 600 605 Gly Ile Arg Lys Leu Ala Arg Pro Gln Leu Lys Lys His Tyr Gly Glu 610 615 620 Leu Leu Glu Gln Ile Tyr Thr Asp Leu Ala His Gly Gln Ala Asp Glu 625 630 635 640 Leu Arg Ser Leu Arg Gln Ser Gly Ala Asp Ala Pro Val Leu Val Thr 645 650 655 Val Cys Arg Ala Ala Ala Ala Leu Leu Gly Gly Ser Ala Ser Asp Val 660 665 670 Gln Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala 675 680 685 Leu Ser Phe Thr Asn Leu Leu His Glu Ile Phe Asp Ile Glu Val Pro 690 695 700 Val Gly Val Ile Val Ser Pro Ala Asn Asp Leu Gln Ala Leu Ala Asp 705 710 715 720 Tyr Val Glu Ala Ala Arg Lys Pro Gly Ser Ser Arg Pro Thr Phe Ala 725 730 735 Ser Val His Gly Ala Ser Asn Gly Gln Val Thr Glu Val His Ala Gly 740 745 750 Asp Leu Ser Leu Asp Lys Phe Ile Asp Ala Ala Thr Leu Ala Glu Ala 755 760 765 Pro Arg Leu Pro Ala Ala Asn Thr Gln Val Arg Thr Val Leu Leu Thr 770 775 780 Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu 785 790 795 800 Arg Met Asp Leu Val Asp Gly Lys Leu Ile Cys Leu Val Arg Ala Lys 805 810 815 Ser Asp Thr Glu Ala Arg Ala Arg Leu Asp Lys Thr Phe Asp Ser Gly 820 825 830 Asp Pro Glu Leu Leu Ala His Tyr Arg Ala Leu Ala Gly Asp His Leu 835 840 845 Glu Val Leu Ala Gly Asp Lys Gly Glu Ala Asp Leu Gly Leu Asp Arg 850 855 860 Gln Thr Trp Gln Arg Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro 865 870 875 880 Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro 885 890 895 Asn Ala Leu Gly Thr Ala Glu Leu Leu Arg Leu Ala Leu Thr Ser Lys 900 905 910 Ile Lys Pro Tyr Ser Tyr Thr Ser Thr Ile Gly Val Ala Asp Gln Ile 915 920 925 Pro Pro Ser Ala Phe Thr Glu Asp Ala Asp Ile Arg Val Ile Ser Ala 930 935 940 Thr Arg Ala Val Asp Asp Ser Tyr Ala Asn Gly Tyr Ser Asn Ser Lys 945 950 955 960 Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu 965 970 975 Pro Val Ala Val Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Thr Trp 980 985 990 Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg Met Ile Leu Ser 995 1000 1005 Leu Ala Ala Thr Gly Ile Ala Pro Gly Ser Phe Tyr Glu Leu Ala 1010 1015 1020 Ala Asp Gly Ala Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val 1025 1030 1035 Glu Phe Ile Ala Glu Ala Ile Ser Thr Leu Gly Ala Gln Ser Gln 1040 1045 1050 Asp Gly Phe His Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly 1055 1060 1065 Ile Gly Leu Asp Glu Phe Val Asp Trp Leu Asn Glu Ser Gly Cys 1070 1075 1080 Pro Ile Gln Arg Ile Ala Asp Tyr Gly Asp Trp Leu Gln Arg Phe 1085 1090 1095 Glu Thr Ala Leu Arg Ala Leu Pro Asp Arg Gln Arg His Ser Ser 1100 1105 1110 Leu Leu Pro Leu Leu His Asn Tyr Arg Gln Pro Glu Arg Pro Val 1115 1120 1125 Arg Gly Ser Ile Ala Pro Thr Asp Arg Phe Arg Ala Ala Val Gln 1130 1135 1140 Glu Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro His Val Gly Ala 1145 1150 1155 Pro Ile Ile Val Lys Tyr Val Ser Asp Leu Arg Leu Leu Gly Leu 1160 1165 1170 Leu <210> 155 <211> 1180 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium liflandii 128FXT <400> 155 Met Ser Ile Thr Cys Val Asp Thr Arg Ala Gln Arg Ser Ala Arg Arg 1 5 10 15 Ile Glu Gln Leu Tyr Ser Thr Asp Ala Gln Phe Ala Ala Ala Arg Pro 20 25 30 Ser Thr Ala Val Gly Ile Ala Ile Ser Lys Ser Gly Leu Gly Leu Pro 35 40 45 Gln Ile Ile Gln Thr Val Met Asp Gly Tyr Pro Gln Arg Pro Ala Leu 50 55 60 Gly Gln Arg Ala Thr Arg Val Val Thr Asp Pro Asn Thr Gly Arg Ser 65 70 75 80 Ser Ala Gln Leu Leu Ala Glu Phe Glu Thr Ile Thr Tyr Arg Glu Leu 85 90 95 Trp Asn Arg Thr Asn Ala Leu Thr Asn Ala Phe Ala Ala Glu Ala Leu 100 105 110 Ala Asp Arg Gly Gln Arg Val Cys Val Leu Gly Phe Ala Ser Ile Asp 115 120 125 Tyr Ala Thr Ile Asp Leu Ala Leu Met Leu Leu Gly Ala Val Ser Val 130 135 140 Pro Leu Pro Thr Asn Ala Ala Arg Ala Gln Leu Cys His Ile Val Ser 145 150 155 160 Glu Thr Gln Pro Ser Leu Ile Ala Ser Ser Thr Glu Asn Leu Pro Asp 165 170 175 Ala Ile Ser Leu Val Leu Ser His Arg Ala Pro His Arg Val Val Val 180 185 190 Phe Asp Tyr Arg Pro Glu Leu Asp Ala His Arg Glu Ala Leu Glu Ala 195 200 205 Ala Arg Ala Arg Leu Ala Ala Ile Pro Val Thr Val Glu Thr Leu Thr 210 215 220 Ala Ile Ile Ala Arg Gly Arg Thr Val Arg Pro Ala Glu Ala Asp Cys 225 230 235 240 Gly Ala Gln Ser Ala Asp Ala Pro Ala Leu Leu Ile Tyr Thr Ser Gly 245 250 255 Ser Thr Gly Ala Pro Lys Gly Val Val Tyr Thr Arg Asn Arg Val Ala 260 265 270 Asp Phe Trp Arg Thr Ser Lys Ala Glu Val Glu Ala Thr Glu Gln Arg 275 280 285 Thr Ala Pro Ser Ile Thr Leu Asn Phe Met Pro Met Ser His Ala Asn 290 295 300 Gly Arg Gln Val Leu Tyr Gly Thr Leu Ser Asn Gly Gly Thr Ala Tyr 305 310 315 320 Phe Thr Ala Arg Ser Asp Leu Ser Thr Leu Phe Asp Asp Leu Ala Leu 325 330 335 Val Arg Pro Thr Glu Leu Gly Phe Pro Pro Arg Ile Trp Asp Met Leu 340 345 350 Leu Glu Arg Phe Gly Arg Glu Val Asp Arg Arg Leu Arg Asp Gly Thr 355 360 365 Ala Glu Gly Ala Asp Pro Gly Ala Leu Lys Ala Arg Val Ala Ala Asp 370 375 380 Leu Arg Gln Val Leu Leu Gly Gly Arg Tyr Ala Leu Ala Met Met Gly 385 390 395 400 Ser Ala Pro Ile Ser Glu Gln Met Lys Ala Ser Val Glu Ser Leu Leu 405 410 415 Asp Leu Asp Val Met Glu Gly Tyr Gly Ser Thr Glu Ala Gly Thr Val 420 425 430 Ile Ile Asn Asn Glu Val Gln Arg Pro Gln Val Ile Asp Tyr Lys Leu 435 440 445 Val Asp Val Ala Glu Leu Gly Tyr Phe Leu Thr Asp Arg Pro Tyr Pro 450 455 460 Arg Gly Glu Leu Leu Val Lys Thr Arg Thr Leu Phe Ser Gly Tyr Tyr 465 470 475 480 Arg Asp Pro Glu Asp Gly Ala Gln Val Phe Asp Pro Asp Gly Phe Tyr 485 490 495 Arg Thr Gly Asp Ile Met Ala Gln Val Gly Pro Asp Arg Leu Ala Tyr 500 505 510 Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val 515 520 525 Ala Val Ser Arg Leu Glu Ala Ile Phe Ala Asn Ser Pro Leu Val Arg 530 535 540 Gln Ile Phe Val Tyr Ala Asn Gly Ala Arg Ala Tyr Pro Leu Ala Val 545 550 555 560 Val Val Pro Thr Gln Asp Ala Gln Ser Arg His Gly Arg Ala Glu Leu 565 570 575 Lys Ala Glu Leu His Thr Ser Leu His Arg Val Ala Met Ser Ala Gly 580 585 590 Leu Ala Pro Tyr Glu Ile Pro Arg Asp Phe Ile Val Glu Thr Thr Pro 595 600 605 Phe Thr Pro Gln Asn Gly Leu Leu Thr Ala Ile His Lys Leu Ala Arg 610 615 620 Pro His Leu Thr Gln Arg Tyr Gly Ala Arg Leu Glu Leu Leu Tyr Thr 625 630 635 640 Glu Leu Ala Asp Ser Gln Thr Arg Arg Leu His Arg Leu Arg Gln Thr 645 650 655 Gly Gly Arg Leu Pro Ala Leu Glu Thr Ile Arg Arg Ala Ala Gly Ala 660 665 670 Leu Leu Gly Thr Glu Thr Thr Glu Pro Arg Pro Glu Ala His Phe Lys 675 680 685 Asp Leu Gly Gly Asp Ser Val Ser Ala Val Thr Phe Ser Asn Leu Leu 690 695 700 His Asp Ile Tyr Gly Phe Asp Val Pro Val Gly Val Ile Leu Gly Pro 705 710 715 720 Ala Thr Asp Leu Arg Ala Leu Ala Ser His Val Glu Ser Arg Arg Gly 725 730 735 Ala Gly Trp Ser Gly Pro Ser Phe Ala Ser Val His Val Pro Arg Ala 740 745 750 Thr Ser Val His Ala Gly Asp Leu Lys Leu Ala Lys Phe Leu Asp Thr 755 760 765 Lys Thr Leu Ala Ala Ala Thr Ser Leu Pro Ala Ala Asp Ala Arg Ala 770 775 780 Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu 785 790 795 800 Val Leu Glu Trp Leu Arg Arg Leu Arg Ala Val Gly Gly Lys Leu Ile 805 810 815 Cys Leu Val Arg Ala Ala Ser Asp Glu Gln Ala Arg Val Arg Leu Asp 820 825 830 Thr Ala Phe Asp Ser Gly Asp Pro Gln Leu Pro Glu His Phe Arg Gln 835 840 845 Leu Ala Val Asp Arg Leu Glu Val Leu Ala Gly Asp Lys Ser Glu Pro 850 855 860 Gly Leu Gly Leu Asp Gly Pro Thr Trp Gln Arg Leu Ala Asp Thr Val 865 870 875 880 Asp Leu Ile Val Asp Pro Ala Thr Leu Val Asn His Val Leu Ser Tyr 885 890 895 Arg Gln Leu Phe Ala Pro Asn Val Ala Gly Thr Ala Glu Leu Leu Arg 900 905 910 Leu Ala Leu Thr Thr Lys Arg Lys Pro Tyr Ala Tyr Val Ser Thr Val 915 920 925 Ser Val Ala Asn Gln Ile Glu Pro Ser Ala Phe Thr Glu Asp Ala Asp 930 935 940 Ile Arg Glu Ile Ser Arg Thr Arg Thr Ile Asp Asp Ser Phe Ala Asn 945 950 955 960 Gly Tyr Thr Thr Ser Lys Trp Ala Ser Glu Val Leu Leu Arg Glu Ala 965 970 975 His Asp Leu Cys Gly Leu Pro Val Thr Val Phe Arg Cys Asp Met Ile 980 985 990 Leu Ala Asp Thr Ser Tyr Ala Gly Gln Leu Asn Leu Ala Asp Thr Phe 995 1000 1005 Thr Arg Leu Met Leu Ser Val Ala Ala Thr Gly Ile Ala Pro Ala 1010 1015 1020 Ser Phe Tyr Arg Leu Gly Pro Asp Gly Lys Arg Gln Pro Ala His 1025 1030 1035 Phe Asp Gly Leu Pro Val Glu Phe Ile Ala Glu Ala Val Ala Thr 1040 1045 1050 Leu Gly Ala Arg Arg His Asp Gly Phe Gln Val His His Val Ala 1055 1060 1065 Asn Pro His His Asp Gly Val Gly Leu Asp Glu Tyr Val Asp Trp 1070 1075 1080 Leu Val Asp Ala Gly Cys Pro Ile Arg Arg Ile Pro Asp Tyr Asp 1085 1090 1095 Glu Trp Leu Ser Arg Phe Glu Thr Ala Leu His Ala Leu Pro Asp 1100 1105 1110 Arg Lys Arg Arg His Ser Leu Leu Pro Leu Leu Gln Asn Tyr Arg 1115 1120 1125 Glu Pro Ala Glu Pro Ile Arg Gly Gly Ile Ala Pro Ala Pro Arg 1130 1135 1140 Phe Arg Gly Ala Val Arg Gln Ala Lys Ile Gly Arg Asp Asn Asp 1145 1150 1155 Ile Pro His Val Gly Pro Ala Ile Ile Ala Lys Tyr Ala Ser Asp 1160 1165 1170 Leu Gln Leu Leu Gly Leu Ala 1175 1180 <210> 156 <211> 1168 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium tuberculosis variant bovis BCG <400> 156 Met Ser Ile Asn Asp Gln Arg Leu Thr Arg Arg Val Glu Asp Leu Tyr 1 5 10 15 Ala Ser Asp Ala Gln Phe Ala Ala Ala Ser Pro Asn Glu Ala Ile Thr 20 25 30 Gln Ala Ile Asp Gln Pro Gly Val Ala Leu Pro Gln Leu Ile Arg Met 35 40 45 Val Met Glu Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg Ala Leu 50 55 60 Arg Phe Val Thr Asp Pro Asp Ser Gly Arg Thr Met Val Glu Leu Leu 65 70 75 80 Pro Arg Phe Glu Thr Ile Thr Tyr Arg Glu Leu Trp Ala Arg Ala Gly 85 90 95 Thr Leu Ala Thr Ala Leu Ser Ala Glu Pro Ala Ile Arg Pro Gly Asp 100 105 110 Arg Val Cys Val Leu Gly Phe Asn Ser Val Asp Tyr Thr Thr Ile Asp 115 120 125 Ile Ala Leu Ile Arg Leu Gly Ala Val Ser Val Pro Leu Gln Thr Ser 130 135 140 Ala Pro Val Thr Gly Leu Arg Pro Ile Val Thr Glu Thr Glu Pro Thr 145 150 155 160 Met Ile Ala Thr Ser Ile Asp Asn Leu Gly Asp Ala Val Glu Val Leu 165 170 175 Ala Gly His Ala Pro Ala Arg Leu Val Val Phe Asp Tyr His Gly Lys 180 185 190 Val Asp Thr His Arg Glu Ala Val Glu Ala Ala Arg Ala Arg Leu Ala 195 200 205 Gly Ser Val Thr Ile Asp Thr Leu Ala Glu Leu Ile Glu Arg Gly Arg 210 215 220 Ala Leu Pro Ala Thr Pro Ile Ala Asp Ser Ala Asp Asp Ala Leu Ala 225 230 235 240 Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met 245 250 255 Tyr Arg Glu Ser Gln Val Met Ser Phe Trp Arg Lys Ser Ser Gly Trp 260 265 270 Phe Glu Pro Ser Gly Tyr Pro Ser Ile Thr Leu Asn Phe Met Pro Met 275 280 285 Ser His Val Gly Gly Arg Gln Val Leu Tyr Gly Thr Leu Ser Asn Gly 290 295 300 Gly Thr Ala Tyr Tyr Val Ala Lys Ser Asp Leu Ser Thr Leu Phe Glu 305 310 315 320 Asp Leu Ala Leu Val Arg Pro Thr Glu Leu Cys Phe Val Pro Arg Ile 325 330 335 Trp Asp Met Val Phe Ala Glu Phe His Ser Glu Val Asp Arg Arg Leu 340 345 350 Val Asp Gly Ala Asp Arg Ala Ala Leu Glu Ala Gln Val Lys Ala Glu 355 360 365 Leu Arg Glu Asn Val Leu Gly Gly Arg Phe Val Met Ala Leu Thr Gly 370 375 380 Ser Ala Pro Ile Ser Ala Glu Met Thr Ala Trp Val Glu Ser Leu Leu 385 390 395 400 Ala Asp Val His Leu Val Glu Gly Tyr Gly Ser Thr Glu Ala Gly Met 405 410 415 Val Leu Asn Asp Gly Met Val Arg Arg Pro Ala Val Ile Asp Tyr Lys 420 425 430 Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Gly Thr Asp Gln Pro Tyr 435 440 445 Pro Arg Gly Glu Leu Leu Val Lys Thr Gln Thr Met Phe Pro Gly Tyr 450 455 460 Tyr Gln Arg Pro Asp Val Thr Ala Glu Val Phe Asp Pro Asp Gly Phe 465 470 475 480 Tyr Arg Thr Gly Asp Ile Met Ala Lys Val Gly Pro Asp Gln Phe Val 485 490 495 Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe 500 505 510 Ile Ala Val Ser Lys Leu Glu Ala Val Phe Gly Asp Ser Pro Leu Val 515 520 525 Arg Gln Ile Phe Ile Tyr Gly Asn Ser Ala Arg Ala Tyr Pro Leu Ala 530 535 540 Val Val Val Pro Ser Gly Asp Ala Leu Ser Arg His Gly Ile Glu Asn 545 550 555 560 Leu Lys Pro Val Ile Ser Glu Ser Leu Gln Glu Val Ala Arg Ala Ala 565 570 575 Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile Ile Glu Thr Thr 580 585 590 Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala 595 600 605 Arg Pro Gln Leu Lys Lys Phe Tyr Gly Glu Arg Leu Glu Arg Leu Tyr 610 615 620 Thr Glu Leu Ala Asp Ser Gln Ser Asn Glu Leu Arg Glu Leu Arg Gln 625 630 635 640 Ser Gly Pro Asp Ala Pro Val Leu Pro Thr Leu Cys Arg Ala Ala Ala 645 650 655 Ala Leu Leu Gly Ser Thr Ala Ala Asp Val Arg Pro Asp Ala His Phe 660 665 670 Ala Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Leu Ala Asn Leu 675 680 685 Leu His Glu Ile Phe Gly Val Asp Val Pro Val Gly Val Ile Val Ser 690 695 700 Pro Ala Ser Asp Leu Arg Ala Leu Ala Asp His Ile Glu Ala Ala Arg 705 710 715 720 Thr Gly Val Arg Arg Pro Ser Phe Ala Ser Ile His Gly Arg Ser Ala 725 730 735 Thr Glu Val His Ala Ser Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala 740 745 750 Ala Thr Leu Ala Ala Ala Pro Asn Leu Pro Ala Pro Ser Ala Gln Val 755 760 765 Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu 770 775 780 Ala Leu Glu Trp Leu Asp Arg Met Asp Leu Val Asn Gly Lys Leu Ile 785 790 795 800 Cys Leu Val Arg Ala Arg Ser Asp Glu Glu Ala Gln Ala Arg Leu Asp 805 810 815 Ala Thr Phe Asp Ser Gly Asp Pro Tyr Leu Val Arg His Tyr Arg Glu 820 825 830 Leu Gly Ala Gly Arg Leu Glu Val Leu Ala Gly Asp Lys Gly Glu Ala 835 840 845 Asp Leu Gly Leu Asp Arg Val Thr Trp Gln Arg Leu Ala Asp Thr Val 850 855 860 Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Ser Gln Leu Phe Gly Pro Asn Ala Ala Gly Thr Ala Glu Leu Leu Arg 885 890 895 Leu Ala Leu Thr Gly Lys Arg Lys Pro Tyr Ile Tyr Thr Ser Thr Ile 900 905 910 Ala Val Gly Glu Gln Ile Pro Pro Glu Ala Phe Thr Glu Asp Ala Asp 915 920 925 Ile Arg Ala Ile Ser Pro Thr Arg Arg Ile Asp Asp Ser Tyr Ala Asn 930 935 940 Gly Tyr Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala 945 950 955 960 His Glu Gln Cys Gly Leu Pro Val Thr Val Phe Arg Cys Asp Met Ile 965 970 975 Leu Ala Asp Thr Ser Tyr Thr Gly Gln Leu Asn Leu Pro Asp Met Phe 980 985 990 Thr Arg Leu Met Leu Ser Leu Ala Ala Thr Gly Ile Ala Pro Gly Ser 995 1000 1005 Phe Tyr Glu Leu Asp Ala His Gly Asn Arg Gln Arg Ala His Tyr 1010 1015 1020 Asp Gly Leu Pro Val Glu Phe Val Ala Glu Ala Ile Cys Thr Leu 1025 1030 1035 Gly Thr His Ser Pro Asp Arg Phe Val Thr Tyr His Val Met Asn 1040 1045 1050 Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu Phe Val Asp Trp Leu 1055 1060 1065 Asn Ser Pro Thr Ser Gly Ser Gly Cys Thr Ile Gln Arg Ile Ala 1070 1075 1080 Asp Tyr Gly Glu Trp Leu Gln Arg Phe Glu Thr Ser Leu Arg Ala 1085 1090 1095 Leu Pro Asp Arg Gln Arg His Ala Ser Leu Leu Pro Leu Leu His 1100 1105 1110 Asn Tyr Arg Glu Pro Ala Lys Pro Ile Cys Gly Ser Ile Ala Pro 1115 1120 1125 Thr Asp Gln Phe Arg Ala Ala Val Gln Glu Ala Lys Ile Gly Pro 1130 1135 1140 Asp Lys Asp Ile Pro His Leu Thr Ala Ala Ile Ile Ala Lys Tyr 1145 1150 1155 Ile Ser Asn Leu Arg Leu Leu Gly Leu Leu 1160 1165 <210> 157 <211> 1148 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces griseus subsp. griseus NBRC 13350 <400> 157 Met Ala Glu Pro Leu Asp Ala Ala Thr Ala Ser Ala His Asp Pro Gly 1 5 10 15 Gln Gly Leu Ala Glu Ala Leu Ala Ala Val Glu Pro Gly Arg Ala Leu 20 25 30 Ala Glu Val Met Ala Ser Val Leu Glu Gly His Gly Asp Arg Pro Ala 35 40 45 Leu Gly Glu Arg Ala Arg Glu Pro Glu Thr Gly Arg Leu Leu Pro His 50 55 60 Phe Asp Thr Ile Ser Tyr Arg Glu Leu Trp Ser Arg Val Arg Ala Leu 65 70 75 80 Ala Gly Arg Trp His His Asp Pro Glu Tyr Pro Leu Gly Pro Gly Asp 85 90 95 Arg Ile Cys Thr Leu Gly Phe Thr Ser Thr Asp Tyr Ala Thr Leu Asp 100 105 110 Leu Ala Cys Ile His Leu Gly Ala Val Pro Val Pro Leu Pro Ser Asn 115 120 125 Ala Pro Leu Pro Arg Leu Ala Pro Val Val Glu Glu Ser Gly Pro Thr 130 135 140 Val Leu Ala Ala Ser Val Asp Arg Leu Asp Thr Ala Ile Asp Val Val 145 150 155 160 Leu Ala Ser Ser Thr Ile Arg Arg Leu Leu Val Phe Asp Asp Gly Pro 165 170 175 Gly Ala Thr Arg Pro Gly Gly Ala Leu Ala Ala Ala Arg Gln Arg Leu 180 185 190 Ser Gly Ser Pro Val Thr Val Asp Thr Leu Ala Gly Leu Ile Asp Arg 195 200 205 Gly Arg Asp Leu Pro Pro Pro Pro Leu Tyr Ile Pro Asp Pro Gly Glu 210 215 220 Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro 225 230 235 240 Lys Gly Ala Met Tyr Thr Gln Arg Leu Leu Gly Thr Ala Trp Tyr Gly 245 250 255 Phe Ser Tyr Gly Ala Ala Asp Thr Pro Ala Ile Ser Val Leu Tyr Leu 260 265 270 Pro Gln Ser His Leu Ala Gly Arg Tyr Ala Val Met Gly Ser Leu Val 275 280 285 Lys Gly Gly Thr Gly Tyr Phe Thr Ala Ala Asp Asp Leu Ser Thr Leu 290 295 300 Phe Glu Asp Ile Ala Leu Val Arg Pro Thr Glu Leu Thr Met Val Pro 305 310 315 320 Arg Leu Cys Asp Met Leu Leu Gln His Tyr Arg Ser Glu Arg Asp Arg 325 330 335 Arg Ala Asp Glu Pro Gly Asp Ile Glu Ala Ala Val Thr Lys Ala Val 340 345 350 Arg Glu Asp Phe Leu Gly Gly Arg Val Ala Lys Ala Phe Val Gly Thr 355 360 365 Ala Pro Leu Ser Ala Glu Leu Thr Ala Phe Val Glu Ser Val Leu Gly 370 375 380 Phe His Leu Tyr Thr Gly Tyr Gly Ser Thr Glu Ala Gly Gly Val Leu 385 390 395 400 Leu Asp Thr Val Val Gln Arg Pro Pro Val Thr Asp Tyr Lys Leu Val 405 410 415 Asp Val Pro Glu Leu Gly Tyr Tyr Ala Thr Asp Leu Pro His Pro Arg 420 425 430 Gly Glu Leu Leu Leu Lys Ser His Thr Leu Ile Pro Gly Tyr Tyr Arg 435 440 445 Arg Pro Asp Leu Thr Ala Ala Ile Phe Asp Ala Asp Gly Tyr Tyr Arg 450 455 460 Thr Gly Asp Val Phe Ala Glu Thr Gly Pro Asp Arg Leu Val Tyr Val 465 470 475 480 Asp Arg Thr Lys Asp Thr Leu Lys Leu Ser Gln Gly Glu Phe Val Ala 485 490 495 Val Ser Arg Leu Glu Thr Val Leu Leu Asp Ser Pro Leu Val Gln His 500 505 510 Leu Tyr Leu Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala Val Val 515 520 525 Val Pro Thr Pro Asp Ala Leu Ala Gly Cys Gly Gly Asp Thr Glu Ala 530 535 540 Leu Arg Pro Leu Leu Met Glu Ser Leu Arg Ser Val Ala Arg Arg Ala 545 550 555 560 Gly Leu Asn Ala Tyr Glu Ile Pro Arg Gly Ile Leu Val Glu Pro Glu 565 570 575 Pro Phe Ser Pro Glu Asn Gly Leu Phe Thr Glu Ser His Lys Leu Leu 580 585 590 Arg Pro Arg Leu Lys Glu Arg Tyr Gly Pro Ala Leu Glu Leu Leu Tyr 595 600 605 Asp Arg Leu Ala Asp Gly Gln Asp Arg Arg Leu Arg Glu Leu Arg Arg 610 615 620 Thr Gly Ala Asp Arg Pro Val Gln Glu Thr Val Leu Arg Ala Ala Gln 625 630 635 640 Ala Leu Leu Gly Ser Pro Gly Ser Asp Leu Arg Pro Gly Ala His Phe 645 650 655 Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Val Ser Phe Ser Glu Leu 660 665 670 Met Lys Glu Ile Phe His Val Asp Val Pro Val Gly Ala Ile Ile Gly 675 680 685 Pro Ala Ala Asp Leu Ala Glu Val Ala Arg Tyr Ile Thr Ala Ala Arg 690 695 700 Arg Pro Ala Gly Ala Pro Arg Pro Thr Pro Ala Ser Val His Gly Glu 705 710 715 720 His Arg Thr Glu Val Arg Ala Gly Asp Leu Ala Pro Glu Lys Phe Leu 725 730 735 Asp Ala Pro Thr Leu Ala Ala Ala Pro Ala Leu Pro Arg Pro Asp Gly 740 745 750 Asp Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Tyr Leu Gly Arg 755 760 765 Phe Leu Cys Leu Glu Trp Leu Glu Arg Leu Ala Pro Ser Gly Gly Arg 770 775 780 Leu Val Cys Leu Val Arg Gly Ser Asp Ala Thr Val Ala Ala Arg Arg 785 790 795 800 Leu Glu Ala Ala Phe Asp Ser Gly Asp Thr Ala Leu Leu Arg Arg Tyr 805 810 815 Arg Lys Ala Ala Gly Lys Thr Leu Asp Val Val Ala Gly Asp Ile Gly 820 825 830 Glu Pro Leu Leu Gly Leu Ala Glu Glu Thr Trp Arg Glu Leu Ala Gly 835 840 845 Ala Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His Leu Leu 850 855 860 Pro Tyr Gly Glu Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ala 865 870 875 880 Ile Arg Leu Ala Leu Thr Thr Arg Leu Lys Pro Val Asn His Val Ser 885 890 895 Thr Val Ala Val Cys Leu Gly Thr Pro Ala Glu Thr Ala Asp Glu Asn 900 905 910 Ala Asp Ile Arg Ala Ala Val Pro Val Arg Thr Thr Gly Gln Gly Tyr 915 920 925 Ala Asp Gly Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 930 935 940 Glu Ala His Glu Arg Tyr Gly Leu Pro Val Ala Val Phe Arg Ser Asp 945 950 955 960 Met Val Leu Ala His Arg Thr Tyr Thr Gly Gln Val Asn Val Pro Asp 965 970 975 Val Leu Thr Arg Leu Leu Leu Ser Leu Val Ala Thr Gly Ile Ala Pro 980 985 990 Gly Ser Phe Tyr Arg Thr Asp Thr Arg Ala His Tyr Asp Gly Leu Pro 995 1000 1005 Val Asp Phe Thr Ala Glu Ala Val Val Ala Leu Gly Ala Pro Ile 1010 1015 1020 Thr Glu Gly His Arg Thr Phe Asn Val Leu Asn Pro His Asp Asp 1025 1030 1035 Gly Val Ser Leu Asp Thr Phe Val Asp Trp Leu Ile Glu Ala Gly 1040 1045 1050 His Pro Ile Arg Arg Ile Asp Asp His Gly Ala Trp Leu Thr Arg 1055 1060 1065 Phe Thr Ala Ala Leu Arg Ala Leu Pro Glu Lys Gln Arg Gln His 1070 1075 1080 Ser Leu Leu Pro Leu Ile Gly Ala Trp Ala Glu Pro Gly Glu Gly 1085 1090 1095 Ala Pro Gly Pro Leu Leu Pro Ala Arg Arg Phe His Ala Ala Val 1100 1105 1110 Arg Ala Ala Gly Val Gly Pro Glu Arg Asp Ile Pro Arg Val Ser 1115 1120 1125 Pro Asp Leu Ile Arg Lys Tyr Val Thr Asp Leu Arg Ala Leu Gly 1130 1135 1140 Leu Leu Ala Gly Pro 1145 <210> 158 <211> 1392 <212> PRT <213> Artificial Sequence <220> <223> Saccharomyces cerevisiae S288C <400> 158 Met Thr Asn Glu Lys Val Trp Ile Glu Lys Leu Asp Asn Pro Thr Leu 1 5 10 15 Ser Val Leu Pro His Asp Phe Leu Arg Pro Gln Gln Glu Pro Tyr Thr 20 25 30 Lys Gln Ala Thr Tyr Ser Leu Gln Leu Pro Gln Leu Asp Val Pro His 35 40 45 Asp Ser Phe Ser Asn Lys Tyr Ala Val Ala Leu Ser Val Trp Ala Ala 50 55 60 Leu Ile Tyr Arg Val Thr Gly Asp Asp Asp Ile Val Leu Tyr Ile Ala 65 70 75 80 Asn Asn Lys Ile Leu Arg Phe Asn Ile Gln Pro Thr Trp Ser Phe Asn 85 90 95 Glu Leu Tyr Ser Thr Ile Asn Asn Glu Leu Asn Lys Leu Asn Ser Ile 100 105 110 Glu Ala Asn Phe Ser Phe Asp Glu Leu Ala Glu Lys Ile Gln Ser Cys 115 120 125 Gln Asp Leu Glu Arg Thr Pro Gln Leu Phe Arg Leu Ala Phe Leu Glu 130 135 140 Asn Gln Asp Phe Lys Leu Asp Glu Phe Lys His His Leu Val Asp Phe 145 150 155 160 Ala Leu Asn Leu Asp Thr Ser Asn Asn Ala His Val Leu Asn Leu Ile 165 170 175 Tyr Asn Ser Leu Leu Tyr Ser Asn Glu Arg Val Thr Ile Val Ala Asp 180 185 190 Gln Phe Thr Gln Tyr Leu Thr Ala Ala Leu Ser Asp Pro Ser Asn Cys 195 200 205 Ile Thr Lys Ile Ser Leu Ile Thr Ala Ser Ser Lys Asp Ser Leu Pro 210 215 220 Asp Pro Thr Lys Asn Leu Gly Trp Cys Asp Phe Val Gly Cys Ile His 225 230 235 240 Asp Ile Phe Gln Asp Asn Ala Glu Ala Phe Pro Glu Arg Thr Cys Val 245 250 255 Val Glu Thr Pro Thr Leu Asn Ser Asp Lys Ser Arg Ser Phe Thr Tyr 260 265 270 Arg Asp Ile Asn Arg Thr Ser Asn Ile Val Ala His Tyr Leu Ile Lys 275 280 285 Thr Gly Ile Lys Arg Gly Asp Val Val Met Ile Tyr Ser Ser Arg Gly 290 295 300 Val Asp Leu Met Val Cys Val Met Gly Val Leu Lys Ala Gly Ala Thr 305 310 315 320 Phe Ser Val Ile Asp Pro Ala Tyr Pro Pro Ala Arg Gln Thr Ile Tyr 325 330 335 Leu Gly Val Ala Lys Pro Arg Gly Leu Ile Val Ile Arg Ala Ala Gly 340 345 350 Gln Leu Asp Gln Leu Val Glu Asp Tyr Ile Asn Asp Glu Leu Glu Ile 355 360 365 Val Ser Arg Ile Asn Ser Ile Ala Ile Gln Glu Asn Gly Thr Ile Glu 370 375 380 Gly Gly Lys Leu Asp Asn Gly Glu Asp Val Leu Ala Pro Tyr Asp His 385 390 395 400 Tyr Lys Asp Thr Arg Thr Gly Val Val Val Gly Pro Asp Ser Asn Pro 405 410 415 Thr Leu Ser Phe Thr Ser Gly Ser Glu Gly Ile Pro Lys Gly Val Leu 420 425 430 Gly Arg His Phe Ser Leu Ala Tyr Tyr Phe Asn Trp Met Ser Lys Arg 435 440 445 Phe Asn Leu Thr Glu Asn Asp Lys Phe Thr Met Leu Ser Gly Ile Ala 450 455 460 His Asp Pro Ile Gln Arg Asp Met Phe Thr Pro Leu Phe Leu Gly Ala 465 470 475 480 Gln Leu Tyr Val Pro Thr Gln Asp Asp Ile Gly Thr Pro Gly Arg Leu 485 490 495 Ala Glu Trp Met Ser Lys Tyr Gly Cys Thr Val Thr His Leu Thr Pro 500 505 510 Ala Met Gly Gln Leu Leu Thr Ala Gln Ala Thr Thr Pro Phe Pro Lys 515 520 525 Leu His His Ala Phe Phe Val Gly Asp Ile Leu Thr Lys Arg Asp Cys 530 535 540 Leu Arg Leu Gln Thr Leu Ala Glu Asn Cys Arg Ile Val Asn Met Tyr 545 550 555 560 Gly Thr Thr Glu Thr Gln Arg Ala Val Ser Tyr Phe Glu Val Lys Ser 565 570 575 Lys Asn Asp Asp Pro Asn Phe Leu Lys Lys Leu Lys Asp Val Met Pro 580 585 590 Ala Gly Lys Gly Met Leu Asn Val Gln Leu Leu Val Val Asn Arg Asn 595 600 605 Asp Arg Thr Gln Ile Cys Gly Ile Gly Glu Ile Gly Glu Ile Tyr Val 610 615 620 Arg Ala Gly Gly Leu Ala Glu Gly Tyr Arg Gly Leu Pro Glu Leu Asn 625 630 635 640 Lys Glu Lys Phe Val Asn Asn Trp Phe Val Glu Lys Asp His Trp Asn 645 650 655 Tyr Leu Asp Lys Asp Asn Gly Glu Pro Trp Arg Gln Phe Trp Leu Gly 660 665 670 Pro Arg Asp Arg Leu Tyr Arg Thr Gly Asp Leu Gly Arg Tyr Leu Pro 675 680 685 Asn Gly Asp Cys Glu Cys Cys Gly Arg Ala Asp Asp Gln Val Lys Ile 690 695 700 Arg Gly Phe Arg Ile Glu Leu Gly Glu Ile Asp Thr His Ile Ser Gln 705 710 715 720 His Pro Leu Val Arg Glu Asn Ile Thr Leu Val Arg Lys Asn Ala Asp 725 730 735 Asn Glu Pro Thr Leu Ile Thr Phe Met Val Pro Arg Phe Asp Lys Pro 740 745 750 Asp Asp Leu Ser Lys Phe Gln Ser Asp Val Pro Lys Glu Val Glu Thr 755 760 765 Asp Pro Ile Val Lys Gly Leu Ile Gly Tyr His Leu Leu Ser Lys Asp 770 775 780 Ile Arg Thr Phe Leu Lys Lys Arg Leu Ala Ser Tyr Ala Met Pro Ser 785 790 795 800 Leu Ile Val Val Met Asp Lys Leu Pro Leu Asn Pro Asn Gly Lys Val 805 810 815 Asp Lys Pro Lys Leu Gln Phe Pro Thr Pro Lys Gln Leu Asn Leu Val 820 825 830 Ala Glu Asn Thr Val Ser Glu Thr Asp Asp Ser Gln Phe Thr Asn Val 835 840 845 Glu Arg Glu Val Arg Asp Leu Trp Leu Ser Ile Leu Pro Thr Lys Pro 850 855 860 Ala Ser Val Ser Pro Asp Asp Ser Phe Phe Asp Leu Gly Gly His Ser 865 870 875 880 Ile Leu Ala Thr Lys Met Ile Phe Thr Leu Lys Lys Lys Leu Gln Val 885 890 895 Asp Leu Pro Leu Gly Thr Ile Phe Lys Tyr Pro Thr Ile Lys Ala Phe 900 905 910 Ala Ala Glu Ile Asp Arg Ile Lys Ser Ser Gly Gly Ser Ser Gln Gly 915 920 925 Glu Val Val Glu Asn Val Thr Ala Asn Tyr Ala Glu Asp Ala Lys Lys 930 935 940 Leu Val Glu Thr Leu Pro Ser Ser Tyr Pro Ser Arg Glu Tyr Phe Val 945 950 955 960 Glu Pro Asn Ser Ala Glu Gly Lys Thr Thr Ile Asn Val Phe Val Thr 965 970 975 Gly Val Thr Gly Phe Leu Gly Ser Tyr Ile Leu Ala Asp Leu Leu Gly 980 985 990 Arg Ser Pro Lys Asn Tyr Ser Phe Lys Val Phe Ala His Val Arg Ala 995 1000 1005 Lys Asp Glu Glu Ala Ala Phe Ala Arg Leu Gln Lys Ala Gly Ile 1010 1015 1020 Thr Tyr Gly Thr Trp Asn Glu Lys Phe Ala Ser Asn Ile Lys Val 1025 1030 1035 Val Leu Gly Asp Leu Ser Lys Ser Gln Phe Gly Leu Ser Asp Glu 1040 1045 1050 Lys Trp Met Asp Leu Ala Asn Thr Val Asp Ile Ile Ile His Asn 1055 1060 1065 Gly Ala Leu Val His Trp Val Tyr Pro Tyr Ala Lys Leu Arg Asp 1070 1075 1080 Pro Asn Val Ile Ser Thr Ile Asn Val Met Ser Leu Ala Ala Val 1085 1090 1095 Gly Lys Pro Lys Phe Phe Asp Phe Val Ser Ser Thr Ser Thr Leu 1100 1105 1110 Asp Thr Glu Tyr Tyr Phe Asn Leu Ser Asp Lys Leu Val Ser Glu 1115 1120 1125 Gly Lys Pro Gly Ile Leu Glu Ser Asp Asp Leu Met Asn Ser Ala 1130 1135 1140 Ser Gly Leu Thr Gly Gly Tyr Gly Gln Ser Lys Trp Ala Ala Glu 1145 1150 1155 Tyr Ile Ile Arg Arg Ala Gly Glu Arg Gly Leu Arg Gly Cys Ile 1160 1165 1170 Val Arg Pro Gly Tyr Val Thr Gly Ala Ser Ala Asn Gly Ser Ser 1175 1180 1185 Asn Thr Asp Asp Phe Leu Leu Arg Phe Leu Lys Gly Ser Val Gln 1190 1195 1200 Leu Gly Lys Ile Pro Asp Ile Glu Asn Ser Val Asn Met Val Pro 1205 1210 1215 Val Asp His Val Ala Arg Val Val Val Ala Thr Ser Leu Asn Pro 1220 1225 1230 Pro Lys Glu Asn Glu Leu Ala Val Ala Gln Val Thr Gly His Pro 1235 1240 1245 Arg Ile Leu Phe Lys Asp Tyr Leu Tyr Thr Leu His Asp Tyr Gly 1250 1255 1260 Tyr Asp Val Glu Ile Glu Ser Tyr Ser Lys Trp Lys Lys Ser Leu 1265 1270 1275 Glu Ala Ser Val Ile Asp Arg Asn Glu Glu Asn Ala Leu Tyr Pro 1280 1285 1290 Leu Leu His Met Val Leu Asp Asn Leu Pro Glu Ser Thr Lys Ala 1295 1300 1305 Pro Glu Leu Asp Asp Arg Asn Ala Val Ala Ser Leu Lys Lys Asp 1310 1315 1320 Thr Ala Trp Thr Gly Val Asp Trp Ser Asn Gly Ile Gly Val Thr 1325 1330 1335 Pro Glu Glu Val Gly Ile Tyr Ile Ala Phe Leu Asn Lys Val Gly 1340 1345 1350 Phe Leu Pro Pro Pro Thr His Asn Asp Lys Leu Pro Leu Pro Ser 1355 1360 1365 Ile Glu Leu Thr Gln Ala Gln Ile Ser Leu Val Ala Ser Gly Ala 1370 1375 1380 Gly Ala Arg Gly Ser Ser Ala Ala Ala 1385 1390 <210> 159 <211> 1144 <212> PRT <213> Artificial Sequence <220> <223> Cyanobium sp. PCC 7001 <400> 159 Met Asn Glu Ser Ser Ala Asp Gln Ser Ser Gly Asn Val Ser Glu Gly 1 5 10 15 Trp Pro Asp Ala Ser Val Thr Ala Arg Ala Leu Gln Ala His Leu Arg 20 25 30 Tyr Glu Gln Ile Ile Asp Ala Ile Leu Ser Gly Tyr Ala Glu Arg Pro 35 40 45 Ala Leu Ala Glu Arg Ser Tyr Leu Val Arg Pro Asp Pro Ser Thr Gly 50 55 60 Gln Thr Val Arg Val His Glu Gln Ala Phe Arg Ser Ile Ser Tyr Arg 65 70 75 80 Thr Leu Gln Glu Arg Val His Ala Leu Thr Met Ala Trp Arg Leu His 85 90 95 Pro Asp Ser Pro Val Gln Ala Gly Ala Phe Val Val Leu Val Gly Phe 100 105 110 Ala Ser Ile Asp Tyr Ala Val Leu Asp Leu Ala Leu Ala Tyr Thr Lys 115 120 125 Gly Val Pro Val Pro Leu Ser Pro Asn His Ser Ser Glu Asp Asp Asp 130 135 140 Ala Ile Leu Gly Thr Val Gln Pro Val Thr Leu Ala Val Ser Ile Ser 145 150 155 160 Glu Phe Ser Gly Cys Val Asp Leu Ile Ala Arg Ser Thr Ser Ile Arg 165 170 175 Thr Val Ile Val Phe Asp Leu Asp Pro Ala Val Asp Cys Glu Arg Ala 180 185 190 Ala Leu Glu Ser Gly Ile Arg Ala Leu Asn Glu Lys Gly Ser Asp Val 195 200 205 Val Val Gln Thr Leu Gln Asp Leu Ile Asp Val Gly Arg Asp Ala Glu 210 215 220 Phe Ser Phe Leu Pro Ile Gln Ala Gln Asp Gln Asp Asp Leu Ala Leu 225 230 235 240 Leu Ile His Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Cys Ile 245 250 255 Ser Ser Arg Ala Leu Ile Asn Thr Trp Arg His Val Ser Gly Pro Tyr 260 265 270 Pro Lys Val Thr Val Val Leu Ala Pro Phe His His Met Met Gly Arg 275 280 285 Asp Ser Met Ile Thr Ala Leu Gly Ala Gly Gly Thr Ala Tyr Phe Thr 290 295 300 Leu Arg Pro Asp Leu Ser Thr Val Ile Glu Asp Ile Arg Leu Ala Arg 305 310 315 320 Pro Thr Gly Leu Val Leu Phe Pro Arg Leu Cys Glu Val Ile Glu His 325 330 335 His Leu Thr Thr Ala Pro Glu Tyr Ser Gly Asn Glu Ile Leu Gly Gly 340 345 350 Arg Leu Gln Ser Ile Val Val Ala Ser Ala Pro Ile Thr Pro Arg Leu 355 360 365 Lys Ala Ser Leu Glu Cys Leu Leu Gly Val Pro Val Ser Glu Gly Tyr 370 375 380 Ser Ser Thr Glu Thr Ala Ser Gly Gly Leu Ala Met Asn Gly Leu Leu 385 390 395 400 Asn Arg Asn Asn Ile Leu Ala Tyr Arg Leu Arg Asp Val Pro Glu Ala 405 410 415 Gly Tyr Ser Val Asn Asp Arg Pro Phe Pro Arg Gly Glu Leu Cys Val 420 425 430 Lys Thr Arg Phe Gly Ile Ser Gly Tyr Phe Arg Asn Pro Glu Ala Thr 435 440 445 Ala Glu Leu Phe Asp Asp Asp Gly Phe Tyr Cys Thr Gly Asp Ile Val 450 455 460 Glu Glu Arg Ala Pro Asp Gln Ile Ala Ile Ile Asp Arg Arg Lys Asn 465 470 475 480 Val Ile Lys Leu Ala Gln Gly Glu Tyr Val Ala Val Gly Arg Leu Glu 485 490 495 Gln Leu Phe Gln Glu Gly Cys Gly Cys Val Gln Gln Ile His Leu His 500 505 510 Gly Asp Ser Thr Arg Ala Tyr Leu Leu Ala Val Val Val Pro Asp Arg 515 520 525 Asn Thr Leu Ala Pro Pro Gly Ser Arg Gln Ala Ser Glu Ala Glu Leu 530 535 540 Lys Ala Arg Val Arg Glu Glu Ile Leu Thr Leu Ala Asn Gln Arg Glu 545 550 555 560 Leu Arg Gly Phe Glu Ile Pro Arg Asp Leu Ile Leu Ala Glu Glu Pro 565 570 575 Phe Ser Gln Gln Asn Gly Leu Leu Ser Ser Leu Gly Lys Pro Ile Arg 580 585 590 Pro Ala Ile Arg Ala Arg Tyr Arg Ser Arg Leu Glu Ser Leu Tyr Ala 595 600 605 Ser His Glu Ala Thr Arg Gly Thr Glu Leu Glu Ala Ile Arg Ala Ser 610 615 620 Ala Gly Ala Val Asp Val Glu Thr Thr Leu Leu Ala Leu Leu Ser Ser 625 630 635 640 Thr Leu Gly Val Val Cys Gly Ala Ala Asp Arg Gln Thr Ser Phe Arg 645 650 655 Glu Leu Gly Gly Asp Ser Leu Ala Ala Val Gln Leu Ala Met Glu Ile 660 665 670 Lys Lys Gln Phe Gly Val Gly Leu Glu Gly Ser Gln Ile Leu Gly Pro 675 680 685 Gly Gly Thr Val Glu Ala Trp Ala Arg Arg Ile His Thr Ala Ser Ile 690 695 700 Gln Gln Ala Pro His Gln Arg Val Gly Ser Pro Leu Ala Ala Ile Pro 705 710 715 720 Ala Glu Gly Trp Leu Lys Pro Asp His Tyr Arg Leu Glu Asn Leu Ile 725 730 735 Gly Ile Pro Ile Gly Thr Pro Ser Ala Glu Val Ala Arg Pro Thr Gly 740 745 750 Gly Pro Pro Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Gly 755 760 765 Arg Leu Cys Leu Glu Trp Leu Gln Arg Leu Ala Gly Gln Gly Gly Arg 770 775 780 Leu Ile Cys Leu Val Arg Pro Ser Asn Ser His Ser Ala Trp Glu Arg 785 790 795 800 Leu Arg Asn Arg Phe Ser His Leu Glu Pro Glu Gln Val Ala Arg Phe 805 810 815 Arg Glu Leu Ala Gly Arg His Leu Glu Val Ile Pro Ala Asp Ile Gly 820 825 830 Glu Pro Gly Leu Gly Leu Glu Pro Gly Cys Gln Glu Arg Leu Ala Thr 835 840 845 Glu Val Asp Ala Ile Cys His Cys Ala Ala Glu Val Asn His Arg Leu 850 855 860 Pro Tyr Arg His Leu Tyr Arg Pro Asn Val Ile Gly Thr Ala Glu Ile 865 870 875 880 Ile His Leu Ala Ile Thr Thr Arg Leu Lys Ser Val Asp Phe Ile Ser 885 890 895 Ser Ile Gly Val Ala Ser Leu Pro Arg Arg Pro Gly Gly Ser Ile Pro 900 905 910 Val Glu Gly Gly Tyr Ala Arg Gly Tyr Phe Ala Ser Lys Trp Ala Cys 915 920 925 Glu Gln Leu Leu Arg Ser Thr His Asp Cys Thr Gly Val Pro Val Arg 930 935 940 Val Ile Arg Pro Ser Leu Ile Leu Pro Asp Arg Val Leu Ala Gly Glu 945 950 955 960 Met Asn Pro Asp Asp Leu Leu Ser Arg Leu Leu Tyr Ser Ile Leu Val 965 970 975 Thr Gly Ile Ala Pro Gly Cys Phe Gly Glu Glu Ser Gln Asn Ser Gly 980 985 990 Arg Ser Gly Phe Ser Val Gln Gly Leu Pro Val Asp Gln Leu Ala Gln 995 1000 1005 Thr Ile Leu Ala Leu Gly Glu Ala Arg Thr Glu Gly Phe His Val 1010 1015 1020 Leu Asn Leu Asn Ala Asp Ser Gly Ser Gly Val Pro Leu Asp Ala 1025 1030 1035 Ile Leu Gln Asp Ile Ala Ala Lys Gly Ile Arg Leu Arg Arg Val 1040 1045 1050 Glu Gly Tyr Asp Leu Trp Leu Asp Ala Ile Thr Thr Arg Leu Arg 1055 1060 1065 Arg Leu Pro Ala Glu Gln Arg Ala Arg Ser Leu Leu Asp Val Ala 1070 1075 1080 Glu Ala Tyr Ala Gly Ser Ala Gly Gln Thr Thr Gln Ser Ser Gly 1085 1090 1095 Glu Met Gln Ala Gly Ser Ser Ser Cys Pro Glu Glu Ile Thr Ser 1100 1105 1110 Leu Gln Pro Asp Phe Ser Arg Ala Tyr Arg Arg Lys Ile Val Asp 1115 1120 1125 Asp Leu Ala Arg Trp Gly Leu Ile Glu Pro Pro Gly Pro Val Asp 1130 1135 1140 Gln <210> 160 <211> 1052 <212> PRT <213> Artificial Sequence <220> <223> Neurospora crassa <400> 160 Met Ser Gln Gln Gln Asn Pro Pro Tyr Gly Arg Arg Leu Ile Leu Asp 1 5 10 15 Ile Ile Lys Glu Arg Ala Leu Asn Glu Pro Asn Arg Glu Trp Val Ser 20 25 30 Val Pro Arg Ser Ser Asp Pro Lys Asp Gly Trp Lys Ile Leu Thr Tyr 35 40 45 Leu Asp Ala Tyr Asn Gly Ile Asn Arg Val Ala His Lys Leu Thr Gln 50 55 60 Val Cys Gly Ala Ala Ala Pro Gly Ser Phe Pro Thr Val Ala Tyr Ile 65 70 75 80 Gly Pro Asn Asp Val Arg Tyr Leu Val Phe Ala Leu Gly Ala Val Lys 85 90 95 Ala Gly Tyr Lys Ala Leu Phe Ile Ser Thr Arg Asn Ser Ala Glu Ala 100 105 110 Gln Val Asn Leu Phe Glu Leu Thr Asn Cys Asn Val Leu Val Phe Asp 115 120 125 Gln Ser Tyr Lys Ala Thr Val Gln Pro Trp Leu His Glu Arg Glu Met 130 135 140 Thr Ala Ile Leu Ala Leu Pro Ala Asp Glu Trp Phe Pro Ala Asp Gln 145 150 155 160 Glu Asp Phe Pro Tyr Asn Lys Thr Phe Glu Glu Ala Glu Trp Asp Pro 165 170 175 Leu Met Val Leu His Thr Ser Gly Ser Thr Gly Phe Pro Lys Pro Ile 180 185 190 Val Ala Arg Gln Gly Met Leu Ala Val Ala Asp Gln Phe His Asn Leu 195 200 205 Pro Pro Arg Glu Asp Gly Lys Leu Met Trp Ile Val Glu Met Ser Lys 210 215 220 Arg Ala Lys Arg Leu Met His Pro Met Pro Leu Phe His Ala Ala Gly 225 230 235 240 Met Tyr Ile Ser Met Leu Met Ile His Tyr Trp Asp Thr Pro Gly Ala 245 250 255 Leu Gly Ile Gly Glu Arg Pro Leu Ser Ser Asp Leu Val Leu Asp Tyr 260 265 270 Ile Glu Tyr Ala Asp Val Glu Gly Met Ile Leu Pro Pro Ala Ile Leu 275 280 285 Glu Glu Leu Ser Arg Asp Glu Lys Ala Ile Gln Ser Leu Gln Lys Leu 290 295 300 Asn Phe Val Ser Phe Gly Gly Gly Asn Leu Ala Pro Glu Ala Gly Asp 305 310 315 320 Arg Leu Val Glu Asn Asn Val Thr Leu Cys Asn Leu Ile Ser Ala Thr 325 330 335 Glu Phe Thr Pro Phe Pro Phe Tyr Trp Gln Tyr Asp Gln Lys Leu Trp 340 345 350 Arg Tyr Phe Asn Phe Asp Thr Asp Leu Phe Gly Ile Asp Trp Arg Leu 355 360 365 His Asp Gly Glu Ser Thr Tyr Glu Gln Val Ile Val Arg Lys Asp Lys 370 375 380 His Pro Gly Leu Gln Gly Phe Phe Tyr Thr Phe Pro Asp Ser Ser Glu 385 390 395 400 Tyr Ser Thr Lys Asp Leu Tyr Lys Arg His Pro Thr His Glu Asp Phe 405 410 415 Trp Ile Tyr Gln Gly Arg Ala Asp Asn Ile Ile Val Phe Ser Asn Gly 420 425 430 Glu Lys Leu Asn Pro Ile Thr Ile Glu Glu Thr Leu Gln Gly His Pro 435 440 445 Lys Val Met Gly Ala Val Val Val Gly Thr Asn Arg Phe Gln Pro Ala 450 455 460 Leu Ile Ile Glu Pro Val Glu His Pro Glu Thr Glu Glu Gly Arg Lys 465 470 475 480 Ala Leu Leu Asp Glu Ile Trp Pro Thr Val Val Arg Val Asn Lys Glu 485 490 495 Thr Val Ala His Gly Gln Ile Gly Arg Gln Tyr Met Ala Leu Ser Thr 500 505 510 Pro Gly Lys Pro Phe Leu Arg Ala Gly Lys Gly Thr Val Leu Arg Pro 515 520 525 Gly Thr Ile Asn Met Tyr Lys Ala Glu Ile Asp Lys Ile Tyr Glu Asp 530 535 540 Ala Glu Lys Gly Val Ala Thr Asp Glu Val Pro Lys Leu Asp Leu Ser 545 550 555 560 Ser Ser Asp Ala Leu Ile Val Ser Ile Glu Lys Leu Phe Glu Thr Ser 565 570 575 Leu Asn Ala Pro Lys Leu Glu Ala Asp Thr Asp Phe Phe Thr Ala Gly 580 585 590 Val Asp Ser Met Gln Val Ile Thr Ala Ser Arg Leu Ile Arg Ala Gly 595 600 605 Leu Ala Ala Ala Gly Val Asn Ile Glu Ala Ser Ala Leu Ala Thr Arg 610 615 620 Val Ile Tyr Gly Asn Pro Thr Pro Lys Arg Leu Ala Asp Tyr Leu Leu 625 630 635 640 Ser Ile Val Asn Lys Asp Ser Asn Gln Gly Thr Leu Asp Asn Glu His 645 650 655 His Val Met Glu Ala Leu Val Glu Lys Tyr Thr Arg Asp Leu Pro Thr 660 665 670 Pro Lys Gln Asn Lys Pro Ala Pro Ala Asp Glu Gly Gln Val Val Val 675 680 685 Ile Thr Gly Thr Thr Gly Gly Ile Gly Ser Tyr Leu Ile Asp Ile Cys 690 695 700 Ser Ser Ser Ser Arg Val Ser Lys Ile Ile Cys Leu Asn Arg Ser Glu 705 710 715 720 Asp Gly Lys Ala Arg Gln Thr Ala Ser Ser Ser Gly Arg Gly Leu Ser 725 730 735 Thr Asp Phe Ser Lys Cys Glu Phe Tyr His Ala Asp Met Ser Arg Ala 740 745 750 Asp Leu Gly Leu Gly Pro Glu Val Tyr Ser Arg Leu Leu Ser Glu Val 755 760 765 Asp Arg Val Ile His Asn Gln Trp Pro Val Asn Phe Asn Ile Ala Val 770 775 780 Glu Ser Phe Glu Pro His Ile Arg Gly Cys Arg Asn Leu Val Asp Phe 785 790 795 800 Ser Tyr Lys Ala Asp Lys Asn Val Pro Ile Val Phe Val Ser Ser Ile 805 810 815 Gly Thr Val Asp Arg Trp His Asp Glu Asp Arg Ile Val Pro Glu Ala 820 825 830 Ser Leu Asp Asp Leu Ser Leu Ala Ala Gly Gly Tyr Gly Gln Ser Lys 835 840 845 Leu Val Ser Ser Leu Ile Phe Asp Lys Ala Ala Glu Val Ser Gly Val 850 855 860 Pro Thr Glu Val Val Arg Val Gly Gln Val Ala Gly Pro Ser Ser Glu 865 870 875 880 Lys Gly Tyr Trp Asn Lys Gln Glu Trp Leu Pro Ser Ile Val Ala Ser 885 890 895 Ser Ala Tyr Leu Gly Val Leu Pro Asp Ser Leu Gly Gln Met Thr Thr 900 905 910 Ile Asp Trp Thr Pro Ile Glu Ala Ile Ala Lys Leu Leu Leu Glu Val 915 920 925 Ser Gly Val Ile Asp Asn Val Pro Leu Asp Lys Ile Asn Gly Tyr Phe 930 935 940 His Gly Val Asn Pro Glu Arg Thr Ser Trp Ser Ala Leu Ala Pro Ala 945 950 955 960 Val Gln Glu Tyr Tyr Gly Asp Arg Ile Gln Lys Ile Val Pro Leu Asp 965 970 975 Glu Trp Leu Glu Ala Leu Glu Lys Ser Gln Glu Lys Ala Glu Asp Val 980 985 990 Thr Arg Asn Pro Gly Ile Lys Leu Ile Asp Thr Tyr Arg Thr Trp Ser 995 1000 1005 Glu Gly Tyr Lys Lys Gly Thr Lys Phe Val Pro Leu Asp Met Thr 1010 1015 1020 Arg Thr Lys Glu Tyr Ser Lys Thr Met Arg Glu Met His Ala Val 1025 1030 1035 Thr Pro Glu Leu Met Lys Asn Trp Cys Arg Gln Trp Asn Phe 1040 1045 1050 <210> 161 <211> 1139 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces fradiae <400> 161 Met Arg Leu Ala His Val Val Ala Ser Val Met Glu Arg His Ala Asp 1 5 10 15 Arg Pro Val Ile Gly Glu Arg Val Lys Glu Phe Ala Arg Asp Asp Glu 20 25 30 Thr Gly Arg Thr Val Ile Arg Leu Leu Pro Arg Tyr Glu Thr Thr Ser 35 40 45 Tyr Gln Glu Leu Trp Ala Arg Val Arg Ser Val Ala Ser Asp Trp His 50 55 60 His His Pro Ser His Ala Leu Thr Ala Gly Glu Arg Val Ala Leu Leu 65 70 75 80 Gly Phe Thr Ser Arg Asp Tyr Thr Thr Val Asp Leu Ala Cys Ile His 85 90 95 Leu Gly Ala Val Ala Val Pro Leu Gln Thr Ser Ala Ala Pro Ala Gln 100 105 110 Leu Arg Ser Ile Val Ala Glu Thr Glu Pro Ala Val Val Ala Ala Ser 115 120 125 Leu Glu Arg Met Asp Ala Ala Val Asp Leu Val Arg Asp Ser Pro Ser 130 135 140 Val Arg Arg Leu Val Val Phe Asp His His Pro Glu Ala Asp Asp His 145 150 155 160 Arg Glu Ala Tyr Asp Ala Ala Arg Ala Arg Leu Ala Glu Ala Arg Pro 165 170 175 Asp Val Leu Val Glu Pro Leu Thr Glu Ile Val Arg Arg Gly Ala Asp 180 185 190 Leu Pro Glu Ala Pro Leu Phe Ala Ala Pro Glu Gly Glu Asp Pro Leu 195 200 205 Ala Met Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 210 215 220 Met Tyr Thr Glu Arg Leu Ala Ala Ala Met Trp Gly Gly Ala Trp Ala 225 230 235 240 Lys Leu Phe Asp Glu Thr Tyr Ala Val Thr Phe His Tyr Met Pro Met 245 250 255 Ser His Val Ala Gly His Ser Ser Leu Lys Ala Thr Met Val Arg Gly 260 265 270 Gly Ala Ser Tyr Phe Thr Ala Ser Ser Asp Leu Ser Thr Phe Phe Glu 275 280 285 Asp Ile Ala Leu Ala Arg Pro Thr Glu Leu Ser Leu Val Pro Arg Val 290 295 300 Cys Glu Met Ile His Gln Arg Phe Arg Ser Glu Val Asp Arg Arg Thr 305 310 315 320 Ala Ala Gly Ala Asp Pro Ala Ala Ala Glu Ala Glu Val Arg Ala Asp 325 330 335 Ile Arg Asp Asn Val Leu Gly Gly Arg Val Thr Trp Ala Ser Cys Ala 340 345 350 Ser Ala Pro Leu Ser Ala Glu Leu Thr Ala Phe Thr Glu Ser Leu Leu 355 360 365 Gly Leu Glu Leu His Asn Val Tyr Gly Ser Thr Glu Ala Ala Gly Val 370 375 380 Ser Val Asp Gly Val Leu Leu Arg Pro Pro Val Thr Asp Tyr Lys Leu 385 390 395 400 Ala Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Ser Pro His Pro 405 410 415 Arg Gly Glu Leu Leu Leu Lys Thr Asp Val Ile Ile Pro Gly Tyr Tyr 420 425 430 Lys Gln Pro Glu Leu Thr Ala Glu Leu Phe Asp Glu Asp Gly Tyr Tyr 435 440 445 Arg Thr Gly Asp Ile Val Ala Glu Leu Glu Pro Asp Arg Ile Ala Ile 450 455 460 Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val 465 470 475 480 Ala Thr Ser Arg Leu Glu Ala Val Phe Ala Ala Ser Pro Leu Val Arg 485 490 495 Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ser Tyr Leu Leu Ala Val 500 505 510 Val Val Pro Thr Pro Asp Ala Leu Arg Ala Ala Asp Gly Asp Glu Arg 515 520 525 Ala Leu Arg Arg Ala Leu Gly Thr Ser Leu Gln Glu Leu Ala Arg Glu 530 535 540 Ser Gly Leu Asn Ser Tyr Glu Ile Pro Arg Asp Leu Leu Val Glu Thr 545 550 555 560 Glu Pro Phe Ser Gln Ala Asn Gly Leu Leu Ser Asp His Arg Lys Leu 565 570 575 Leu Trp Pro Arg Leu Val Glu Arg Tyr Gly Glu Arg Leu Glu Gln Leu 580 585 590 Tyr Ala Asp Thr Ala Ala Arg Glu Asp Glu Glu Leu Arg Glu Ile Arg 595 600 605 Arg Thr Gly Ala Asp Arg Pro Val Leu Glu Thr Val Gln Arg Ala Ala 610 615 620 Arg Ala Leu Leu Gly Gly Ser Ala Ala Ala Ile Gly Pro Asp Ala Arg 625 630 635 640 Phe Arg Asp Leu Gly Gly Asp Ser Leu Ser Ala Val Ser Phe Ser Ala 645 650 655 Leu Leu Gln Glu Thr Phe Gly Val Arg Val Pro Val Asp Val Val Ile 660 665 670 Ser Pro Ala Ser Asp Leu Arg His Leu Ala Glu Tyr Ile Glu Gly Arg 675 680 685 Arg Gly Ala Ala Asp Arg Pro Thr Phe Ala Ser Val His Gly Glu Gly 690 695 700 Ala Thr Glu Val His Ala Lys Asp Leu Thr Leu Asp Ala Phe Val Asp 705 710 715 720 Ala Ser Thr Leu Ala Ala Ala Arg Thr Leu Pro Arg Ala His Asp Glu 725 730 735 Pro Arg Thr Val Leu Leu Thr Gly Ala Ser Gly Trp Leu Gly Arg Phe 740 745 750 Leu Val Leu Gln Trp Leu Glu Arg Leu Ala Pro Ser Gly Gly Arg Val 755 760 765 Val Ala Leu Val Arg Gly Arg Asp Ala Glu Ala Ala Arg Arg Arg Leu 770 775 780 Asp Ala Ala Phe Asp Ser Gly Asp Pro Glu Leu Arg Arg Ala Tyr Glu 785 790 795 800 Thr Leu Ala Glu Gly Arg Leu Glu Val Val Ala Gly Asp Met Ala Ala 805 810 815 Pro Gly Leu Gly Leu Asp Glu Ala Val Trp Glu Arg Leu Ala Asp Glu 820 825 830 Val Asp Leu Val Val His Ala Gly Ala Leu Val Asn His Val Leu Pro 835 840 845 Tyr Pro Glu Leu Phe Glu Ala Asn Val Val Gly Thr Ala Glu Leu Ile 850 855 860 Arg Leu Ala Leu Thr Arg Arg Leu Lys Pro Phe Thr Tyr Ile Ser Ser 865 870 875 880 Val Ala Val Ala Thr Ser Leu Pro Gly Gly Ala Ala Leu Asp Glu Asp 885 890 895 Ser Asp Val Arg Asp Ala Leu Pro Val Gln Pro Val Asp Gly Gly Tyr 900 905 910 Ala Gly Gly Tyr Ala Ala Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 915 920 925 Glu Ala His Asp Leu Cys Gly Leu Pro Val Thr Thr Phe Arg Ser Asn 930 935 940 Met Ile Leu Ala His Ser Arg Tyr Gly Gly Gln Leu Asn Val Pro Asp 945 950 955 960 Met Phe Ser Arg Leu Leu Phe Ser Val Leu Ala Thr Gly Ile Ala Pro 965 970 975 Arg Thr Phe Tyr Arg Gly Asp Ala Ala Arg Ala His Tyr Asp Gly Leu 980 985 990 Pro Val Asp Phe Thr Ala Ala Ala Val Val Ala Leu Gly Gly Glu Thr 995 1000 1005 Gly Arg Ala Asp Thr Tyr Arg Thr Phe Ser Leu Val Asn Pro Asn 1010 1015 1020 Asp Asp Gly Val Gly Leu Asp Thr Phe Val Asp Trp Leu Thr Glu 1025 1030 1035 Ala Gly His Arg Val Glu Arg Leu Asp Asp Tyr Ala Asp Trp Tyr 1040 1045 1050 Ala Arg Phe Glu Ala Ala Met Arg Ala Leu Pro Glu Ala Gln Arg 1055 1060 1065 Arg His Ser Ala Leu Pro Ile Leu His Gly Phe Arg Glu Pro Glu 1070 1075 1080 Glu Pro Val Pro Gly Ser Val Ile Pro Ser Asp Arg Phe Arg Ala 1085 1090 1095 Ala Val Arg Ala Gly Gly Val Gly Gly Tyr Arg Asp Ile Pro Gly 1100 1105 1110 Leu Asp Arg Pro Leu Leu Ala Lys Tyr Ala Gln Asp Leu Thr Ser 1115 1120 1125 Leu Ala Ser Ser Ala Gly Val Val Thr Arg Ala 1130 1135 <210> 162 <211> 1180 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium liflandii 128FXT <400> 162 Met Ser Ile Thr Cys Val Asp Thr Arg Ala Gln Arg Ser Ala His Arg 1 5 10 15 Ile Glu Gln Leu Tyr Ser Thr Asp Ala Gln Phe Ala Ala Ala Arg Pro 20 25 30 Ser Thr Thr Val Gly Ile Ala Ile Ser Lys Ser Arg Leu Gly Leu Arg 35 40 45 Gln Ile Ile Gln Thr Val Met Asp Gly Tyr Ala Gln Arg Pro Ala Leu 50 55 60 Gly Gln Arg Ala Thr Arg Val Val Thr Asp Pro Asn Thr Gly Arg Ser 65 70 75 80 Ser Ala Gln Leu Leu Ala Glu Phe Glu Thr Ile Thr Tyr Arg Glu Leu 85 90 95 Trp Asn Arg Thr Asn Ala Leu Thr Asn Ala Phe Ala Ala Glu Ala Leu 100 105 110 Ala Asp Arg Gly Gln Arg Val Cys Val Leu Gly Phe Ala Ser Ile Asp 115 120 125 Tyr Ala Thr Ile Asp Leu Ala Leu Thr Leu Leu Gly Ala Val Ser Val 130 135 140 Pro Leu Pro Thr Asn Ala Ala Arg Ala Gln Leu Cys His Ile Val Ser 145 150 155 160 Glu Thr Gln Pro Ser Leu Ile Ala Ser Ser Thr Glu Asn Leu Ser Asp 165 170 175 Ala Ile Ser Leu Val Leu Ser His Arg Ala Pro His Arg Val Val Val 180 185 190 Phe Asp Tyr Arg Pro Glu Leu Asp Ala His Arg Glu Ala Leu Glu Ala 195 200 205 Ala Arg Ala Arg Leu Ala Ala Ile Pro Val Thr Val Glu Thr Leu Thr 210 215 220 Ala Ile Ile Ala Arg Gly Arg Thr Val Arg Pro Ala Glu Ala Tyr Cys 225 230 235 240 Gly Thr Gln Ser Ala Asp Ala Pro Ala Leu Leu Ile Tyr Thr Ser Gly 245 250 255 Ser Thr Gly Ala Pro Lys Gly Val Val Tyr Thr Arg Lys Arg Val Ala 260 265 270 Asp Phe Trp Arg Thr Ser Lys Ala Glu Val Glu Pro Thr Glu Gln Arg 275 280 285 Thr Ala Pro Ser Ile Thr Leu Asn Phe Met Pro Met Ser His Ala Asn 290 295 300 Gly Arg Gln Val Leu Tyr Gly Thr Leu Ser Asn Gly Gly Thr Ala Tyr 305 310 315 320 Phe Thr Ala Arg Ser Asp Leu Ser Thr Leu Phe Asp Asp Leu Ala Leu 325 330 335 Val Arg Pro Thr Gln Leu Gly Phe Pro Pro Arg Ile Trp Asp Met Leu 340 345 350 Leu Glu Arg Phe Gly Arg Glu Val Asp Arg Arg Leu Arg Asp Gly Thr 355 360 365 Ala Glu Gly Ala Asp Pro Gly Ala Leu Lys Ala Arg Val Ala Ala Asp 370 375 380 Leu Arg Gln Val Leu Leu Gly Gly Arg Tyr Ala Leu Ala Met Met Gly 385 390 395 400 Ser Ala Pro Ile Ser Glu Gln Met Lys Ala Ser Val Glu Ser Leu Leu 405 410 415 Asp Leu Asp Val Met Glu Gly Tyr Gly Ser Thr Glu Ala Gly Thr Val 420 425 430 Ile Ile Asn Asn Glu Val Gln Arg Pro Gln Val Ile Asp Tyr Lys Leu 435 440 445 Val Asp Val Ala Glu Leu Gly Tyr Phe Leu Thr Asp Arg Pro Tyr Pro 450 455 460 Arg Gly Glu Leu Leu Val Lys Thr Arg Thr Leu Phe Ser Gly Tyr Tyr 465 470 475 480 Arg Asp Pro Glu Asp Gly Ala Gln Val Phe Asp Pro Asp Gly Phe Tyr 485 490 495 Arg Thr Gly Asp Ile Met Ala Gln Val Gly Pro Asp Arg Leu Ala Tyr 500 505 510 Leu Asp Arg Arg Asn Asn Val Leu Asn Leu Ser Gln Gly Glu Phe Val 515 520 525 Ala Val Ser Arg Leu Glu Ala Ile Phe Ala Asn Ser Pro Leu Val Arg 530 535 540 Gln Ile Phe Val Tyr Ala Asn Gly Ala Arg Ala Tyr Pro Leu Ala Val 545 550 555 560 Val Val Pro Thr Glu Asp Ala Gln Ser Arg His Gly Arg Ala Glu Leu 565 570 575 Lys Ala Glu Leu His Thr Ser Leu His Arg Val Ala Met Ser Ala Gly 580 585 590 Leu Glu Pro Tyr Glu Ile Pro Arg Asp Phe Ile Val Glu Thr Thr Pro 595 600 605 Phe Thr Pro Gln Asn Gly Leu Leu Thr Ala Ile His Lys Leu Ala Arg 610 615 620 Pro His Leu Thr Gln Arg Tyr Gly Ala Arg Leu Glu Leu Leu Tyr Thr 625 630 635 640 Glu Leu Ala Asp Ser Gln Thr Cys Arg Leu His Arg Leu Arg Gln Thr 645 650 655 Gly Gly Arg Leu Pro Ala Leu Glu Thr Ile Arg Arg Ala Ala Gly Ala 660 665 670 Leu Leu Gly Thr Ala Thr Thr Glu Pro Arg Pro Glu Ala His Phe Lys 675 680 685 Asp Leu Gly Gly Asp Ser Val Ser Ala Val Thr Phe Ser Asn Leu Leu 690 695 700 His Asp Ile Tyr Gly Phe Asp Val Pro Val Gly Val Ile Leu Gly Pro 705 710 715 720 Ala Thr Asp Leu Arg Ala Leu Ala Ser His Val Glu Ser Arg Arg Gly 725 730 735 Ala Gly Trp Ser Gly Pro Ser Phe Ala Ser Val His Ala Pro Arg Ala 740 745 750 Thr Ser Val His Ala Gly Asp Leu Lys Leu Ala Lys Phe Leu Asp Thr 755 760 765 Lys Thr Leu Ala Ala Ala Thr Ser Leu Pro Ala Ala Glu Ala Arg Ala 770 775 780 Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu 785 790 795 800 Val Leu Glu Trp Leu Arg Arg Leu Arg Ala Val Gly Gly Lys Leu Ile 805 810 815 Cys Leu Val Arg Ala Ala Ser Asp Glu Gln Ala Arg Val Arg Leu Asp 820 825 830 Thr Ala Phe Asp Ser Gly Asp Pro Arg Leu Leu Gly His Phe Arg Gln 835 840 845 Leu Ala Val Asp Arg Leu Glu Val Ile Ala Gly Asp Lys Ser Glu Pro 850 855 860 Gly Leu Gly Leu Asp Gly Arg Thr Trp Gln Arg Leu Ala Asp Thr Val 865 870 875 880 Asp Leu Ile Val Asp Pro Ala Thr Leu Val Asn His Val Leu Ser Tyr 885 890 895 Arg Gln Leu Phe Ala Pro Asn Val Ala Gly Thr Ala Glu Leu Leu Arg 900 905 910 Leu Ala Leu Thr Thr Lys Arg Lys Pro Tyr Ala Tyr Val Ser Thr Val 915 920 925 Ser Val Ala Asn Gln Ile Glu Pro Ser Ala Phe Thr Glu Asp Ala Asp 930 935 940 Ile Arg Glu Ile Ser Arg Thr Arg Thr Ile Asp Asp Ser Tyr Ala Asn 945 950 955 960 Gly Tyr Thr Thr Ser Lys Trp Ala Ser Glu Val Leu Leu Arg Glu Ala 965 970 975 His Asp Leu Cys Gly Leu Pro Val Thr Val Phe Arg Cys Asp Met Ile 980 985 990 Leu Ala Asp Thr Ser Tyr Ala Gly Gln Leu Asn Leu Ala Asp Thr Phe 995 1000 1005 Thr Arg Leu Met Leu Ser Val Ala Ala Thr Gly Ile Ala Pro Ala 1010 1015 1020 Ser Phe Tyr Arg Leu Gly Pro Asp Gly Lys Arg Gln Pro Ala His 1025 1030 1035 Phe Asp Gly Leu Pro Val Glu Phe Ile Gly Glu Ala Val Thr Thr 1040 1045 1050 Leu Gly Ala Arg Arg His Asp Gly Phe Gln Val His His Val Ala 1055 1060 1065 Asn Pro His His Asp Gly Val Gly Leu Asp Glu Tyr Val Asp Trp 1070 1075 1080 Leu Val Asp Ala Gly Cys Pro Ile Arg Arg Ile Pro Asp Tyr Asp 1085 1090 1095 Glu Trp Leu Ser Arg Phe Glu Thr Ala Leu His Ala Leu Pro Asp 1100 1105 1110 Arg Lys Arg Arg His Ser Leu Leu Pro Leu Leu Gln Asn Tyr Arg 1115 1120 1125 Glu Pro Ala Glu Pro Ile Arg Gly Gly Ile Ala Pro Ala Pro Arg 1130 1135 1140 Phe Arg Gly Ala Val Arg Gln Ala Lys Ile Gly Arg Asp Asn Asp 1145 1150 1155 Ile Pro His Val Gly Pro Ala Ile Ile Ala Lys Tyr Ala Ser Asp 1160 1165 1170 Leu Gln Leu Leu Gly Leu Ala 1175 1180 <210> 163 <211> 1187 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus <400> 163 Met Thr Val Thr Asn Glu Thr Asn Pro Gln Gln Glu Gln Leu Ser Arg 1 5 10 15 Arg Ile Glu Ser Leu Arg Glu Ser Asp Pro Gln Phe Arg Ala Ala Gln 20 25 30 Pro Asp Pro Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu 35 40 45 Ser Glu Ala Ile Ala Ala Leu Met Thr Gly Cys Ala Glu Arg Pro Ala 50 55 60 Leu Gly Glu Arg Ala Arg Glu Leu Val Ile Asp Gln Asp Gly Arg Thr 65 70 75 80 Thr Leu Arg Leu Leu Pro Arg Phe Asp Thr Thr Thr Tyr Gly Glu Leu 85 90 95 Trp Ser Arg Thr Thr Ser Val Ala Ala Ala Trp His His Asp Ala Thr 100 105 110 His Pro Val Lys Ala Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser 115 120 125 Ile Asp Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val 130 135 140 Ala Val Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Trp Thr Thr Ile 145 150 155 160 Leu Ala Glu Ala Glu Pro Asn Thr Leu Ala Val Ser Ile Glu Leu Ile 165 170 175 Cys Ala Ala Met Glu Ser Val Arg Ala Thr Pro Ser Ile Lys Gln Val 180 185 190 Val Val Phe Asp Tyr Thr Pro Glu Val Asp Asp Gln Arg Glu Ala Phe 195 200 205 Glu Ala Ala Ser Thr Gln Leu Ala Gly Thr Gly Ile Ala Leu Glu Thr 210 215 220 Leu Asp Ala Val Ile Ala Arg Gly Ala Ala Leu Pro Ala Ala Pro Leu 225 230 235 240 Tyr Ala Pro Ser Ala Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile 260 265 270 Val Arg Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn 275 280 285 Leu Pro Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly 290 295 300 Arg Gly Thr Leu Thr Ser Thr Leu Ser Thr Gly Gly Thr Gly Tyr Phe 305 310 315 320 Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile 325 330 335 Arg Pro Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe 340 345 350 Gln Arg Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Ser Gly Asp Thr 355 360 365 Ala Ser Ala Glu Ala Val Ala Ala Glu Val Lys Ala Asp Ile Arg Asp 370 375 380 Asn Leu Phe Gly Gly Arg Val Ser Ala Val Met Val Gly Ser Ala Pro 385 390 395 400 Leu Ser Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu Asn 405 410 415 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp 420 425 430 Gly Ile Val Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro His Pro Arg Gly Glu 450 455 460 Leu Leu Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Ser Val Phe Asp Ala Asp Gly Phe Tyr Met Thr Gly 485 490 495 Asp Ile Val Ala Glu Leu Ala His Asp Asn Ile Glu Ile Ile Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 515 520 525 Thr Leu Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr 530 535 540 Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 545 550 555 560 Thr Pro Glu Ala Val Ala Ala Ala Lys Gly Asp Ala Ala Ala Leu Lys 565 570 575 Thr Thr Ile Ala Asp Ser Leu Gln Asp Ile Ala Lys Glu Ile Gln Leu 580 585 590 Gln Ser Tyr Glu Val Pro Arg Asp Phe Ile Ile Glu Pro Gln Pro Phe 595 600 605 Thr Gln Gly Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro 610 615 620 Asn Leu Lys Ala His Tyr Gly Pro Arg Leu Glu Gln Met Tyr Ala Glu 625 630 635 640 Ile Ala Glu Gln Gln Ala Ala Glu Leu Arg Ala Leu His Gly Val Asp 645 650 655 Pro Asp Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala Leu 660 665 670 Leu Gly Val Ser Ser Ala Glu Leu Ala Ala Asp Ala His Phe Thr Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Asp Leu Leu Arg 690 695 700 Asp Ile Phe Ala Val Glu Val Pro Val Gly Val Ile Val Ser Ala Ala 705 710 715 720 Asn Asp Leu Gly Gly Val Ala Lys Phe Val Asp Glu Gln Arg His Ser 725 730 735 Gly Gly Thr Arg Pro Thr Ala Glu Thr Val His Gly Ala Gly His Thr 740 745 750 Glu Ile Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala 755 760 765 Thr Leu His Ala Ala Pro Ser Leu Pro Lys Ala Ala Gly Ile Pro His 770 775 780 Thr Val Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly His Tyr Leu Ala 785 790 795 800 Leu Glu Trp Leu Glu Arg Leu Asp Lys Thr Asp Gly Lys Leu Ile Val 805 810 815 Ile Ile Arg Gly Lys Asn Ala Glu Ala Ala Tyr Gly Arg Leu Glu Glu 820 825 830 Ala Phe Asp Thr Gly Asp Thr Gln Leu Leu Ala His Phe Arg Ser Leu 835 840 845 Ala Asp Lys His Leu Glu Val Leu Ala Gly Asp Ile Gly Asp Pro Asn 850 855 860 Leu Gly Leu Asp Ala Asp Thr Trp Gln Arg Leu Ala Asp Thr Val Asp 865 870 875 880 Val Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Lys Leu 900 905 910 Ala Ile Thr Thr Lys Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ala 915 920 925 Val Ala Ala Tyr Val Asp Pro Thr Thr Phe Asp Glu Glu Ser Asp Ile 930 935 940 Arg Leu Ile Ser Ala Val Arg Pro Val Asp Glu Leu Tyr Ala Asn Gly 945 950 955 960 Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Arg Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Gly Ser 1010 1015 1020 Phe Tyr Gln Ala Gln Thr Thr Gly Glu Arg Pro Leu Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Gly Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Thr Gln Val Pro Glu Gly Ser Glu Gly Phe Val Thr Tyr Asp 1055 1060 1065 Cys Val Asn Pro His Ala Asp Gly Ile Ser Leu Asp Asn Phe Val 1070 1075 1080 Asp Trp Leu Ile Glu Ala Gly Tyr Pro Ile Ala Arg Ile Asp Asn 1085 1090 1095 Tyr Thr Glu Trp Phe Thr Arg Phe Asp Thr Ala Ile Arg Gly Leu 1100 1105 1110 Pro Glu Lys Gln Lys Gln His Ser Leu Leu Pro Leu Leu His Ala 1115 1120 1125 Phe Glu Gln Pro Ser Ala Ala Glu Asn His Gly Val Val Pro Ala 1130 1135 1140 Lys Arg Phe Gln His Ala Val Gln Ala Ala Gly Ile Gly Pro Val 1145 1150 1155 Gly Gln Asp Gly Thr Thr Asp Ile Pro His Leu Ser Arg Arg Leu 1160 1165 1170 Ile Val Lys Tyr Ala Lys Asp Leu Glu Gln Leu Gly Leu Leu 1175 1180 1185 <210> 164 <211> 1167 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium vaccae ATCC 25954 <400> 164 Met Phe Val Val Pro Asp Asp Gly His Pro Pro Pro Ser Leu Pro Ile 1 5 10 15 Asp Arg Lys Ser Val Met Pro Thr Ser Asp His Asp Gln Trp Leu Arg 20 25 30 Arg Phe Glu Gln Leu Thr Ser Ser Asp Ala Gln Leu Val Ala Ala Gln 35 40 45 Pro Asp Pro Ala Val Thr Asp Ala Ile Ser Ser Pro Asp Ala Arg Leu 50 55 60 Val Asp Val Met Arg Thr Val Met Thr Gly Tyr Ala Asp Arg Pro Ala 65 70 75 80 Leu Gly Gln Arg Ala Val Glu Phe Val Thr Asp Val Thr Gly Arg Thr 85 90 95 Val Ala Glu Leu Gln Pro Arg Phe Glu Thr Leu Thr Tyr Gly Glu Thr 100 105 110 Trp Ala Arg Val Arg Ala Leu Ala His Ala Leu Ile Asn Asp Pro Val 115 120 125 Arg Pro Gly Asp Arg Ile Ala Thr Leu Gly Phe Thr Ser Ala Asp Tyr 130 135 140 Ala Val Val Asp Met Ala Val Ser Leu Thr Gly Ala Val Gly Val Pro 145 150 155 160 Leu Gln Thr Ser Ala Ala Leu Ala Gln Leu Gln Pro Ile Val Val Glu 165 170 175 Ser Ala Pro Ala Val Ile Leu Ser Ser Val Gly Asp Leu Ala Asp Ala 180 185 190 Val Glu Leu Ala Leu Ser Ala His Ala Pro Glu Arg Val Ile Val Phe 195 200 205 Asp Tyr His Pro Gln Leu Asp Glu His Arg Asp Ala Phe Ala Ala Ala 210 215 220 Ala Asp Arg Leu His Asp Ile Pro Leu Glu Ser Leu Asp Asp Val Ile 225 230 235 240 Ala Arg Gly Ala Glu His Leu Ala Glu Ser Glu Pro Asp Ala Gly Ala 245 250 255 Pro Asp Asp Leu Arg Met Leu Val Tyr Thr Ser Gly Ser Thr Gly Ala 260 265 270 Pro Lys Gly Ala Met Tyr Thr Asp Arg Leu Met Ala Asn Cys Trp Arg 275 280 285 Gly Trp Phe Ser Pro Glu Arg Asn Val Asp Gly Arg Leu Pro Ala Ile 290 295 300 Thr Leu Asp Phe Met Pro Leu Ser His Val Met Gly Arg Val Val Leu 305 310 315 320 Tyr Gly Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Thr Ala Arg Ser 325 330 335 Asp Leu Ser Thr Leu Leu Asp Asp Leu Ala Leu Val Arg Pro Thr Arg 340 345 350 Leu Asp Phe Val Pro Arg Ile Trp Glu Met Leu Phe Gln Glu Val Gln 355 360 365 Asn Ser Gly Gly Gln Gly Lys Asp Leu Leu Gly Gly Arg Gln Leu Phe 370 375 380 Ala Met Thr Gly Ser Ala Pro Thr Ser Pro Glu Leu Arg Gln Trp Ala 385 390 395 400 Glu Asp Tyr Thr Gly Ile His Ile Ile Asp Gly Tyr Gly Ser Thr Glu 405 410 415 Ala Gly Ile Ala Leu Val Asp Gly Glu Ile Gln Arg Pro Ala Val Leu 420 425 430 Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe Thr Thr Asp 435 440 445 Arg Pro His Pro Arg Gly Glu Leu Phe Leu Lys Thr Thr Asn Leu Ile 450 455 460 Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Glu Leu Phe Asp Ala 465 470 475 480 Asp Gly Trp Tyr His Thr Gly Asp Val Met Ala Glu Val Gly Pro Asp 485 490 495 Arg Leu Glu Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln 500 505 510 Gly Glu Phe Val Thr Val Ser Thr Leu Glu Ala Ala Tyr Gly Gly His 515 520 525 Pro Ser Ile Arg Gln Ile Phe Val Tyr Gly Asn Ser Ser Arg Ser Tyr 530 535 540 Val Leu Ala Val Ile Val Pro Thr Asp Asp Val Leu Ala Gly Val Gly 545 550 555 560 Gly Asp Val Thr Ala Val Lys Pro Val Leu Ala Glu Ala Leu Gln Ala 565 570 575 Val Ala Arg Gly Ala Gly Leu Gln Ser Phe Glu Ile Pro Arg Asp Phe 580 585 590 Leu Val Glu Thr Gln Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly 595 600 605 Ile Arg Lys Leu Ala Arg Pro Gln Leu Lys Gln Arg Tyr Gly Pro Ala 610 615 620 Leu Glu Gln Leu Tyr Thr Asp Leu Ala Glu Gly Gln Ala Asp Val Leu 625 630 635 640 Arg Glu Leu Arg Arg Thr Gly Ala Asp Gly Pro Ala Leu Gln Thr Val 645 650 655 Thr His Ala Ala Glu Ala Leu Leu Gly Thr Thr Gly Ala Ala Pro Asp 660 665 670 Thr Ala Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe 675 680 685 Gly Asn Leu Leu His Asp Ile Phe Asp Val Asp Val Pro Val Gly Val 690 695 700 Ile Val Ser Pro Ala Ser Asp Leu Ala Ala Ile Ala Ala Tyr Val Glu 705 710 715 720 Ala Gln Arg Ala Gly Gly Ala Thr Arg Pro Ser Tyr Asp Ala Val His 725 730 735 Gly Pro Ala Ala Thr Glu Val His Ala Lys Asp Leu Thr Leu Asp Arg 740 745 750 Phe Leu Asp Glu Ala Thr Leu Ala His Ala Ala Ala Leu Pro Gly Pro 755 760 765 Ser Gly Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu 770 775 780 Gly Arg Tyr Leu Ala Leu His Trp Leu Glu Gln Met Ser Leu Val Gly 785 790 795 800 Gly Thr Val Ile Ala Leu Ile Arg Ala Lys Asp Asp Ala Ala Ala Arg 805 810 815 Ala Arg Leu Asp Ala Thr Phe Ser Ser Asp Pro Arg Leu Leu Ala His 820 825 830 Tyr Arg Glu Leu Ala Ala Glu His Leu Glu Val Leu Ala Gly Asp Lys 835 840 845 Gly Glu Ala Asp Leu Gly Leu Thr Arg Ala Thr Trp Gln Arg Leu Ala 850 855 860 Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn His Val 865 870 875 880 Leu Pro Tyr Arg Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu 885 890 895 Leu Ile Arg Leu Ala Leu Thr Thr Arg Ile Lys Pro Phe Val Tyr Val 900 905 910 Ser Thr Ile Gly Val Gly Asp Gly Ile Ala Pro Gly Arg Phe Val Glu 915 920 925 Asp Ala Asp Ile Arg Gln Ile Ser Ala Thr Arg Thr Ile Gly Asp Asn 930 935 940 Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu 945 950 955 960 Arg Glu Ala His Asp Leu Ala Gly Leu Pro Val Ser Val Phe Arg Cys 965 970 975 Asp Met Ile Met Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Val Pro 980 985 990 Asp Met Phe Thr Arg Leu Met Leu Ser Leu Ala Val Thr Gly Ile Ala 995 1000 1005 Pro Asn Ser Phe Tyr Glu Leu Asp Glu Gly Gly Ser Arg Gln Arg 1010 1015 1020 Ala His Phe Asp Gly Leu Pro Val Glu Phe Ile Ala Asp Ala Ile 1025 1030 1035 Ser Thr Ile Gly Ala Gln Val Ile Glu Gly Phe Glu Thr Tyr His 1040 1045 1050 Val Met Asn Pro His Asp Asp Ala Ile Ser Leu Asp Thr Phe Val 1055 1060 1065 Asp Trp Leu Ile Ala Ala Gly Tyr Pro Ile Val Arg Val Pro Gly 1070 1075 1080 Tyr Ala Ala Trp Leu Gln Arg Phe Asp Thr Ala Leu Arg Gly Leu 1085 1090 1095 Pro Glu Lys Gln Arg Gln Ala Ser Leu Leu Pro Leu Ile His Asn 1100 1105 1110 Tyr Gln His Pro Glu His Pro Ile Asn Gly Pro Leu Ala Pro Ala 1115 1120 1125 Asp Arg Phe Arg Ala Ala Val Gln Glu Ala Lys Ile Gly Pro Asp 1130 1135 1140 Lys Asp Ile Pro His Leu Ser Ala Pro Val Ile Val Lys Tyr Leu 1145 1150 1155 Thr Asp Leu Glu Leu Leu Gly Leu Ile 1160 1165 <210> 165 <211> 1325 <212> PRT <213> Artificial Sequence <220> <223> Sorangium cellulosum <400> 165 Met Asp Pro Ser Ser Asp Thr Arg Asp Pro Gln Glu Ser Glu Ile Thr 1 5 10 15 Gln Asn Asp Asp Ser Asn Glu Leu Leu Leu Thr Arg Ser Leu Glu Arg 20 25 30 Cys Ala Arg Leu Val Gln Thr Asp Glu Glu Leu Arg Arg Ala Leu Pro 35 40 45 Ser Pro Ala Ala Leu Glu Lys Ile Arg Arg Cys His Thr Thr Ile Glu 50 55 60 Cys Val Ala Thr Ala Phe Glu Leu Tyr Ala Asp Arg Pro Cys Leu Gly 65 70 75 80 His Arg Pro Leu Asp Ala Ala Ala Thr Ala Ala Asp Gly Gly Ser Ala 85 90 95 Pro Arg Tyr Leu Pro Glu Phe Arg Ala Val Ser Tyr Ala Asp Val Trp 100 105 110 Ser Arg Val Glu Ala Phe Ala Ser Gly Leu Gln His Glu Lys Leu Ala 115 120 125 Asn Thr Gly Asp Phe Val Gly Ile Ser Gly Phe Gly Ser Thr Asp Trp 130 135 140 Val Val Ala Gly Leu Ala Cys Met Tyr Leu Ser Ala Val Ser Val Pro 145 150 155 160 Leu Gln Thr Asp Leu Thr Pro Ala Asp Leu Glu Leu Ile Val Thr Glu 165 170 175 Ala Glu Leu Ala Cys Val Val Cys Ser Val Gly Gln Leu Ala Arg Ile 180 185 190 Glu Asp Ile Leu Pro Arg Cys Pro Ser Val Arg Ser Val Val Val Met 195 200 205 Asp Leu Leu Glu Gly Asp Arg Cys Gly Gln Ser Glu Leu Glu Arg Ala 210 215 220 Arg Arg Ala Leu Arg Pro Leu Glu Ala Arg Gly Arg Arg Leu Ala Val 225 230 235 240 Arg Ala Met His Glu Val Glu Arg Leu Gly Arg Gln Gln Gly Ile Ala 245 250 255 Pro Lys Val Leu Pro Ala Gln Arg Gly Glu Pro Asp Pro Leu Met Thr 260 265 270 Leu Met Tyr Thr Ser Gly Ser Thr Gly Ser Pro Lys Gly Ala Met Val 275 280 285 Pro Glu Ser Leu Trp Arg Arg Tyr Trp Gln Ile Ala Phe Thr Arg Ser 290 295 300 Gln Asp Pro Arg Leu Asp Leu Leu Pro His Val Gly Leu Asn Tyr Ser 305 310 315 320 Pro Met Asn His Phe Ile Gly Arg Ser Gln Val Gly Arg Ser Leu Met 325 330 335 Arg Gly Gly Ile Thr His Phe Val Leu Lys Ser Asp Met Ser Thr Leu 340 345 350 Phe Glu Asp Ile Arg Leu Ala Arg Pro Thr Thr Leu Phe Leu Val Pro 355 360 365 Arg Ile Ala Glu Leu Ile His Gln Gln Phe Gln Ala Asp Val Leu Arg 370 375 380 Arg Ala Arg Gly Leu Gly Ala Gly Gly Asp Asp Ala Ala Arg Arg Arg 385 390 395 400 Ile Glu Arg Glu Ile Met Ala Glu Met Arg Gly Ser Leu Leu Gly Asp 405 410 415 Arg Leu Leu Leu Ala Ser Ile Gly Ser Ala Pro Thr Pro Pro Glu Val 420 425 430 Leu Ser Phe Leu Lys Arg Cys Phe Asp Val Pro Val Phe Glu Gly Tyr 435 440 445 Gly Ser Thr Glu Ala Ser Ser Leu Thr Thr Asp Gly Arg Leu Asp Arg 450 455 460 Glu Leu Val Thr Glu Phe Lys Leu Val Asp Val Pro Glu Leu Gly Tyr 465 470 475 480 Ser Ala Thr Asp Gln Pro Tyr Pro Arg Gly Glu Leu His Ile Arg Ser 485 490 495 Ser Leu Met Val Pro Gly Tyr Tyr Lys Asn Glu Lys Ala Thr Arg Ala 500 505 510 Leu Phe Asp Glu Glu Gly Leu Met Asn Thr Gly Asp Ile Val Glu Gln 515 520 525 Arg Gly Pro Asp Thr Val Val Trp Ile Asp Arg Ala Arg Asn Val Leu 530 535 540 Lys Leu Ser Gln Gly Glu Phe Val Ala Thr Ser Arg Leu Glu Val Leu 545 550 555 560 Tyr Ser Ala Gly Ser Pro Phe Ile Gln Gln Ile Phe Leu Tyr Gly Asn 565 570 575 Ser Thr Arg Ser Tyr Leu Leu Ala Val Val Val Pro Glu Met Arg Glu 580 585 590 Ile Ser Ala His Leu Arg Gln Arg Asp Val Lys Pro Asp Gly Glu Pro 595 600 605 Val Arg Gln Leu Leu Arg Ala Glu Ile Asp Arg Ile Ala Arg Glu Asn 610 615 620 Gln Leu Arg Gly Tyr Glu Ile Pro Arg Asp Phe Leu Ile Glu Pro Ala 625 630 635 640 Pro Phe Thr Arg Ala Ser Gly Leu Leu Thr Glu Thr Gln Lys Pro Ala 645 650 655 Arg Ala Arg Leu Lys Ala Arg Tyr Gly Ala Arg Leu Glu Glu Leu Tyr 660 665 670 Ala Thr Ile Glu Arg Thr Gln Leu Gln Glu Leu Arg Asn Leu Arg Glu 675 680 685 Gly Gly Gly Ala Ala Pro Ala Ser Ala Ala Leu Val Val Lys Lys Ala 690 695 700 Leu Glu Ala Thr Leu Gly Ile Thr Gly Val Glu Pro Arg Ser Ala Arg 705 710 715 720 Ser Phe Ala Gln Leu Gly Gly Asp Ser Leu Ser Ala Val Arg Leu Ser 725 730 735 Arg Leu Ile Glu Glu Ile Ser Gly Val Ala Val Pro Val Gly Leu Val 740 745 750 Leu Asn Pro Thr Ser Ser Val Arg Ala Ile Ala Asp His Leu Glu His 755 760 765 Ala Leu Ala Gly Glu Ala Pro Arg Arg Ala Ala Arg Phe Asp Glu Val 770 775 780 His Gly Ala Gly Ala Glu Val Val Arg Ala Ala Asp Leu Arg Leu Asp 785 790 795 800 Arg Phe Leu Gly Pro Asp Glu Leu Ala Ala Ala Arg Arg Ala Thr Pro 805 810 815 Ala Ala Ala Leu Pro Ala Gln Ala Arg Val Ala Leu Leu Thr Gly Ala 820 825 830 Asn Gly Phe Leu Gly Arg Phe Leu Ala Leu Glu Leu Leu Glu Arg Leu 835 840 845 Pro Glu Glu Gly Arg Leu Tyr Cys Val Val Arg Ser Pro Asp Asp Ala 850 855 860 Leu Ala Phe Asp Arg Leu Arg Ala Thr Tyr Glu Ser Asp Pro Ala Leu 865 870 875 880 Leu Glu Arg Phe Asp Ala Leu Ser Ala His Gly Arg Leu Val Val Leu 885 890 895 Ala Gly Asp Leu Val Glu Pro Arg Phe Gly Leu Ala Asp Asp Leu Tyr 900 905 910 Ala His Leu Cys Val Glu Val Asp Cys Val Val His Asn Gly Ala Leu 915 920 925 Val Asn His Ala Leu Ser Tyr Pro Gln Leu Phe Glu Pro Asn Val Leu 930 935 940 Gly Thr Val Glu Ala Ile Arg Leu Ser Leu Ala His Arg Val Lys Ser 945 950 955 960 Met Asn Tyr Ile Ser Thr Ile Ala Ala Val Gly Gly Leu Asp Arg Ser 965 970 975 Gly Pro Ile Arg Glu Asp Glu Asp Ile Arg Glu Leu Trp Pro Glu Arg 980 985 990 Ala Leu Gly Ala Gly Tyr Ala Val Gly Tyr Ala Thr Ser Lys Trp Ala 995 1000 1005 Ser Glu Val Leu Leu Gln Asp Ala His Asp Ala Leu Gly Leu Pro 1010 1015 1020 Val Asn Val Tyr Arg Pro Ser Gly Ile Met Ala His Ser Leu Tyr 1025 1030 1035 Arg Ser Gln Ile Asn Val Pro Asp Phe Phe Thr Arg Leu Leu Cys 1040 1045 1050 Gly Val Val Tyr Thr Gly Leu Ala Pro Arg Ser Phe Tyr Glu Gly 1055 1060 1065 Gly Arg Pro His Arg Asp Gly His Tyr Asp Gly Leu Pro Val Asp 1070 1075 1080 Ala Val Ala Arg Ser Ile Ala Arg Arg Arg Arg Ser Thr Ala Pro 1085 1090 1095 His Gly Gly Arg Arg Arg Ser Thr Ala Pro His Gly Arg Gly Gly 1100 1105 1110 Gly Glu Gly Glu Pro Arg Asp Leu Ser Cys Arg Glu Pro Leu Leu 1115 1120 1125 Gly Arg Arg His Leu Ala Arg Arg His Arg Leu Val Gly Pro Ile 1130 1135 1140 Gly Gly Leu Pro Gly Gly Ala Arg Arg Arg Leu Arg Arg Val Val 1145 1150 1155 Arg Gly Val Pro Arg Pro Ala Asp Ala Ala Glu Arg Ala Ala Gln 1160 1165 1170 Ala Pro Leu Ala Ala Ala His Pro Gln Arg Val Gly Ala Pro Gly 1175 1180 1185 Ala Arg Arg Arg Arg Gly Val Arg Arg Gly Ala Pro Pro Arg Pro 1190 1195 1200 Ala Ala Ala Ala Arg Gly Ala Arg Arg Gly Gly Arg Ser Arg Asp 1205 1210 1215 Pro Ala Ala Arg Arg Arg Ala Ala His Ser Gln Val Pro Gly Arg 1220 1225 1230 His Gly Arg Ala Gly Ala His Arg Ala Arg Arg Arg Ala Arg Arg 1235 1240 1245 Val Leu Thr Arg Ala Leu Ala Pro Arg Ala Leu Asp Pro Ala Arg 1250 1255 1260 Ala Arg Tyr Arg Ser Pro Pro Ala Met Cys Ala Asn Ser Thr Ser 1265 1270 1275 Gly Ala Ile Gly Leu Thr Arg Cys Ala Ser His Pro Ala Ser Leu 1280 1285 1290 Asp Arg Arg Thr Ser Ser Cys Trp Pro Tyr Pro Val Asn Ala Arg 1295 1300 1305 Ile Arg Arg Ala Pro Ala Pro Ala Ser Pro Arg Ile Leu Arg Ala 1310 1315 1320 Thr Ser 1325 <210> 166 <211> 1215 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. massiliense <400> 166 Met Ala Ser Thr Ser Ser Gln Gly Ile Val Ser Leu Gly Met Tyr Phe 1 5 10 15 Tyr Arg Val Gly Ser Gly Ala Pro Val Leu Val Thr Asn Thr Asp Ser 20 25 30 Ser Glu Val Ser Gly Met Thr Glu Thr Ile Ser Thr Ala Ala Val Pro 35 40 45 Thr Thr Asp Leu Glu Glu Gln Val Lys Arg Arg Ile Asp Gln Ile Val 50 55 60 Ser Asn Asp Pro Gln Leu Ala Ala Leu Leu Pro Glu Asp Ser Val Thr 65 70 75 80 Glu Ala Val Asn Glu Pro Asp Leu Pro Leu Val Glu Val Val Arg Arg 85 90 95 Leu Leu Glu Gly Tyr Gly Asp Arg Pro Ala Leu Gly Gln Arg Ala Phe 100 105 110 Glu Phe Val Thr Gly Asp Asp Gly Ala Thr Val Ile Ala Leu Lys Pro 115 120 125 Glu Tyr Thr Thr Val Ser Tyr Arg Glu Leu Trp Glu Arg Ala Glu Ala 130 135 140 Ile Ala Ala Ala Trp His Glu Gln Gly Ile Arg Asp Gly Asp Phe Val 145 150 155 160 Ala Gln Leu Gly Phe Thr Ser Thr Asp Phe Ala Ser Leu Asp Val Ala 165 170 175 Gly Leu Arg Leu Gly Thr Val Ser Val Pro Leu Gln Thr Gly Ala Ser 180 185 190 Leu Gln Gln Arg Asn Ala Ile Leu Glu Glu Thr Arg Pro Ala Val Phe 195 200 205 Ala Ala Ser Ile Glu Tyr Leu Asp Ala Ala Val Asp Ser Val Leu Ala 210 215 220 Thr Pro Ser Val Arg Leu Leu Ser Val Phe Asp Tyr His Ala Glu Val 225 230 235 240 Asp Ser Gln Arg Glu Ala Leu Glu Ala Val Arg Ala Arg Leu Glu Ser 245 250 255 Ala Gly Arg Thr Ile Val Val Glu Ala Leu Ala Glu Ala Leu Thr Arg 260 265 270 Gly Arg Asp Leu Pro Ala Ala Pro Leu Pro Ser Ala Asp Pro Asp Ala 275 280 285 Leu Arg Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly 290 295 300 Ala Met Tyr Pro Gln Trp Leu Val Ala Asn Leu Trp Gln Lys Lys Trp 305 310 315 320 Leu Thr Asp Asp Val Ile Pro Ser Ile Gly Val Asn Phe Met Pro Met 325 330 335 Ser His Leu Ala Gly Arg Leu Thr Leu Met Gly Thr Leu Ser Gly Gly 340 345 350 Gly Thr Ala Tyr Tyr Ile Ala Ser Ser Asp Leu Ser Thr Phe Phe Glu 355 360 365 Asp Ile Ala Leu Ile Arg Pro Ser Glu Val Leu Phe Val Pro Arg Val 370 375 380 Val Glu Met Val Phe Gln Arg Phe Gln Ala Glu Leu Asp Arg Ser Leu 385 390 395 400 Ala Pro Gly Glu Ser Asn Ser Glu Ile Ala Glu Arg Ile Lys Val Arg 405 410 415 Ile Arg Glu Glu Asp Phe Gly Gly Arg Val Leu Ser Ala Gly Ser Gly 420 425 430 Ser Ala Pro Leu Ser Pro Glu Met Thr Glu Phe Met Glu Ser Leu Leu 435 440 445 Gln Val Pro Leu Arg Asp Gly Tyr Gly Ser Thr Glu Ala Gly Gly Val 450 455 460 Trp Arg Asp Gly Val Leu Gln Arg Pro Pro Val Thr Asp Tyr Lys Leu 465 470 475 480 Val Asp Val Pro Glu Leu Gly Tyr Phe Thr Thr Asp Ser Pro His Pro 485 490 495 Arg Gly Glu Leu Arg Leu Lys Ser Glu Thr Met Phe Pro Gly Tyr Tyr 500 505 510 Lys Arg Pro Glu Thr Thr Ala Asp Val Phe Asp Asp Glu Gly Tyr Tyr 515 520 525 Lys Thr Gly Asp Val Val Ala Glu Leu Gly Pro Asp His Leu Lys Tyr 530 535 540 Leu Asp Arg Val Lys Asn Val Leu Lys Leu Ala Gln Gly Glu Phe Val 545 550 555 560 Ala Val Ser Lys Leu Glu Ala Ala Tyr Thr Gly Ser Pro Leu Val Arg 565 570 575 Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ser Phe Leu Leu Ala Val 580 585 590 Val Val Pro Thr Pro Glu Val Leu Glu Arg Tyr Ala Asp Ser Pro Asp 595 600 605 Ala Leu Lys Pro Leu Ile Gln Asp Ser Leu Gln Gln Val Ala Lys Asp 610 615 620 Ala Glu Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile Val Glu Thr 625 630 635 640 Val Pro Phe Thr Val Glu Ser Gly Leu Leu Ser Asp Ala Arg Lys Leu 645 650 655 Leu Arg Pro Lys Leu Lys Asp His Tyr Gly Glu Arg Leu Glu Ala Leu 660 665 670 Tyr Ala Glu Leu Ala Glu Ser Gln Asn Glu Arg Leu Arg Gln Leu Ala 675 680 685 Arg Glu Ala Ala Thr Arg Pro Val Leu Glu Thr Val Thr Asp Ala Ala 690 695 700 Ala Ala Leu Leu Gly Ala Ser Ser Ser Asp Leu Ala Pro Asp Val Arg 705 710 715 720 Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Tyr Ser Glu 725 730 735 Leu Leu Arg Asp Ile Phe Glu Val Asp Val Pro Val Gly Val Ile Asn 740 745 750 Ser Val Ala Asn Asp Leu Ala Ala Ile Ala Arg His Ile Glu Ala Gln 755 760 765 Arg Thr Gly Thr Ala Thr Gln Pro Thr Phe Ala Ser Val His Gly Lys 770 775 780 Asp Ala Thr Val Ile Thr Ala Gly Glu Leu Thr Leu Asp Lys Phe Leu 785 790 795 800 Asp Glu Ser Leu Leu Lys Ala Ala Lys Asp Ile Gln Pro Val Thr Ala 805 810 815 Asp Val Lys Thr Val Leu Val Thr Gly Gly Asn Gly Trp Leu Gly Arg 820 825 830 Trp Leu Val Leu Asp Trp Leu Glu Arg Leu Ala Pro Asn Gly Gly Lys 835 840 845 Val Tyr Ala Leu Ile Arg Gly Ala Asp Ala Glu Ala Ala Arg Ala Arg 850 855 860 Leu Asp Ala Ala Tyr Glu Ser Gly Asp Pro Lys Leu Ser Ala His Tyr 865 870 875 880 Arg Gln Leu Ala Gln Gln Ser Leu Glu Val Ile Ala Gly Asp Phe Gly 885 890 895 Asp Gln Asp Leu Gly Leu Ser Gln Glu Val Trp Gln Lys Leu Ala Lys 900 905 910 Asp Val Asp Leu Ile Val His Ser Gly Ala Leu Val Asn His Val Leu 915 920 925 Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val Ala Gly Thr Ala Glu Ile 930 935 940 Ile Lys Leu Ala Ile Ser Glu Arg Leu Lys Pro Val Thr Tyr Leu Ser 945 950 955 960 Thr Val Gly Ile Ala Asp Gln Ile Pro Val Thr Glu Phe Glu Glu Asp 965 970 975 Ser Asp Val Arg Val Met Ser Ala Glu Arg Gln Ile Asn Asp Gly Tyr 980 985 990 Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 995 1000 1005 Glu Ala His Asp Leu Ala Gly Leu Pro Val Arg Val Phe Arg Ser 1010 1015 1020 Asp Met Ile Leu Ala His Ser Asp Tyr His Gly Gln Leu Asn Val 1025 1030 1035 Thr Asp Val Phe Thr Arg Ser Ile Gln Ser Leu Leu Leu Thr Gly 1040 1045 1050 Val Ala Pro Ala Ser Phe Tyr Glu Leu Asp Ala Asp Gly Asn Arg 1055 1060 1065 Gln Arg Ala His Tyr Asp Gly Val Pro Gly Asp Phe Thr Ala Ala 1070 1075 1080 Ser Ile Thr Ala Ile Gly Gly Val Asn Val Ile Asp Gly Tyr Arg 1085 1090 1095 Ser Phe Asp Val Phe Asn Pro His His Asp Gly Val Ser Met Asp 1100 1105 1110 Thr Phe Val Asp Trp Leu Ile Asp Ala Gly Tyr Lys Ile Thr Arg 1115 1120 1125 Ile Asp Asp Tyr Asp Gln Trp Leu Ala Arg Phe Glu Leu Ala Leu 1130 1135 1140 Lys Gly Leu Pro Glu Gln Gln Arg Gln Gln Ser Val Leu Pro Leu 1145 1150 1155 Leu Lys Met Tyr Glu Lys Pro Gln Pro Ala Ile Asp Gly Ser Ala 1160 1165 1170 Leu Pro Thr Ala Glu Phe Ser Arg Ala Val His Glu Ala Lys Val 1175 1180 1185 Gly Asp Gly Gly Glu Ile Pro His Val Thr Lys Glu Leu Ile Leu 1190 1195 1200 Lys Tyr Ala Ser Asp Ile Gln Leu Leu Gly Leu Val 1205 1210 1215 <210> 167 <211> 1088 <212> PRT <213> Artificial Sequence <220> <223> Curtobacterium sp. MCSS17_007 <400> 167 Met Ala Asp Val Phe Ala Arg Phe Gly Asp Arg Pro Ala Val Gly Glu 1 5 10 15 Arg Ala Arg Glu Tyr Val Arg Asp Asp Arg Thr Gly Arg Val Ser Ala 20 25 30 Arg Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Arg Glu Leu Trp Gly 35 40 45 Arg Val Gly Ala Val Ala Ala Glu Trp His His His Pro Glu His Pro 50 55 60 Leu Ala Ala Gly Asp Arg Val Ala Leu Leu Gly Phe Thr Ser Arg Asp 65 70 75 80 Tyr Ala Thr Leu Lys Leu Thr Cys Gly Tyr Leu Gly Ala Val Ser Val 85 90 95 Pro Leu Gln Thr Ser Ala Ser Pro Ala Asn Leu Ala Ala Ile Leu Ser 100 105 110 Glu Thr Glu Pro Val Leu Leu Ala Thr Ala Ile Asp Arg Leu Asp Val 115 120 125 Ala Ala Glu Leu Ala Arg Gly Ser Ser Ser Ile Arg Arg Val Val Val 130 135 140 Phe Asp Tyr Asp Pro Arg Asp Asp Asp Gln Ala Asp Arg Phe Ala Ala 145 150 155 160 Ala Arg Asp Val Gly Ala Val Ala Leu Ser Asp Leu Leu Asp Leu Gly 165 170 175 Ala Thr Leu Pro Glu Ala Pro Pro Tyr Val Pro Gly Asp Asp Glu Asp 180 185 190 Pro Leu Ala Met Leu Val Tyr Thr Ser Gly Ser Ser Gly Thr Pro Lys 195 200 205 Gly Ala Met Tyr Pro Glu Trp Leu Ala Arg Val Met Trp Glu Asp Arg 210 215 220 Ala Arg Arg Thr Pro Asp Gly Gly Leu Ser Thr Val His Tyr Met Pro 225 230 235 240 Leu Ser His Ile Gly Gly His Phe Thr Leu Met Asn Thr Leu Ala Arg 245 250 255 Gly Gly Leu Ser Cys Phe Thr Ala Ala Ala Asp Leu Ser Thr Leu Phe 260 265 270 Glu Asp Leu Ala Leu Val Arg Pro Thr Glu Val Ser Leu Val Pro Arg 275 280 285 Val Cys Glu Met Leu His Gln Arg Tyr Arg Gly Glu Pro Asp Glu Arg 290 295 300 Ala Arg Ala Glu Ala Leu Gly Gly Arg Val Thr Phe Ala Thr Cys Gly 305 310 315 320 Ser Ala Pro Leu Ser Ala Ala Leu Thr Asp Phe Met Glu Thr Leu Leu 325 330 335 Gly Val Pro Leu Tyr Asp Met Tyr Gly Ser Thr Glu Val Ala Gly Ile 340 345 350 Ala Val Asn Gly Ile Leu Met Asn Pro Pro Val Leu Asp Tyr Arg Leu 355 360 365 Val Asp Val Pro Glu Leu Gly Tyr Phe Gly Thr Asp Val Pro His Pro 370 375 380 Arg Gly Glu Leu Leu Leu Arg Ala Thr Gly Val Pro Gly Tyr Tyr Arg 385 390 395 400 His Pro Glu Leu Thr Ala Glu Leu Phe Asp Ala Asp Gly Tyr Tyr Arg 405 410 415 Thr Gly Asp Ile Val Ala Glu Leu Gly Pro Arg Arg Ile Ala Phe Val 420 425 430 Asp Arg Arg Thr Ser Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala 435 440 445 Thr Ser Arg Val Glu Ser Val Leu Gly Ala Gly Pro Leu Val Arg Gln 450 455 460 Ile Phe Val Tyr Gly Asp Ser Gly Arg Ser His Leu Leu Ala Val Val 465 470 475 480 Val Pro Thr Pro Glu Ala Leu Ala Ala His Gly Asp Asp Pro Ala Arg 485 490 495 Leu Asp Gln Leu Leu Gly Glu Ser Leu Arg Arg Val Ala Arg Asp Ala 500 505 510 Gly Leu Asn Ser Tyr Glu Ile Pro Arg Gly Gln Leu Ile Glu Thr Glu 515 520 525 Pro Phe Ser His Arg Asn Gly Leu Leu Ser Asp Asn Arg Lys Leu Leu 530 535 540 Arg Pro Arg Leu Val Glu Arg Tyr Arg Ala Glu Leu Asp Gln Leu Tyr 545 550 555 560 Asp Arg Ile Ala Ala Arg Ala Glu Gln Glu Leu Leu Asp Leu Arg Arg 565 570 575 Thr Gly Gly Asp Arg Pro Ala Leu Glu Thr Val Gln Arg Ala Val Arg 580 585 590 Ala Leu Leu Gly Gly Thr Ala Ala Glu Met Arg Pro Asp Thr Cys Phe 595 600 605 Arg Asp Leu Gly Gly Asp Ser Leu Ser Ala Val Thr Leu Ala Asn Leu 610 615 620 Leu Tyr Asp Ile Phe Ala Val Pro Val Pro Val Asp Val Val Leu Arg 625 630 635 640 Pro Gly His Asp Leu Arg Gln Leu Ala Gly Phe Ile Glu Ser Lys Arg 645 650 655 Asp Gly Thr Thr Gly Arg Pro Thr Phe Gly Ser Val His Gly Ala Gly 660 665 670 Ala Ala Gln Ala Tyr Ala Arg Asp Leu Thr Leu Asp Arg Phe Leu Asp 675 680 685 Ala Gly Ile Arg Glu Thr Ala Ala Arg Leu Pro Gly Pro Val Gly Ala 690 695 700 Pro Arg Cys Val Leu Leu Thr Gly Ala Ala Gly Tyr Leu Gly Arg Phe 705 710 715 720 Leu Ala Leu Glu Trp Leu Arg Arg Leu Ala Pro Asp Gly Gly Arg Leu 725 730 735 Ile Ala Val Val Arg Gly Arg Asp Ala Glu Ala Ala Gly Gln Arg Leu 740 745 750 Ala Asp Ala Phe Ala Gly Ala Asp Pro Glu Pro Glu Ala Ala Lys His 755 760 765 Leu Glu Val Val Ala Gly Asp Leu Ala Glu Pro Arg Leu Gly Leu Asp 770 775 780 Glu Thr Thr Trp Ala Arg Leu Ala Ser Glu Val Asp Leu Ile Val His 785 790 795 800 Ala Gly Ala Leu Val Asn His Val Leu Pro Tyr Pro His Leu Phe Glu 805 810 815 Ala Asn Val Ala Gly Thr Ala Glu Val Ile Arg Leu Ala Leu Thr Thr 820 825 830 Arg Met Lys Pro Val Thr Tyr Val Ser Ser Val Ala Val Ala Ala Ala 835 840 845 Pro Leu Ala Ala Gly Thr Gly Pro Pro Leu Asp Glu Asp Ala Asp Val 850 855 860 Arg Val Ala Leu Pro Val Gln Pro Val Asp Gly Gly Tyr Ala Ser Gly 865 870 875 880 Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 885 890 895 Asp Arg Phe Ala Leu Pro Val Thr Val Phe Arg Ala Ser Met Leu Leu 900 905 910 Ala His Arg Arg Tyr Ala Gly Gln Leu Asn Ala Gly Asp Leu Phe Ser 915 920 925 Arg Leu Val Phe Ser Val Leu Ala Thr Gly Met Ala Pro Glu Ser Phe 930 935 940 Tyr Gln Pro Gly Arg Ala His Tyr Asp Gly Leu Pro Val Asp Phe Thr 945 950 955 960 Ala Ala Ala Ile Val Gly Leu Gly Ser Gly Ala Pro Gly Phe Arg Thr 965 970 975 Arg His Val Val Asn Pro His Asp Asp Gly Ile Ser Leu Asp Thr Val 980 985 990 Val Thr Trp Leu Ile Glu Asp Gly Arg Arg Ile Glu Arg Ile Pro Glu 995 1000 1005 His Ala Asp Trp Leu Ala Arg Val Glu Ala Ala Leu Arg Ala Leu 1010 1015 1020 Pro Glu Thr His Arg Gln His Ser Val Leu Pro Leu Leu His Ala 1025 1030 1035 Phe Arg Glu Pro Glu Pro Ala Val Pro Gly Ser Ala Leu Pro Ser 1040 1045 1050 Glu Arg Phe Arg Ala Val Ala Gly Glu Ile Pro His Leu Thr Ser 1055 1060 1065 Asp Leu Ile Arg Arg Tyr Ala Thr Asp Leu His Asp Arg Thr Gly 1070 1075 1080 Gly Pro Trp Thr Arg 1085 <210> 168 <211> 1165 <212> PRT <213> Artificial Sequence <220> <223> Nocardia brasiliensis ATCC 700358 <400> 168 Met Thr Asp Val Glu Val Ala Arg Arg Ile Asn Asp Leu Ser Ala Thr 1 5 10 15 Asp Glu Val Leu Ala Gly Ala Leu Pro Asp Pro Ala Val Asp Ala Arg 20 25 30 Ile Gln Asp Pro Ala Val Gly Leu Ala Glu Leu Ile Arg Ile Val Phe 35 40 45 Ala Ala Tyr Gly Asp Arg Pro Ala Val Gly Ala Arg Ala Thr Arg Leu 50 55 60 Val Thr Asp Pro Val Thr Gly Arg Thr Thr Leu His Val Leu Pro Glu 65 70 75 80 Tyr Glu Thr Thr Thr Tyr Ala Glu Leu Gly Gln Gln Val Ala Ala Val 85 90 95 Ala Ala Gly Leu Arg Gly Asp Ala Ala Asp Gly Gly Trp Val Arg Leu 100 105 110 Gly Glu His Val Ala Met Leu Gly Phe Thr Ser Val Glu Tyr Thr Val 115 120 125 Leu Asp Leu Ala Ala Thr Leu Ala Gly Ala Val Ala Val Pro Met Gln 130 135 140 Ser Asn Ala Pro Ala Ala Gln Leu Arg Pro Ile Leu Ala Glu Thr Gln 145 150 155 160 Pro Arg Val Leu Ala Ala Gly Val Asp Gln Leu Ala Glu Ala Leu Asp 165 170 175 Leu Ala Asp Gly Glu His Arg Pro Gly Leu Ile Val Val Leu Asp His 180 185 190 Arg Pro Glu Val Asp Ala His Arg Glu Ala Phe Asp Glu Ala Ala Ala 195 200 205 Arg Leu Ser Gly Thr Gly Val Ala Leu Lys Thr Leu Ala Glu Leu Ala 210 215 220 Asp Ser Gly Lys Asp Gly Val Val Ala Pro Glu Pro Ala Asp Ser Glu 225 230 235 240 Arg Ile Val Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys 245 250 255 Gly Ala Met Tyr Ser Glu Arg Leu Val Ala Asn Leu Trp Gln Gly Lys 260 265 270 Phe Gly Leu Ala Glu Gly Pro His Ala Ala Gly Pro Trp Ile Thr Leu 275 280 285 Asn Phe Met Pro Met Ser His Leu Met Gly Arg Tyr Thr Leu Tyr Gly 290 295 300 Thr Leu Ala Arg Gly Gly Ile Ala Tyr Phe Ala Ala Ser Ser Asp Leu 305 310 315 320 Ser Thr Phe Leu Glu Asp Leu Ser Leu Val Arg Pro Thr Gln Leu Gln 325 330 335 Phe Val Pro Arg Val Trp Asp Leu Leu Tyr Gln Glu Tyr Gln Arg Ala 340 345 350 Leu Asp Gly Val Asp Pro Ala Glu Arg Ser Gly Arg Thr Pro Glu Leu 355 360 365 Leu Ala Glu Met Arg Arg Asp Leu Leu Gly Gly Arg Val Leu Gly Ala 370 375 380 Val Thr Gly Ser Ala Pro Ile Ser Val Glu Val Arg Glu Phe Val Asp 385 390 395 400 Ala Leu Leu Gly Phe His Leu Pro Asp Gly Tyr Gly Ser Thr Glu Ala 405 410 415 Gly Gly Ile Thr Val Asp Gly Lys Val Val Arg Pro Pro Val Leu Asp 420 425 430 Tyr Lys Leu Ala Asp Val Pro Glu Leu Gly Tyr Tyr Ser Thr Asp Arg 435 440 445 Pro His Pro Arg Gly Glu Leu Leu Val Lys Thr Gln Asn Ile Phe Pro 450 455 460 Gly Tyr Tyr Arg Arg Pro Glu Val Thr Ala Glu Val Phe Asp Pro Asp 465 470 475 480 Gly Tyr Tyr Arg Thr Gly Asp Ile Val Ala Glu Val Gln Pro Asp Glu 485 490 495 Leu His Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly 500 505 510 Glu Phe Val Thr Val Ser Lys Leu Glu Ala Ala Phe Gly Ala Ser Pro 515 520 525 Leu Ile Gln Gln Ile Tyr Ile Tyr Gly Asn Ser Ser Arg Pro Tyr Leu 530 535 540 Leu Ala Val Ile Val Pro Asp Asp Ala Val Leu Glu Arg Val Ser Gly 545 550 555 560 Asp Val Gly Ala Val Gly Pro Leu Leu Thr Glu Ala Leu Arg Ala Val 565 570 575 Ala Ala Asp Ala Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Leu 580 585 590 Val Glu Thr Ser Pro Phe Thr Val Glu Asn Gly Leu Leu Thr Gly Ile 595 600 605 Arg Lys Leu Ala Arg Pro Lys Leu Arg Gln Arg Tyr Gly Glu Leu Leu 610 615 620 Glu Gln Leu Tyr Gln Arg Leu Ser Asp Gly Gln Ala Glu Glu Leu Arg 625 630 635 640 Ala Leu Arg Val Gly Ala Ala Asp Arg Pro Val Leu Glu Thr Val Ser 645 650 655 Arg Val Ala Ala Ala Leu Leu Gly Ile Ala Ala Ala Asp Val His Pro 660 665 670 Ala Ala His Phe Thr Glu Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Gly Asn Ala Leu His Asp Ile Leu Gly Val Glu Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Thr Asp Leu Arg Ala Leu Ala Thr Phe Leu 705 710 715 720 Glu Ser Gly Ala Gln Thr Ser Arg Pro Thr Phe Ala Thr Val His Gly 725 730 735 Pro Asp Ala Thr Glu Val Arg Ala Ala Asp Leu Thr Leu Glu Lys Phe 740 745 750 Leu Asp Ala Ala Thr Leu Asp Gly Ala Ala Ala Leu Pro Ala Pro Asn 755 760 765 Tyr Ala Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly 770 775 780 Arg Phe Leu Ala Leu Ala Leu Leu Glu Arg Leu Gly Pro Val Asp Gly 785 790 795 800 Thr Leu Ile Cys Leu Val Arg Ala Thr Asp Asp Thr Ala Ala Arg Gln 805 810 815 Arg Leu Asp Glu Val Phe Asp Ser Gly Asp Pro Gln Leu Leu Thr His 820 825 830 Tyr Arg Arg Leu Ala Glu Arg His Leu Glu Val Val Ala Gly Asp Lys 835 840 845 Gly Glu Leu Asp Leu Gly Leu Asp Arg Gly Thr Trp Gln Gln Leu Ala 850 855 860 Glu Arg Val Asp Leu Ile Val Asp Cys Ala Ala Leu Val Asn His Val 865 870 875 880 Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu 885 890 895 Leu Ile Arg Leu Ala Leu Thr Gly Lys Gln Lys Ile Phe Asp Tyr Ile 900 905 910 Ser Thr Val Gly Val Gly Asp Gln Ile Ala Ala Gly Gln Phe Val Glu 915 920 925 Asp Ala Asp Ile Arg Thr Ile Ser Ala Thr Arg Ser Val Asp Glu Arg 930 935 940 Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu 945 950 955 960 Arg Glu Ala Asn Glu Arg Tyr Gly Leu Pro Val Ser Val Phe Arg Cys 965 970 975 Asp Met Ile Met Val Asp Gly Ser Tyr Val Gly Gln Leu Asn Val Pro 980 985 990 Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr Gly Val Ala 995 1000 1005 Pro Gly Ser Phe Tyr Gln Thr Asp Ala Ala Gly Gln Arg Gln Arg 1010 1015 1020 Ala His Tyr Asp Gly Leu Pro Val Asp Phe Ile Ala Glu Ala Val 1025 1030 1035 Thr Glu Leu Gly Val His Glu Gly Phe Ser Thr Tyr His Val Met 1040 1045 1050 Asn Pro His His Asp Gly Ile Gly Leu Asp Glu Phe Val Asp Trp 1055 1060 1065 Leu Val Ala Ala Gly Tyr Pro Ile Thr Arg Val Ala Asp Tyr Gln 1070 1075 1080 Thr Trp Leu Glu Gln Phe Gly Thr Lys Leu Arg Ala Leu Pro Glu 1085 1090 1095 Gln Gln Arg Arg His Ser Leu Leu Pro Leu Leu His Ser Tyr Ala 1100 1105 1110 His Pro Gln Pro Pro Val Glu Gly Ser Val Ala Pro Ala Asp Arg 1115 1120 1125 Phe Arg Ala Ala Val Gln Asp Ala Asn Ile Gly Pro Asp Lys Asp 1130 1135 1140 Ile Pro His Leu Thr Glu Ser Thr Ile Leu Lys Tyr Ile Thr Asn 1145 1150 1155 Leu Glu His Leu Gly Leu Leu 1160 1165 <210> 169 <211> 1064 <212> PRT <213> Artificial Sequence <220> <223> Allokutzneria albata <400> 169 Met Thr Thr Ala Thr Gly Pro Arg Pro Asp Ile Thr Ala Ala Ile Thr 1 5 10 15 Arg Pro Gly Val Arg Val Gln Glu Ile Leu Arg Thr Val Leu Asp Gly 20 25 30 Tyr Ser Asp Arg Pro Ala Leu Gly Glu Arg Glu Thr Val Leu Arg Thr 35 40 45 Asp Pro Val Thr Gly Arg Arg Thr Arg Glu Leu Leu Pro Gly Phe Arg 50 55 60 Thr Ile Ser Tyr Gly Glu Leu Arg Ala Arg Ile Glu Ala Val Ala Ala 65 70 75 80 Asp Leu Arg Leu Gln Ser Gly Asp Val Val Gly Leu Leu Gly Phe Thr 85 90 95 Ser Leu Asp His Thr Thr Val Asp Leu Ala Cys Val His Leu Gly Ala 100 105 110 Val Cys Val Pro Leu Gln Ser Ser Ala Ser Ala Ala Gln Leu Lys Pro 115 120 125 Val Ile Ala Glu Ile Glu Pro Arg Leu Leu Ala Thr Ser Leu Gln Leu 130 135 140 Leu Asp Thr Ala Val Glu Val Ala Leu Ser Ser Thr Ser Val Gln Trp 145 150 155 160 Ile Val Val Phe Asp Tyr His Glu Asp Asp Asp Asp Glu Arg Glu Ile 165 170 175 Phe Leu Ala Ala Gln Glu Arg Phe Ala Val Glu Ser Leu Thr Asp Val 180 185 190 Leu Glu Arg Gly Ala Ala Leu Pro Ala Pro Pro Ala His Val Pro Arg 195 200 205 Pro Asp Glu Asp Pro Leu Ser Leu Leu Val Tyr Thr Ser Gly Ser Thr 210 215 220 Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Arg Leu Leu Arg Arg Leu 225 230 235 240 Trp Leu Gly Tyr Leu Pro Pro Ile Pro Asp Leu Ser Val Ile Arg Val 245 250 255 His Tyr Met Pro Met Ser His Leu Thr Gly Arg Ala Ala Val Ile Glu 260 265 270 Thr Leu Val Ala Gly Gly Ile Gly Tyr Phe Thr Ala Arg Ser Asp Leu 275 280 285 Ser Thr Leu Phe Glu Asp Ile Ala Leu Ala Arg Pro Thr Glu Leu Phe 290 295 300 Leu Ile Pro Arg Leu Ser Asp Met Leu Phe Gln Arg Tyr Gln Arg Glu 305 310 315 320 Leu Asp Arg Gly Val Pro Glu Ala Glu Ala Met Ala Val Ile Arg Glu 325 330 335 Ala Val Leu Gly Gly Arg Val Glu Arg Ser Ala Thr Gly Ser Ala Pro 340 345 350 Leu Ser Ala Glu Leu Ala Ala Phe Val Gln Asn Cys Leu Gly Val Arg 355 360 365 Leu His Asp Gly Tyr Gly Ser Thr Glu Thr Gly Arg Val Phe Val Asp 370 375 380 Gly Lys Val Thr Arg Pro Pro Val Ile Asp Tyr Lys Val Val Asp Val 385 390 395 400 Pro Glu Leu Gly Tyr Phe Arg Thr Asp Ala Pro His Pro Arg Gly Glu 405 410 415 Leu Leu Val Arg Thr Glu Ala Met Ile Ser Gly Tyr Tyr Lys Arg Pro 420 425 430 Asp Leu Asn Ala Glu Val Phe Asp Glu Asp Gly Phe Tyr Arg Thr Gly 435 440 445 Asp Ile Val Ala Glu Pro Gly Pro Asp Gln Leu Val Tyr Leu Asp Arg 450 455 460 Arg Lys Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ser 465 470 475 480 Arg Val Glu Ala Ala Leu Gly Ala Ser Pro Leu Val Arg Gln Ile Phe 485 490 495 Val Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala Val Val Val Pro 500 505 510 Thr Gly Ala His Arg Lys Glu Arg Ile Ser Glu Ser Phe His His Ile 515 520 525 Ala Arg Glu Ala Gly Leu Ser Ser Tyr Glu Ile Pro Arg Glu Phe Ile 530 535 540 Val Glu Thr Glu Pro Phe Ser Thr Ala Asn Gly Leu Leu Ser Asp Leu 545 550 555 560 Asn Lys Pro Leu Arg Pro Ala Leu Arg Glu Arg Tyr Gly Pro Arg Leu 565 570 575 Glu Gln Leu Tyr Val Glu Leu Ala Glu Arg Glu Ala Asp Glu Leu Arg 580 585 590 Ala Leu Arg Ala Ala Gly Ala Asp Gln Pro Val Leu Pro Ala Ile Arg 595 600 605 Ser Ala Ala Arg Ala Leu Leu Gly Ser Ala Asp Ala Asp Ala Arg Phe 610 615 620 Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Met Ala Asn Leu 625 630 635 640 Leu Arg Asp Ile Phe Asp Val Asp Val Pro Val Ser Leu Ile Ile Ser 645 650 655 Pro Ala Thr Thr Leu Arg Gly Leu Ala Asp His Ile Glu Arg Ala Pro 660 665 670 Arg Ala Ala Arg Gly Pro Lys Thr Ser Val Arg Ala Ala Asp Leu Thr 675 680 685 Leu Asp Lys Phe Val Arg Pro Thr Pro Asn Thr Ile Gly Thr Val Leu 690 695 700 Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Val Cys Leu Glu Trp 705 710 715 720 Leu Gln Arg Leu Ala Ala Thr Gly Gly Lys Leu Ile Cys Leu Val Arg 725 730 735 Gly Gly Ser Thr Arg Leu Glu Glu Ala Phe Gly Asp Ser Ala Leu Leu 740 745 750 Arg Arg Phe Arg Glu Leu Ser Gly His Val Glu Val Val Ser Gly Asp 755 760 765 Leu Ser Glu Pro Asp Leu Gly Leu Pro Arg Arg Thr Trp Asp Arg Leu 770 775 780 Ala Glu Thr Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His 785 790 795 800 Val Leu Pro Tyr Glu Glu Leu Phe Gly Pro Asn Val Val Gly Val Ala 805 810 815 Glu Leu Ile Lys Leu Ala Ile Thr Lys Arg Arg Lys Gly Phe Thr Phe 820 825 830 Leu Ser Ser Ile Ala Val Ala Glu Gly Glu Asp Thr Asp Val Arg Arg 835 840 845 Ala Ser Pro Val Arg Ala Leu Asp Gly Ser Tyr Ala Asn Gly Tyr Ala 850 855 860 Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Glu Arg 865 870 875 880 Tyr Arg Leu Pro Val Val Val Leu Arg Ser Asp Met Ile Leu Ala His 885 890 895 Ser Thr Cys Thr Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg Leu 900 905 910 Leu Phe Ser Leu Ile Ala Thr Gly Ile Ala Pro Arg Ser Phe Tyr Arg 915 920 925 Ser Asp Ala Glu His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Arg 930 935 940 Val Val Ala Asp Leu Gly Ala Pro Ser Glu Gly Tyr Arg Thr Phe Asn 945 950 955 960 Val Val Asn Pro His Glu Asp Gly Ile Ser Leu Asp Thr Phe Val Asp 965 970 975 Trp Leu Ile Glu Ala Gly His Arg Ile His Arg Ile Asp Asp His Ala 980 985 990 Glu Trp Ser Arg Arg Phe Glu Met Ala Leu Arg Ala Leu Pro Glu Lys 995 1000 1005 Gln Arg Lys His Ser Met Leu Pro Leu Leu His Ala Val Ala Ala 1010 1015 1020 Pro Val Glu Pro Gly Pro Leu Val Pro Ser Glu Arg Phe Gln Ala 1025 1030 1035 Ala Val Gly Glu Ile Pro Gln Val Ser Arg Glu Leu Ile Val Lys 1040 1045 1050 Tyr Ala Asp Asp Leu Arg Ser Leu Gly Leu Leu 1055 1060 <210> 170 <211> 1164 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium vanbaalenii PYR-1 <400> 170 Met Glu Arg Lys Ala Glu Val Leu Ala Ala Arg Arg Val Glu Asp Leu 1 5 10 15 Ile Glu Arg Asp Ala Gln Val Arg Ala Ala Ile Pro Asp Pro Val Val 20 25 30 Thr Ala Glu Leu Glu Arg Ala Asp Gly Ser Leu Ala Gln Thr Val Ala 35 40 45 Arg Val Met Ala Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg Ala 50 55 60 Val Glu Phe Val Pro Asp Glu Asn Gly Cys Arg Arg Thr Arg Leu Leu 65 70 75 80 Pro Trp Phe Asp Thr Ile Thr Phe Gly Glu Leu Trp Gln Arg Val Gly 85 90 95 Thr Val Ala Ala Val Trp Gln Ser Arg Ala Glu Arg Ser Val Arg Ala 100 105 110 Gly Asp Phe Val Ala Val Leu Gly Ser Thr Gly Ile Asp Tyr Thr Val 115 120 125 Val Asp Leu Ala Cys Thr Tyr Ser Gly Ala Val Pro Val Pro Leu Gln 130 135 140 Ala Gly Ala Ser Pro Thr Gln Leu Ala Pro Ile Val Arg Glu Val Glu 145 150 155 160 Pro Lys Val Leu Ala Thr Asp Val Gly Gln Leu Glu Val Ala Val Asp 165 170 175 Leu Ala Ser Ala Gly Asp Ser Val Arg Ser Leu Leu Ile Phe Gly Leu 180 185 190 Tyr Ala Glu Asp Asp Glu His Cys Ala Ala Val Glu Ser Ala Arg Arg 195 200 205 Arg Leu Ala Asp Thr Pro Val Val Val Glu Thr Ile Val Glu Leu Leu 210 215 220 Ala Ser Gly Gln Asp Arg Pro Ala Ala Ser Leu His Ala Ser Ala Asp 225 230 235 240 Pro Asp Glu Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr 245 250 255 Pro Lys Gly Ala Met Tyr Thr Gln Arg Leu Leu Thr Asn Ala Trp Cys 260 265 270 Ala Ala Gly Ala Ser Pro Met Pro Ser Ile Ala Leu Ser Tyr Leu Pro 275 280 285 Met Ser His Thr Met Ala Arg Gln Leu Leu Leu Thr Gly Leu Ala Arg 290 295 300 Gly Gly Thr Val Tyr Phe Ala Ala Arg Asn Asp Met Ser Thr Leu Phe 305 310 315 320 Asp Asp Phe Ala Leu Ala Arg Pro Thr Leu Leu Gly Phe Val Pro Arg 325 330 335 Val Cys Asp Met Val Leu Gln Arg Phe Gln Ser Glu Met Ala Arg Arg 340 345 350 Val Gly Ala Asp Asp Glu Pro Thr Val Val Glu Gln Glu Val Lys Thr 355 360 365 Glu Leu Arg Glu Gln Phe Leu Gly Gly Arg Phe Leu Val Ala Ser Ile 370 375 380 Gly Ser Ala Pro Leu Ser Ala Asp Met Arg Glu Phe Met Gln Ser Val 385 390 395 400 Leu Gly Ile Ala Leu Ile Asp Ala Tyr Gly Ser Thr Glu Thr Gly Gly 405 410 415 Val Leu Met Asn Asn Lys Val Val Arg Thr Ala Ile Leu Asp Tyr Lys 420 425 430 Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Arg Pro His 435 440 445 Pro Arg Gly Glu Leu Leu Ile Lys Ser Arg Thr Leu Ile Pro Gly Tyr 450 455 460 Tyr Lys Arg Pro Glu Leu Asn Ser Gln Phe Phe Asp Ala Glu Gly Phe 465 470 475 480 Tyr Arg Thr Gly Asp Val Met Ala Gln Thr Gly Phe Asp Glu Leu Val 485 490 495 Tyr Val Asp Arg Arg Asn Ser Val Leu Lys Leu Ser Gln Gly Glu Phe 500 505 510 Val Ala Val Ser Lys Leu Glu Ala Ile Phe Val Gly Ser Pro Leu Val 515 520 525 Glu Gln Ile Tyr Val Tyr Gly Ser Ser Glu Arg Ala Tyr Leu Leu Ala 530 535 540 Val Ile Val Pro Val Ala Glu Ala Ile Ala Thr His Ala Gly Thr Ala 545 550 555 560 Glu Leu Lys Ala Ala Ile Ser Glu Ser Leu Arg Gln Ile Ala Lys Asp 565 570 575 Ala Glu Leu Ser Ser Tyr Glu Val Pro Arg Asp Phe Leu Leu Glu Ser 580 585 590 Glu Pro Phe Thr Val Asp Asn Gly Leu Leu Ala Gly Leu Ser Lys Leu 595 600 605 Leu Arg Pro Ser Leu Lys Glu Arg Tyr Gly Glu Arg Leu Glu Ala Leu 610 615 620 Tyr Arg Val Ala Glu Ala Ala Gln Thr Gln Glu Leu Ala Ala Leu Arg 625 630 635 640 Gln Gln Ala Gly Met Leu Pro Val Leu Glu Thr Val Ser Arg Ala Ala 645 650 655 Gln Ala Val Leu Gly Val Ser Ala Ala Glu Leu Arg Pro Asp Ala His 660 665 670 Phe Thr Asp Leu Gly Gly Asp Ser Leu Ala Ala Leu Ser Phe Ser Thr 675 680 685 Leu Leu Gln Glu Leu Leu Gly Val Gln Val Pro Val Gly Val Ile Ala 690 695 700 Ser Ser Ala Asn Asp Leu Arg Arg Ile Ala Asn Tyr Ala Val Ala Glu 705 710 715 720 Arg Ser Ala Gly Ser Leu Arg Pro Thr Ser Thr Gly Val His Gly Thr 725 730 735 Gly Ser Gln Leu Arg Ala Ile Asp Leu Arg Leu Asp Lys Phe Ile Asp 740 745 750 Pro Ser Thr Leu Ala Ala Ala Thr Thr Leu Pro Arg Ala Gly Glu Pro 755 760 765 Arg Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu 770 775 780 Cys Leu Glu Trp Leu Gln Arg Leu His His Ser Gly Gly Thr Leu Ile 785 790 795 800 Cys Val Val Arg Gly Ile Asp Ala Val Ala Ala Arg Glu Arg Leu Asp 805 810 815 Glu Val Phe Asp Ser Gly Asp Pro Glu Leu Leu His Arg Tyr Arg Glu 820 825 830 Leu Ala Glu Gly Thr Leu Glu Val Leu Cys Gly Asp Ile Ser Glu Pro 835 840 845 Gly Leu Gly Leu Ser Glu Arg Asp Trp Arg Arg Leu Ala Asp Thr Val 850 855 860 Glu Leu Ile Val His Ala Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Gly Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Arg 885 890 895 Leu Ala Met Thr Thr Arg Ile Lys Pro Val Thr Tyr Leu Ser Thr Val 900 905 910 Ala Val Ala Ala Gln Val Ala Pro Glu Gln Phe Thr Glu Asp Gly Asp 915 920 925 Ile Arg Glu Ile Ser Ala Val Arg Ser Leu Asp Glu Gly Tyr Ala Asp 930 935 940 Gly Tyr Gly Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala 945 950 955 960 Tyr Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile 965 970 975 Leu Ala His Ser Arg Phe Ala Gly Gln Leu Asn Val Ser Asp Met Phe 980 985 990 Thr Arg Leu Val Leu Ser Val Leu Ala Thr Gly Val Ala Pro Lys Ser 995 1000 1005 Phe Tyr Glu Thr Asp Arg Met Gly Asn Arg Gln Arg Ala His Tyr 1010 1015 1020 Asp Gly Leu Pro Val Asp Phe Thr Ala Gln Ala Ile Thr Val Leu 1025 1030 1035 Gly Ser Gln Val Val Ser Gly Phe Glu Thr Phe Asp Val Leu Asn 1040 1045 1050 Pro His Asp Asp Gly Leu Ser Leu Asp Glu Phe Val Asp Trp Leu 1055 1060 1065 Ile Ala Ala Gly His Ser Ile Asp Arg Ile Asp Gly Tyr Ala Glu 1070 1075 1080 Trp Leu Ser Arg Phe Gly Thr Ala Leu Arg Val Leu Ser Glu Arg 1085 1090 1095 Gln Arg Gln His Ser Val Leu Pro Leu Leu His Ala Tyr Arg Arg 1100 1105 1110 Ala Ala Val Pro Ile Pro Gly Ala Ala Leu Pro Ala Lys Lys Phe 1115 1120 1125 Gln Ala Ala Val Gln Asp Ala Gln Leu Gly Pro Gly Arg Asp Ile 1130 1135 1140 Pro His Leu Thr Pro Asp Leu Ile Glu Lys Tyr Val Ser Asp Leu 1145 1150 1155 Lys Leu Arg Asn Leu Leu 1160 <210> 171 <211> 1166 <212> PRT <213> Artificial Sequence <220> <223> Nocardia vulneris <400> 171 Met Ala Thr Asp Ser Arg Ser Asp Arg Leu Arg Arg Arg Ile Ala Gln 1 5 10 15 Leu Phe Ala Glu Asp Glu Gln Val Lys Ala Ala Val Pro Asp Pro Glu 20 25 30 Val Val Glu Ala Ile Arg Ala Pro Gly Leu Arg Leu Ala Gln Ile Met 35 40 45 Ala Thr Val Met Glu Arg Tyr Ala Asp Arg Pro Ala Val Gly Gln Arg 50 55 60 Ala Ser Glu Pro Val Thr Glu Ser Gly Arg Thr Thr Phe Arg Leu Leu 65 70 75 80 Pro Glu Phe Glu Thr Leu Thr Tyr Arg Glu Leu Trp Ala Arg Val Arg 85 90 95 Ala Val Ala Ala Ala Trp His Gly Asp Pro Glu Arg Pro Leu Arg Ala 100 105 110 Gly Asp Phe Val Ala Leu Leu Gly Phe Thr Ser Ile Asp Tyr Gly Thr 115 120 125 Leu Asp Leu Ala Asn Ile His Leu Gly Leu Val Thr Val Pro Leu Gln 130 135 140 Ser Gly Ala Ala Ala Pro Gln Leu Ala Ala Ile Leu Ala Glu Thr Thr 145 150 155 160 Pro Arg Val Leu Ala Ala Thr Pro Asp His Leu Asp Val Ala Val Glu 165 170 175 Leu Leu Thr Gly Gly Ala Ser Pro Glu Arg Leu Val Val Phe Asp Tyr 180 185 190 Arg Pro Ala Asp Asp Asp His Arg Ala Ala Leu Glu Ser Ala Arg Arg 195 200 205 Arg Leu Ser Asp Ala Gly Ser Ala Val Val Val Glu Thr Leu Asp Ala 210 215 220 Val Arg Ala Arg Gly Gly Glu Leu Pro Ala Ala Pro Leu Phe Val Pro 225 230 235 240 Ala Ala Asp Glu Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Gly Leu Asn Arg Thr 260 265 270 Thr Trp Leu Asn Gly Ala Lys Gly Val Gly Leu Thr Leu Cys Tyr Met 275 280 285 Pro Met Ser His Val Ala Gly Arg Ala Thr Phe Ser Gly Val Leu Ala 290 295 300 Arg Gly Gly Thr Ala Tyr Phe Thr Ala Arg Ser Asp Met Ser Thr Leu 305 310 315 320 Phe Glu Asp Leu Ala Leu Val Arg Pro Thr Glu Met Phe Phe Val Pro 325 330 335 Arg Val Cys Asp Met Ile Phe Gln Arg Tyr Gln Ala Glu Leu Ser Arg 340 345 350 Arg Ala Pro Ala Ala Asp Ala Ser Pro Glu Leu Glu Gln Glu Leu Lys 355 360 365 Thr Glu Leu Arg Leu Ser Ala Val Gly Asp Arg Leu Leu Gly Ala Ile 370 375 380 Ala Gly Ser Ala Pro Leu Ser Ala Glu Met Arg Glu Phe Met Glu Ser 385 390 395 400 Leu Leu Asp Leu Glu Leu His Asp Gly Tyr Gly Ser Thr Glu Ala Gly 405 410 415 Ile Gly Val Leu Gln Asp Asn Val Val Gln Arg Pro Pro Val Ile Asp 420 425 430 Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Gln 435 440 445 Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Glu Gly Met Ile Pro 450 455 460 Gly Tyr Tyr Arg Arg Pro Glu Val Thr Ala Glu Ile Phe Asp Glu Asp 465 470 475 480 Gly Phe Tyr Lys Thr Gly Asp Ile Val Ala Glu Leu Glu Pro Asp Arg 485 490 495 Leu Ile Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly 500 505 510 Glu Phe Val Thr Val Ala His Leu Glu Ala Val Phe Ala Thr Ser Pro 515 520 525 Leu Ile Arg Gln Ile Tyr Ile Tyr Gly Asn Ser Glu Arg Ser Phe Leu 530 535 540 Leu Ala Val Ile Val Pro Thr Ala Asp Ala Leu Ala Gly Gly Val Thr 545 550 555 560 Asp Ala Leu Asn Thr Ala Leu Thr Glu Ser Leu Gln Gln Leu Ala Lys 565 570 575 Glu Ala Gly Leu Gln Ser Tyr Glu Leu Pro Arg Glu Phe Leu Val Glu 580 585 590 Thr Glu Pro Phe Thr Val Ala Asn Gly Leu Leu Ser Gly Ile Ala Lys 595 600 605 Leu Leu Arg Pro Lys Leu Lys Glu His Tyr Gly Glu Arg Leu Glu Gln 610 615 620 Leu Tyr Arg Asp Met Glu Ala Asn Arg Asn Asp Glu Leu Ile Glu Leu 625 630 635 640 Arg Arg Thr Ala Ala Glu Leu Pro Val Leu Glu Thr Val Thr Arg Ala 645 650 655 Ala Arg Ser Met Leu Gly Leu Ala Ala Ser Glu Leu Arg Pro Asp Ala 660 665 670 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser 675 680 685 Thr Leu Leu Gln Asp Met Leu Asp Val Glu Val Pro Val Gly Val Ile 690 695 700 Val Ser Pro Ala Asn Ser Leu Ala Asp Leu Ala Lys Tyr Ile Glu Ala 705 710 715 720 Glu Arg His Ser Gly Ala Arg Arg Pro Ser Leu Val Ser Val His Gly 725 730 735 Pro Gly Thr Glu Val Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile 740 745 750 Asp Glu Arg Thr Leu Ala Ala Ala Lys Ala Val Pro Ala Ala Pro Ala 755 760 765 Gln Ala Gln Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg 770 775 780 Phe Leu Cys Leu Glu Trp Leu Gln Arg Leu Asp Lys Thr Gly Gly Thr 785 790 795 800 Leu Ile Cys Ile Val Arg Gly Thr Asp Ala Ala Ala Ala Arg Lys Arg 805 810 815 Leu Asp Ala Val Phe Asp Ser Gly Asp Pro Glu Leu Leu Asp Arg Tyr 820 825 830 Arg Lys Leu Ala Ala Asp His Leu Glu Val Leu Ala Gly Asp Ile Gly 835 840 845 Asp Pro Asn Leu Gly Leu Asp Glu Ala Thr Trp Gln Arg Leu Ala Ala 850 855 860 Thr Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His Val Leu 865 870 875 880 Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile 885 890 895 Ile Arg Leu Ala Ile Thr Glu Arg Arg Lys Pro Val Thr Tyr Leu Ser 900 905 910 Thr Val Ala Val Ala Ala Gln Val Asp Pro Ala Val Phe Asp Glu Glu 915 920 925 Arg Asp Ile Arg Glu Met Ser Ala Val Arg Thr Ile Asp Ala Gly Tyr 930 935 940 Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 945 950 955 960 Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp 965 970 975 Met Ile Leu Ala His Ser Thr Tyr Val Gly Gln Leu Asn Val Pro Asp 980 985 990 Val Phe Thr Arg Leu Ile Leu Ser Leu Val Leu Thr Gly Ile Ala Pro 995 1000 1005 Tyr Ser Phe Tyr Gly Thr Asp Ser Asp Gly Gln Arg Arg Arg Ala 1010 1015 1020 His Tyr Asp Gly Leu Pro Ala Asp Phe Val Ala Glu Ser Ile Thr 1025 1030 1035 Thr Leu Gly Ala Arg Ala Asp Ser Gly Phe His Thr Tyr Asp Val 1040 1045 1050 Trp Asn Pro Tyr Asp Asp Gly Ile Ser Leu Asp Glu Phe Val Asp 1055 1060 1065 Trp Leu Ser Asp Phe Gly Val Pro Met Gln Arg Ile Asp Asp Tyr 1070 1075 1080 Asp Glu Trp Phe Arg Arg Phe Glu Thr Ala Ile Arg Ala Leu Pro 1085 1090 1095 Glu Lys Gln Arg Asp Ala Ser Leu Leu Pro Leu Leu Asp Ala His 1100 1105 1110 Arg Arg Pro Leu Arg Ala Val Arg Gly Ser Leu Leu Pro Ala Lys 1115 1120 1125 Asn Phe Gln Ala Ala Val Gln Ser Ala Arg Ile Gly Pro Asp Gln 1130 1135 1140 Asp Ile Pro His Leu Ser Pro Gln Leu Ile Asp Lys Tyr Val Thr 1145 1150 1155 Asp Leu Arg His Leu Gly Leu Ile 1160 1165 <210> 172 <211> 1175 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium confluentis <400> 172 Met Ser Val Asp Thr Gln Asp Asp Gln Leu Ala Arg Arg Ile Ala Asp 1 5 10 15 Leu Val Gly Asp Asp Ala Gln Phe Ala Ala Ala Arg Pro Asp Asp Ala 20 25 30 Val Thr Ala Ala Ile Asn Glu Pro Ser Leu Arg Leu Ala Gln Ile Met 35 40 45 Asp Thr Leu Ala Glu Gly Tyr Ala Asp Arg Pro Ala Leu Gly Ala Arg 50 55 60 Ala Val Glu Phe Val Glu Asp Pro Ala Thr Gly Arg Thr Thr Thr Thr 65 70 75 80 Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Arg Glu Leu Trp Ala Arg 85 90 95 Leu Arg Ser Val Ala Ala Ala Leu Ala Asp Gly Ala Val Ser Pro Gly 100 105 110 Asp Arg Val Gly Val Leu Gly Phe Thr Ser Ile Asp Tyr Ala Val Ile 115 120 125 Asp Met Ala Thr Val Leu Leu Gly Ala Val Cys Val Pro Leu Gln Thr 130 135 140 Ser Ala Pro Leu Thr Gln Leu Gln Pro Ile Val Asp Glu Thr Glu Pro 145 150 155 160 Thr Leu Ile Ala Ala Ser Val Asp His Leu Gly Asp Ala Ile Gly Leu 165 170 175 Ser Gly Asn Ser Glu Ser Pro Ala Arg Leu Ile Val Phe Asp Leu His 180 185 190 Pro Glu Val Asp Asp His Arg Asp Ala Val Ala Asp Ala Gln Arg Arg 195 200 205 Leu Ala Asp Gly Glu His Ala Val Thr Val Glu Ala Leu Ala Asp Val 210 215 220 Ile Ala Arg Gly Glu Ser Lys Val Thr Gly Pro Val Pro Val Val Gly 225 230 235 240 Glu Gly Asp Pro Leu Ser Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly 245 250 255 Arg Pro Lys Gly Ala Met Tyr Pro Glu Ser Leu Val Thr Asn Ala Trp 260 265 270 Arg Arg Ser Thr Asn Met Val Gly Ala Gln Gly Thr Thr Gly Pro Ser 275 280 285 Ile Thr Leu Ser Phe Met Pro Met Ser His Val Met Gly Arg His Ile 290 295 300 Leu Phe Glu Thr Leu Ala Ser Gly Gly Thr Ser Tyr Phe Ala Ala Thr 305 310 315 320 Ser Asp Leu Ser Thr Phe Leu Glu Asp Leu Ala Leu Val Arg Pro Thr 325 330 335 Leu Leu Ser Phe Val Pro Arg Ile Trp Glu Met Ile Phe Thr Glu His 340 345 350 Gln Ser Ala Leu Asn Arg Arg Val Asn Ala Gly Glu Asp Glu Ala Thr 355 360 365 Ala Ser Glu Ala Val Ser Ala Asp Leu Arg Asp Asn Leu Leu Gly Gly 370 375 380 Arg Tyr Val Ala Ala Leu Thr Gly Ser Ala Pro Ile Ser Ala Glu Met 385 390 395 400 Thr Ala Phe Val Glu Ser Leu Leu Gly Leu His Leu Val Glu Gly Tyr 405 410 415 Gly Ser Thr Glu Ala Gly Met Val Phe Ile Asp Gly Ala Val Arg Arg 420 425 430 Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr 435 440 445 Phe His Thr Asp Arg Pro Asn Pro Arg Gly Glu Leu Leu Val Lys Ser 450 455 460 Asp Thr Met Phe Pro Gly Tyr Phe Asn Arg Pro Asp Ala Thr Ala Asp 465 470 475 480 Val Phe Asp Glu Asp Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala Glu 485 490 495 Thr Gly Pro Asp Gln Leu Val Tyr Leu Asp Arg Arg Asn Asn Val Leu 500 505 510 Lys Leu Ser Gln Gly Glu Phe Val Thr Val Ser Lys Val Glu Ala Val 515 520 525 Phe Ala Asp Ser Pro Val Ile Gly Gln Ile Tyr Ile Tyr Gly Asn Ser 530 535 540 Ala Arg Ala Phe Leu Leu Ala Val Ile Val Pro Thr Asp Asp Ala Leu 545 550 555 560 Ala Gln Val Asp Ser Asp Val Asp Ala Val Lys Pro Ile Leu Gly Glu 565 570 575 Ser Leu Gln Arg Ala Ala Lys Ala Ala Gly Leu Gln Ser Tyr Glu Ile 580 585 590 Pro Arg Asp Phe Ile Val Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly 595 600 605 Leu Leu Thr Gly Ile Arg Lys Leu Ala Arg Pro Arg Leu Lys Glu Lys 610 615 620 Tyr Gly Glu Ala Leu Glu Gln His Tyr Ala Asp Leu Ala Asp Gly Gln 625 630 635 640 Thr Asn Glu Leu Ala Ala Leu Arg Arg Asp Gly Asp Thr Ala Pro Val 645 650 655 Leu Glu Ser Val Ser Arg Ala Ala Ala Ala Leu Leu Ser Ala Ser Ala 660 665 670 Ser Asp Val Gln Ala Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser 675 680 685 Leu Ser Ala Val Thr Phe Ala Asn Leu Leu Arg Glu Ile Phe Asp Ile 690 695 700 Asp Val Pro Val Gly Val Ile Val Asn Pro Ala Ala Asp Leu Gln Ala 705 710 715 720 Ile Ala Asp Tyr Ile Asp Asn Glu Arg Asn Ser Gly Ala Thr Arg Pro 725 730 735 Thr Phe Ala Thr Val His Gly Ala Asp Ala Thr Ala Val His Ala Arg 740 745 750 Asp Leu Thr Leu Asp Lys Phe Val Asp Ala Glu Thr Leu Ala Ala Ala 755 760 765 Pro Ser Leu Pro Arg Pro Gly Glu Gln Val Arg Thr Val Leu Leu Thr 770 775 780 Gly Ala Thr Gly Phe Leu Gly Arg Phe Leu Ala Leu Glu Trp Leu Glu 785 790 795 800 Arg Met Asp Leu Val Asp Gly Thr Leu Ile Cys Ile Val Arg Ala Lys 805 810 815 Asp Asp Ala Ala Ala Arg Ala Arg Leu Asp Ala Thr Phe Asp Ser Gly 820 825 830 Asp Pro Ala Leu Leu Ala Arg Tyr Glu Lys Leu Ala Ala Asp His Leu 835 840 845 Glu Val Val Ala Gly Asp Lys Ser Glu Ala Asp Leu Gly Leu Asp Ala 850 855 860 Gln Thr Trp Gln Arg Ile Ala Asp Thr Val Asp Leu Ile Val Asp Pro 865 870 875 880 Ala Ala Leu Val Asn His Val Leu Pro Tyr Ala Gln Leu Phe Gly Pro 885 890 895 Asn Ala Leu Gly Thr Ala Glu Leu Ile Arg Ile Ala Leu Thr Ser Lys 900 905 910 Leu Lys Gln Phe Ala Tyr Val Ser Thr Ile Gly Val Gly Ala Gly Ile 915 920 925 Glu Pro Ala Ser Ala Phe Val Glu Asp Ala Asp Ile Arg Glu Ile Ser 930 935 940 Ala Thr Arg Ala Val Asp Glu Thr Tyr Ala Asn Gly Tyr Gly Thr Ser 945 950 955 960 Lys Trp Ala Gly Glu Val Leu Leu Trp Glu Ala His Asp Leu Cys Gly 965 970 975 Leu Pro Val Ser Val Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Gln 980 985 990 Phe Val Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg Leu Met Leu 995 1000 1005 Ser Leu Val Ala Thr Gly Val Ala Pro Lys Ser Phe Tyr Glu Leu 1010 1015 1020 Asp Ser Asp Gly Asn Arg Gln Arg Ala His Tyr Asp Gly Leu Pro 1025 1030 1035 Val Asp Phe Ile Ala Glu Ala Ile Ser Thr Leu Ser Val Gln Leu 1040 1045 1050 Leu Asp Gly Phe Glu Thr Tyr His Val Met Asn Pro Tyr Asp Asp 1055 1060 1065 Gly Ile Gly Gln Asp Gln Phe Val Asp Trp Leu Val Asp Ala Gly 1070 1075 1080 Tyr Ser Ile Gln Arg Val Asp His Tyr Asp Thr Trp Leu Gln Arg 1085 1090 1095 Phe Glu Thr Ala Val Arg Ala Leu Pro Ala Lys Gln Arg Ser Ala 1100 1105 1110 Ser Leu Leu Pro Leu Leu His Asn Tyr Gln Gln Pro Val Pro Pro 1115 1120 1125 Leu Asn Gly Ala Met Ala Ser Thr Asp Arg Phe Arg Ala Ala Val 1130 1135 1140 Gln Asp Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro His Ile Thr 1145 1150 1155 Pro Gln Ile Ile Val Lys Tyr Ala Thr Asn Leu Glu Val Leu Gly 1160 1165 1170 Leu Leu 1175 <210> 173 <211> 1170 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacter arupensis <400> 173 Met Ala Thr Ala Ala Gln Pro Glu Trp Met Ala Arg Arg Ile Ser Glu 1 5 10 15 Leu Tyr Ala Thr Asp Pro Gln Phe Ala Ala Ala Arg Pro Ser Asp Val 20 25 30 Val Arg Ala Gln Ile Asp His Pro Gly Leu Arg Leu Pro Glu Leu Val 35 40 45 Arg Thr Val Cys Glu Gly Tyr Ala Glu Arg Pro Ala Leu Gly Gln Arg 50 55 60 Asp Tyr Arg Leu Val Thr Asp Pro Ser Thr Gly Arg Thr Ser Ala Gln 65 70 75 80 Ala Gln Pro Gly Met Thr Thr Ile Ser Tyr Arg Glu Met Ala Lys Arg 85 90 95 Val Asp Ala Val Ala Gly Gly Leu Ala Gly Asp Pro Val Gln Pro Gly 100 105 110 Asp Leu Val Ala Val Leu Gly Phe Thr Ser Val Asp Tyr Thr Ile Val 115 120 125 Asp Leu Ala Val Val Gln Leu Gly Ala Val Ala Val Pro Val Gln Tyr 130 135 140 Thr Thr Ala Ala Ala Gly Leu Gln His Ile Ile Ala Glu Thr Glu Pro 145 150 155 160 Thr Val Leu Ala Val Ser Val Glu Asp Leu Pro Lys Ala Val Glu Val 165 170 175 Ala Ala Thr Ala Ser Ala Leu Arg Arg Leu Val Val Phe Asp Tyr Leu 180 185 190 Ala Gln Ile Asp Asp His Arg Asp Ala Ile Ala Ala Ala Arg Gln Arg 195 200 205 Leu Thr Gln Ala Gly Ser Ala Ala Val Val Glu Thr Leu Ala Gln Val 210 215 220 Met Asp Arg Gly Lys Asp Arg Pro Thr Pro Arg Val Asp Ala Pro Ala 225 230 235 240 Asp Asn Pro Met Val Ala Val Leu Tyr Thr Ser Gly Ser Thr Gly Ala 245 250 255 Pro Lys Gly Val Met Cys Ser Glu Gln Leu Val Thr Leu Ala Trp Arg 260 265 270 Gly Ile Ala Pro Ala Gly Leu Arg His Asp Leu Pro Ser Ile Thr Leu 275 280 285 Asn Phe Arg Pro Met Ser His Val Val Gly Arg Ser Met Leu Tyr Gly 290 295 300 Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Val Ser Ser Arg Asp Phe 305 310 315 320 Ser Thr Phe Leu Asp Asp Leu Ala Leu Val Arg Pro Thr Gln Leu Asn 325 330 335 Phe Val Pro Arg Val Trp Asp Met Leu Ser Glu Glu Phe Gly Arg Ala 340 345 350 Val Ser Gln Arg Val Thr Asp Glu Ala Glu Arg Ala Ala Val Gln Glu 355 360 365 Gln Val Met Ala Gln Gln Arg Arg Asp Leu Leu Gly Ala Arg Tyr Val 370 375 380 Val Ala Ser Thr Gly Ser Ala Pro Ile Ser Ala Glu Leu Lys Ala Trp 385 390 395 400 Val Glu Ala Phe Thr Ala Ile His Leu Thr Glu Thr Tyr Gly Ser Thr 405 410 415 Glu Ser Val Leu Leu Met Val Asp Gly Arg Val Gln Cys Pro Pro Val 420 425 430 Thr Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr 435 440 445 Asp Arg Pro His Pro Arg Gly Glu Phe Ala Val Lys Ser Ser Ser Gln 450 455 460 Phe Ser Gly Tyr Tyr Lys Arg Pro Asp Lys Thr Ala Glu Ala Phe Asp 465 470 475 480 Ala Asp Gly Tyr Tyr Leu Thr Gly Asp Ile Leu Ala Glu Val Ala Pro 485 490 495 Gly Glu Phe Thr Phe Val Asp Arg Arg Asn Asp Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Thr Val Ser Lys Val Glu Gly Val Phe Ala Asp 515 520 525 Ser Pro Leu Ile His Gln Ile Tyr Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Leu Val Ala Val Val Val Pro Thr Glu Glu Ala Leu Ala Ala His 545 550 555 560 Asp Glu Arg Thr Leu Glu Ser Leu Ile Arg Gln Ser Leu Gln Asp Thr 565 570 575 Val Lys Arg Ala Gly Leu Gln Ser Tyr Glu Val Pro Arg Asp Phe Leu 580 585 590 Ile Glu Ser Glu Pro Phe Thr Ala Gln Asn Gly Leu Leu Thr Ala Val 595 600 605 Gly Lys Pro Ala Arg Pro Lys Leu Lys Glu His Tyr Gly Glu Arg Leu 610 615 620 Glu Arg Leu Tyr Asp Asp Val Ser Ala Arg Gln Ala Arg Glu Leu Gln 625 630 635 640 Ala Leu Arg Glu Gly Ala Ser Asp Arg Ser Val Gln Glu Thr Val Ile 645 650 655 Arg Ala Ala Ala Ala Leu Leu Gly Val Ser Ala Ala Glu Leu Ser Ala 660 665 670 Glu Ala Arg Phe Ala Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Leu Ser Asn Leu Leu His Glu Ile Val Lys Val Glu Val Pro Val Gly 690 695 700 Val Ile Val Gly Pro Thr Ser Asp Leu Arg Thr Ile Ala Gly Tyr Val 705 710 715 720 Glu Ala Gln Arg Glu Ser Gly Ala Gln His Ala Ser Tyr Ala Gly Val 725 730 735 His Gly Pro Asp Ala Thr Glu Leu His Ala Ala Asp Leu Ala Leu Asp 740 745 750 Lys Phe Leu Asp Ala Asp Thr Leu Ala Ala Ala Pro Thr Leu Pro Arg 755 760 765 Pro Ala Glu Gln Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Tyr Leu Val Leu Gln Trp Leu Glu Arg Leu Ala Pro Ile 785 790 795 800 Gly Gly Thr Leu Ile Cys Leu Val Arg Ala Gly Asp Ala Ala Glu Gly 805 810 815 Arg Ala Arg Leu Asp Gln Val Phe Asp Ser Gly Asp Ala Gly Leu Leu 820 825 830 Ala His Tyr Gln Arg Leu Ala Ala Glu His Leu Glu Val Ile Ala Ala 835 840 845 Asp Lys Gly Glu Pro Gly Leu Gly Val Asp Ala Met Thr Trp Gln Arg 850 855 860 Leu Ala Asp Thr Val Asp Leu Ile Ile Asp Pro Ala Ala Leu Val Asn 865 870 875 880 His Met Leu Pro Tyr Arg Gln Leu Phe Val Pro Asn Val Arg Gly Thr 885 890 895 Ala Glu Leu Leu Arg Val Ala Ile Thr Gly Arg Leu Lys Pro Tyr Val 900 905 910 Tyr Leu Ser Thr Val Ala Val Gly Asp Gln Ile Pro Pro Ala Met Phe 915 920 925 Thr Glu Asp Ala Asp Ile Arg Ala Ile Ser Pro Ser Arg Gln Leu Gly 930 935 940 Glu Gly His Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Ser Glu Val 945 950 955 960 Leu Leu Arg Gln Ala Asn Asp Leu Cys Gly Leu Pro Ile Thr Val Phe 965 970 975 Arg Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn 980 985 990 Leu Pro Asp Asn Phe Thr Arg Leu Ile Leu Ser Leu Ala Leu Thr Gly 995 1000 1005 Ile Val Pro Gly Ser Phe Tyr Glu Arg Gly Pro Asp Gly Glu Arg 1010 1015 1020 Gln Arg Ala His Tyr Asp Gly Leu Pro Val Gly Phe Val Ala Asp 1025 1030 1035 Ala Val Ser Thr Leu Gly Glu Lys Tyr Asp Ala Gly His Arg Thr 1040 1045 1050 Phe His Val Ala Asn Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu 1055 1060 1065 Phe Ala Asp Trp Leu Ile Ala Ala Asp Pro Ala Ile Arg Arg Ile 1070 1075 1080 Asp Asp Tyr Ala Ile Trp Leu Gln Arg Phe Glu Thr Ala Leu Arg 1085 1090 1095 Ala Leu Pro Asp Arg Leu Arg Gln His Ser Leu Leu Pro Leu Leu 1100 1105 1110 Gly Asn Tyr Arg Arg Pro Arg Thr Pro Ile Ala Gly Ser Leu Val 1115 1120 1125 Pro Ala Thr Arg Phe Arg Ala Ala Val Gln Ala Ala Lys Ile Gly 1130 1135 1140 Pro Asp Gln Asp Ile Pro His Ile Ser Ala Pro Ile Ile Gly Lys 1145 1150 1155 Tyr Leu Ser Asp Leu Arg Leu Leu Gly Leu Leu Gly 1160 1165 1170 <210> 174 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium simiae <400> 174 Met Gln Thr Thr Lys Ser Lys Tyr Gln Ala Ala Arg Leu Asp Leu Ala 1 5 10 15 Glu His Ile Lys Ala Leu Val Thr Gln Asp Ala Gln Leu Gln Gly Ala 20 25 30 Met Pro Leu Ser Pro Ile Ser Asp Ala Lys Val Asn Pro Ala Leu Gly 35 40 45 Leu Ala Gln Thr Val Ala Leu Cys Met Glu Gly Tyr Ser Asp Arg Pro 50 55 60 Ala Leu Ala Gln Arg Gly Ile Asp His Val Ser Asp Pro Val Thr Gly 65 70 75 80 Arg Val Ser Arg Arg Leu Leu Gln His Phe Thr Thr Leu Ser Tyr Gly 85 90 95 Glu Leu Trp Gly Arg Ala Lys Ala Leu Ala Ser Leu Trp Gln His Asp 100 105 110 Asp Ala Arg Gln Leu Arg Ala Asn Asp Phe Leu Cys Ile Ile Ala Phe 115 120 125 Ala Gly Ser Asp Phe Val Thr Val Asp Leu Ala Ala Ile His Asn Gly 130 135 140 Ala Val Val Ala Pro Leu Gln Thr Asn Ala Pro Leu Gly Gln Leu Thr 145 150 155 160 Glu Ile Val Lys Glu Val Gln Pro Arg Trp Leu Ala Thr Ser Leu Glu 165 170 175 Cys Leu Pro Ile Thr Val Lys Leu Val Leu Leu Gly His Arg Pro Thr 180 185 190 Gly Val Leu Leu Phe Asp Tyr Asp Glu His Val Asp Asp His Arg Glu 195 200 205 Ala Leu Ala Ala Ala Arg Ala Glu Leu Ser Ala Ala Gly Leu Pro Asp 210 215 220 Leu Leu Leu Thr Leu Glu Ala Ala Cys Ala Leu Gly Ala Lys Leu Pro 225 230 235 240 Ile Pro Gln Leu Phe Ser Glu Lys Ala Thr Asp Ser Arg Leu Ser Thr 245 250 255 Leu Tyr Tyr Thr Ser Gly Ser Thr Gly Leu Pro Lys Gly Ala Met Tyr 260 265 270 Pro Glu Ser Met Leu Lys Pro Asn Trp Arg Val Val Ala Pro Ile Pro 275 280 285 Val Ile Tyr Met His Tyr Met Pro Met Asn His Ser Phe Gly Arg Ser 290 295 300 Gly Val Phe Ser Thr Leu Ser Asn Gly Gly Thr Cys Tyr Phe Thr Ala 305 310 315 320 Lys Ser Asp Leu Ser Glu Leu Phe Asn Asp Ile Gln Ser Val Arg Pro 325 330 335 Thr Val Met Ala Val Val Pro Arg Ile Cys Glu Met Val Tyr Gln Gln 340 345 350 Tyr Gln Thr Gln Leu Glu Arg Arg Ser Ala Gly Asn Ser Glu Thr Glu 355 360 365 Ala Leu Arg Gln Gln Leu Ile Asp Glu Ile Arg Asn Gly Leu Leu Gly 370 375 380 Gly Arg Leu Leu Ser Gly Ser Phe Gly Ser Ala Pro Leu Ala Pro Glu 385 390 395 400 Leu Arg Glu Phe Met Glu Ala Cys Leu Gly Phe Gly Met Asp Glu Phe 405 410 415 Tyr Gly Ala Thr Glu Ile Ser Gly Ile Ser Arg Asn Asn Arg Leu Leu 420 425 430 Arg Pro Pro Ile Ile Asp Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly 435 440 445 Tyr Phe Thr Thr Asp Lys Pro His Pro Arg Gly Glu Leu Leu Val Lys 450 455 460 Thr His Ala Ile Met Leu Gly Tyr Tyr Lys Arg Pro Glu Val Thr Ala 465 470 475 480 Ser Ala Phe Asp Glu Asp Gly Tyr Tyr Lys Thr Gly Asp Ile Met Ala 485 490 495 Glu Thr Ala Thr Asp Val Leu Val Tyr Leu Asp Arg Arg Asn Asn Val 500 505 510 Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Ile Ala Arg Leu Glu Ala 515 520 525 Leu Phe Thr Asn Gly His Pro Leu Ile Arg Gln Ala Tyr Leu Tyr Gly 530 535 540 Thr Ser Asp Arg Ser Phe Leu Leu Gly Val Leu Val Pro Asn Asp Glu 545 550 555 560 Ser Val Arg Asp Met Gly Ile Thr Asp Glu Ala Ala Leu Lys Ala Ala 565 570 575 Leu Arg Glu Ala Val Lys Gln Val Ala Arg Glu Glu Gln Leu Asn Ala 580 585 590 Tyr Glu Val Pro Arg Asp Phe Leu Leu Glu His Thr Pro Phe Ser Val 595 600 605 Glu Asn Gly Leu Leu Thr Gly Ile Gly Lys Tyr Gln Arg Pro Lys Phe 610 615 620 Lys Glu Arg Tyr Ala Ala Arg Leu Glu Gln Leu Tyr Asp Asp Ile Ala 625 630 635 640 Thr His Gln Ala Asp Glu Leu Gln Thr Leu Arg Arg Glu Gly Cys Ser 645 650 655 Ala Pro Ile Val Glu Thr Val Ala Arg Ala Ile Glu Ala Thr Leu Gly 660 665 670 Ile Glu Val Leu Asp Pro Tyr Thr Gln Ala Ser Phe Thr Glu Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Ser Cys Ser Val Leu Leu Glu Asp Ile 690 695 700 Tyr Gln Ile Glu Val Pro Ala Ser Val Ile Asn His Pro Thr Gly Asn 705 710 715 720 Leu Gln Gln Val Val Gln Tyr Ile Glu Arg Ala Gln Asp Lys Thr Ile 725 730 735 Arg Arg Pro Thr Phe Ser Ser Val His Gly Arg Ser Ala Thr Glu Ile 740 745 750 Arg Ala Ser Asp Leu Asn Leu Asp Asn Phe Leu Asn Ala Gly Ala Leu 755 760 765 Glu Glu Ala Ala Asp Ala Thr Pro Pro Ala Ser Glu Pro Arg Thr Val 770 775 780 Leu Val Thr Gly Ala Asn Gly Tyr Leu Gly His Phe Leu Cys Leu Glu 785 790 795 800 Trp Leu Glu Arg Met Ala Ala Val Gly Gly Arg Val Ile Cys Ile Ala 805 810 815 Arg Gly Arg Asp Thr Asp Ser Ala Arg Gln Arg Ile Ala Glu Ala Phe 820 825 830 Glu Ser Gly Asp Ala Gln Leu Lys Gln Tyr Phe Glu Thr Leu Ala Asn 835 840 845 Lys His Leu Asp Val Leu Pro Gly Asp Leu Gly Glu Pro Glu Leu Gly 850 855 860 Leu Ser Ala Thr Asp Trp Asn Ala Leu Thr Glu Thr Val Asp Leu Ile 865 870 875 880 Val His Pro Ala Ala Phe Val Asn His Val Leu Pro Tyr Ser Gln Leu 885 890 895 Phe Gly Pro Asn Val Ala Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu 900 905 910 Ser Ala Arg Leu Lys Pro Ile His Tyr Val Ser Thr Val Ala Ala Ala 915 920 925 Ala Ile Val Gly Gly Val Ile Asp Glu Glu Ala Asp Val Arg Glu Ala 930 935 940 Ser Pro Val Arg Pro Leu Asp Ala Glu Arg Tyr Ala Asp Gly Tyr Ala 945 950 955 960 Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Asp Ala His Glu Arg 965 970 975 Phe Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala His 980 985 990 Ser Tyr Tyr Gln Gly Gln Val Asn Ala Ser Asp Met Phe Thr Arg Trp 995 1000 1005 Leu Ser Ser Val Val Arg Thr Gly Leu Ala Pro Arg Ser Phe Tyr 1010 1015 1020 Ala Gln Gly Ala Gly Glu Pro His Tyr Asp Gly Leu Pro Val Asp 1025 1030 1035 Phe Thr Ala Lys Ala Ile Ala Val Leu Gly Ala Glu Ala Arg Asp 1040 1045 1050 Gly Tyr Gln Thr Tyr His Val Ile Asn Pro His Glu Asp Gly Ile 1055 1060 1065 Ser Met Asp Thr Phe Val Asp Trp Ala Ile Ser Ala Gly His Pro 1070 1075 1080 Ile Gln Arg Ile Asp Gln Tyr Asp Asp Trp Phe Ala Arg Phe Glu 1085 1090 1095 Thr Ala Leu Arg Gly Leu Pro Glu Lys Gln Arg Gln Gln Ser Phe 1100 1105 1110 Leu Pro Leu Leu His Gln Leu Arg Gln Pro Met Pro Arg Thr Ala 1115 1120 1125 Gly Ala Trp Val Ser Ala Thr Arg Phe Gln Arg Asp Val Arg Lys 1130 1135 1140 Phe Gly Val Gly Pro Asp Arg Asp Ile Pro His Leu Ser Ala Ala 1145 1150 1155 Phe Ile Gly Lys Cys Leu Ala Asp Ile Lys His Leu Gly Leu Met 1160 1165 1170 <210> 175 <211> 1148 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces sp. TSRI0395 <400> 175 Met Ala Glu Pro Leu Asp Ala Ala Ala Val Pro Ala His Asp Pro Gly 1 5 10 15 Gln Gly Leu Ala Glu Val Leu Ala Ser Val Glu Pro Gly Arg Ala Leu 20 25 30 Ala Glu Val Met Ala Ser Val Leu Glu Ser His Gly Asp Arg Pro Ala 35 40 45 Leu Gly Glu Arg Ala Arg Asp Pro Glu Thr Gly Arg Leu Leu Pro His 50 55 60 Phe Asp Thr Ile Ser Tyr Arg Glu Leu Trp Ser Arg Val Arg Ala Leu 65 70 75 80 Ala Gly Arg Trp His His Asp Pro Ala Tyr Pro Leu Gly Pro Gly Asp 85 90 95 Arg Ile Cys Thr Leu Gly Phe Thr Ser Thr Asp Tyr Ala Thr Leu Asp 100 105 110 Leu Ala Cys Ile His Leu Gly Ala Val Pro Val Pro Leu Gln Ser Asn 115 120 125 Ala Ala Leu Pro Arg Leu Ala Pro Ile Val Glu Glu Ser Gly Pro Thr 130 135 140 Val Leu Ala Ala Ser Val Asp Arg Leu Asp Thr Ala Val Asp Val Val 145 150 155 160 Leu Ala Ser Arg Thr Ile Arg Arg Leu Leu Val Phe Asp Asp Gly Pro 165 170 175 Gly Thr Thr Arg Pro Ser Gly Ala Leu Ala Ala Ala Arg Glu Arg Leu 180 185 190 Ala Gly Ser Pro Val Thr Val Asp Thr Leu Ala Glu Leu Ile Asp Arg 195 200 205 Gly Arg Asp Leu Pro Pro Pro Pro Leu His Thr Pro Asp Pro Gly Glu 210 215 220 Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro 225 230 235 240 Lys Gly Ala Met Tyr Thr Gln Arg Leu Leu Gly Thr Ala Trp Tyr Gly 245 250 255 Phe Ser Tyr Gly Ala Ala Asp Thr Pro Ala Ile Ser Val Leu Tyr Leu 260 265 270 Pro Gln Ser His Leu Ala Gly Arg Tyr Ala Val Met Gly Ser Leu Val 275 280 285 Lys Gly Gly Thr Gly Tyr Phe Thr Ala Ala Asp Asp Leu Ser Thr Leu 290 295 300 Phe Glu Asp Ile Ala Leu Val Arg Pro Thr Glu Leu Thr Met Val Pro 305 310 315 320 Arg Leu Cys Asp Met Leu Leu Gln His Tyr Arg Ser Glu Leu Glu Arg 325 330 335 Arg Ser Asp Glu Pro Gly Asp Ile Glu Ala Ala Val Arg Lys Ala Val 340 345 350 Arg Glu Asp Phe Leu Gly Gly Arg Val Ala Lys Ala Phe Val Gly Thr 355 360 365 Ala Pro Leu Ser Ala Glu Leu Thr Ala Phe Val Glu Ser Val Leu Gly 370 375 380 Phe His Leu Tyr Thr Gly Tyr Gly Ser Thr Glu Ala Gly Gly Val Leu 385 390 395 400 Leu Asp Thr Val Val Gln Arg Pro Pro Val Thr Asp Tyr Lys Leu Val 405 410 415 Asp Val Pro Glu Leu Gly Tyr Tyr Ala Thr Asp Leu Pro His Pro Arg 420 425 430 Gly Glu Leu Leu Leu Lys Ser His Thr Leu Ile Pro Gly Tyr Tyr Arg 435 440 445 Arg Pro Asp Leu Thr Ala Thr Ile Phe Asp Ala Asp Gly Tyr Tyr Arg 450 455 460 Thr Gly Asp Val Phe Ala Glu Thr Gly Pro Asp Arg Leu Val Tyr Val 465 470 475 480 Asp Arg Thr Lys Asp Thr Leu Lys Leu Ser Gln Gly Glu Phe Val Ala 485 490 495 Val Ser Arg Leu Glu Thr Val Leu Leu Asp Ser Pro Leu Val Gln His 500 505 510 Leu Tyr Leu Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala Val Val 515 520 525 Val Pro Thr Pro Ala Ala Leu Ala Gly Ser Gly Gly Asp Thr Glu Ala 530 535 540 Leu Arg Pro Leu Leu Met Glu Ser Leu Arg Ser Val Ala Arg Arg Ala 545 550 555 560 Gly Leu Asn Ala Tyr Glu Ile Pro Arg Gly Ile Leu Val Glu Pro Glu 565 570 575 Pro Phe Ser Ala Gly Asn Gly Leu Phe Thr Glu Ser His Lys Leu Leu 580 585 590 Arg Pro Arg Leu Lys Glu Arg Tyr Gly Pro Val Leu Glu Leu Leu Tyr 595 600 605 Asp Gln Leu Ala Asp Gly Gln Asp Arg Arg Leu Arg Glu Leu Arg Arg 610 615 620 Thr Gly Ala Asp Arg Pro Val Pro Glu Thr Val Val Arg Ala Ala Gln 625 630 635 640 Ala Leu Leu Gly Cys Leu Ser Ser Asp Leu Arg Pro Gly Ala His Phe 645 650 655 Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Val Ser Phe Ser Glu Leu 660 665 670 Leu Lys Glu Ile Phe His Val Asp Val Pro Val Gly Val Ile Ile Gly 675 680 685 Pro Ala Ala Asp Leu Ala Glu Val Ala Arg Tyr Ile Thr Ala Ala Arg 690 695 700 Arg Pro Thr Gly Ile Arg Arg Pro Thr Phe Ala Ser Val His Gly Glu 705 710 715 720 His Leu Thr Glu Val Arg Ala Gly Asp Leu Val Pro Glu Lys Phe Leu 725 730 735 Asp Ala Pro Thr Leu Ala Ala Ala Pro Gly Leu Pro Arg Pro Asp Gly 740 745 750 Asp Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Tyr Leu Gly Arg 755 760 765 Phe Leu Cys Leu Glu Trp Leu Glu Arg Leu Ala Pro Ser Gly Gly Arg 770 775 780 Leu Ile Cys Leu Val Arg Gly Ser Asp Ala Thr Val Ala Thr Arg Arg 785 790 795 800 Leu Glu Ala Ala Phe Asp Ser Gly Asp Ala Ala Leu Leu Arg Arg Tyr 805 810 815 Arg Lys Ala Ala Ala Lys Thr Leu Glu Val Val Ala Gly Asp Ile Gly 820 825 830 Glu Pro Leu Leu Gly Leu Ala Glu Asp Thr Trp Arg Glu Leu Ala Gly 835 840 845 Thr Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His Leu Leu 850 855 860 Pro Tyr Gly Glu Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val 865 870 875 880 Ile Arg Leu Ala Leu Thr Ala Arg Leu Lys Pro Val Asn His Val Ser 885 890 895 Thr Val Ala Val Cys Leu Gly Thr Pro Ala Glu Thr Ala Asp Glu Asn 900 905 910 Ala Asp Ile Arg Ala Thr Val Pro Val Arg Thr Ile Gly Gln Gly Tyr 915 920 925 Ala Asp Gly Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 930 935 940 Glu Ala His Glu Arg Tyr Gly Leu Pro Val Ala Val Phe Arg Ser Asp 945 950 955 960 Met Val Leu Ala His Arg Thr Tyr Ala Gly Gln Val Asn Val Pro Asp 965 970 975 Val Leu Thr Arg Leu Leu Leu Ser Leu Val Asn Thr Gly Ile Ala Pro 980 985 990 Gly Ser Phe Tyr Arg Thr Asp Thr Arg Ala His Tyr Asp Gly Leu Pro 995 1000 1005 Val Asp Phe Thr Ala Glu Ala Val Val Ala Leu Gly Ala Arg Val 1010 1015 1020 Thr Glu Gly His Arg Thr Phe Asn Val Leu Asn Pro His Asp Asp 1025 1030 1035 Gly Val Cys Leu Asp Thr Phe Val Asp Trp Leu Ile Glu Ala Gly 1040 1045 1050 His Pro Ile Arg Arg Ile Asp Asp His Gly Ala Trp Leu Thr Arg 1055 1060 1065 Phe Thr Ala Ala Leu Arg Ala Leu Pro Glu Lys His Arg Gln His 1070 1075 1080 Ser Leu Leu Pro Leu Ile Gly Ala Trp Ala Glu Pro Asp Glu Gly 1085 1090 1095 Ala Pro Gly Pro Leu Leu Pro Ala Glu Arg Phe His Ala Ala Val 1100 1105 1110 Arg Ala Ala Gly Val Gly Pro Glu Arg Asp Ile Pro Arg Val Ser 1115 1120 1125 Pro Asp Leu Ile Arg Lys Tyr Val Thr Asp Leu Arg Ala Leu Gly 1130 1135 1140 Leu Leu Val Asp Pro 1145 <210> 176 <211> 1172 <212> PRT <213> Artificial Sequence <220> <223> Nocardia seriolae <400> 176 Met Val Glu Asp Val Arg Gly Glu Leu Gln Arg Ile Ala Asp Arg Leu 1 5 10 15 Ala Gln Ser Glu Val Met Lys Arg Phe Glu Ala Leu Leu Ala Asp Glu 20 25 30 Gln Ile Arg Ala Ala Met Pro Val Pro Glu Val Ala Glu Ala Ala Arg 35 40 45 Arg Pro Gly Leu Gly Leu Ala Gly Ile Ala Ala Val Leu Met Glu Gly 50 55 60 Tyr Ala Asp Arg Pro Ala Ile Gly Glu Arg Ala Ala Glu Ile Val Val 65 70 75 80 Asp Ala Asp Gly Arg Arg Thr Arg Arg Leu Leu Pro Ala Tyr Val Thr 85 90 95 Thr Thr Tyr Arg Asp Leu Trp Thr Arg Ala Gly His Ile Ala Ala Ser 100 105 110 Trp Gln His Asp Gly Arg Asn Pro Leu Arg Ala Gly Asp Phe Leu Cys 115 120 125 Ile Leu Gly Phe Ala Ser Gly Asp Phe Ala Ala Leu Glu Leu Ala Ala 130 135 140 Ile Arg Gln Gly Leu Val Thr Val Pro Leu Gln Ser Ser Ala Ala Ala 145 150 155 160 Ala Gln Trp His Ser Ile Ile Thr Glu Thr Glu Ser Arg Thr Leu Ala 165 170 175 Val Ser Leu Glu Leu Leu Ala Pro Ala Leu Glu Cys Val Leu Asp Gly 180 185 190 Thr Ala Val Thr Ser Ile Val Val Phe Asp Phe Glu Pro Glu Asp Asp 195 200 205 Arg Gln Ala Glu Ala Phe Ala Ala Ala Gln Arg Arg Leu Glu Gly Thr 210 215 220 Gly Ile Thr Leu Glu Ser Leu Ala Thr Val Val Asp Arg Gly Ala Arg 225 230 235 240 Leu Pro Glu Ala Pro Leu His Val Pro Ala Asp Glu Asn Glu Leu Ala 245 250 255 Val Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met 260 265 270 Tyr Pro His Arg Leu Ala Ala Gly Met Trp Leu Gly Pro Thr Val Ile 275 280 285 Pro Ala Pro Val Met Asn Phe Cys Tyr Met Pro Leu Ser His Val Ala 290 295 300 Gly Arg Met Val Leu Asn Gly Thr Phe Ser Arg Gly Gly Thr Ala Tyr 305 310 315 320 Phe Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Ile Ala Leu 325 330 335 Val Arg Pro Thr Glu Val Phe Phe Val Pro Arg Val Cys Asp Met Val 340 345 350 Tyr Gln Arg Tyr Gln Ser Glu Thr Gln Arg Arg Ile Ala Ala Gly Glu 355 360 365 Ser Ala Glu Asp Ala Asp Arg Ile Val Lys Thr Ala Leu Arg Glu Glu 370 375 380 Phe Leu Gly Gly Arg Met Ala Arg Val Met Val Gly Ser Ala Pro Ile 385 390 395 400 Ser Ala Glu Met Lys Glu Phe Met Arg Ser Val Leu Gly Gln Pro Ile 405 410 415 Ile Asp Gly Tyr Gly Ser Thr Glu Ala Gly Gly Gly Leu Leu Ile Asp 420 425 430 Asn Glu Ile Arg Arg Pro Pro Val Ile Asp Tyr Lys Leu Ala Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro Tyr Pro Arg Gly Glu 450 455 460 Leu Val Val Lys Ser Met Gln Gln Ile Pro Gly Tyr Phe Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Glu Ile Phe Asp Glu Asp Gly Tyr Tyr Arg Thr Gly 485 490 495 Asp Ile Val Ala Glu Ile Arg Pro Asp Tyr Leu Val Tyr Val Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Thr Val Ala 515 520 525 Lys Leu Glu Ala Val Tyr Ala Thr Ser Pro Leu Ile Ala Gln Ile Phe 530 535 540 Val His Gly Ser Ser Glu Arg Ser His Leu Val Ala Val Ile Val Pro 545 550 555 560 Thr Asp Ala Ala Arg Ala Leu Glu Pro Ala Glu Arg Ile Ala Ala Ile 565 570 575 Thr Glu Ser Met Gln Arg Ile Ala Lys Glu Asn Gly Leu Glu Ser Tyr 580 585 590 Glu Ile Pro Arg Ala Phe Leu Leu Glu Asp Glu Pro Phe Thr Gln Asp 595 600 605 Asn Gly Leu Leu Ser Gly Ile Gly Lys Leu Leu Arg Pro Lys Phe Lys 610 615 620 Glu Arg Phe Gly Glu Arg Leu Glu Gln Leu Tyr Thr Glu Gln Ala Gln 625 630 635 640 Arg Gln Arg Asp Glu Leu Ala Val Leu Arg Arg Glu Ala Ala Asp Arg 645 650 655 Pro Val Ile Glu Thr Val Cys Arg Ala Ala Arg Ala Val Leu Gly Gly 660 665 670 Gly Glu Pro Gln Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser 675 680 685 Leu Ser Ala Leu Ser Phe Ser Thr Leu Leu Ala Glu Ile Phe Gly Val 690 695 700 Glu Val Pro Val Gly Val Ile Val Ser Pro Ala Asn Asn Leu Asp Arg 705 710 715 720 Leu Ala Ala His Ile Glu Ala Glu Arg Asp Ser Gly Gly Thr Arg Pro 725 730 735 Thr Val Ala Thr Ile His Gly Gly Lys Glu Ile Arg Ala Thr Asp Leu 740 745 750 Thr Leu Asp Lys Phe Leu Asp Ala Ala Thr Leu Ala Ala Ala Pro Ala 755 760 765 Leu Pro Arg Ala Ser Gln Pro Pro Arg Thr Val Leu Leu Thr Gly Ala 770 775 780 Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Gln Arg Leu 785 790 795 800 Asp Gly Thr Asp Gly Thr Leu Ile Cys Val Ile Arg Gly Arg Asp Ala 805 810 815 Glu Thr Ala Arg Arg Arg Leu Asp Glu Val Phe Asp Ser Gly Asp Pro 820 825 830 Glu Leu Leu Arg Arg Tyr Arg Glu Leu Ala Gln Arg Arg Leu Arg Val 835 840 845 Leu Pro Gly Asp Ile Gly Glu Pro Asn Phe Gly Leu Ser Gln Gln Asp 850 855 860 Trp Gln Glu Leu Ala Asp Thr Val Asp Leu Ile Val His Pro Ala Ala 865 870 875 880 Leu Val Asn His Val Leu Pro Tyr Gly Gln Leu Phe Gly Pro Asn Val 885 890 895 Val Gly Thr Ala Glu Val Ile Arg Leu Ala Leu Thr Ser Thr Leu Lys 900 905 910 Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala Ala Gln Ile Asp Pro 915 920 925 Ala Val Phe Thr Glu Asp Gly Asp Ile Arg Glu Ile Ser Ala Val Arg 930 935 940 Ser Val Asp Asp Gly Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala 945 950 955 960 Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val 965 970 975 Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Asp Phe Ala Gly 980 985 990 Gln Leu Asn Leu Pro Asp Met Phe Thr Arg Leu Leu Leu Ser Val Leu 995 1000 1005 Ala Thr Gly Leu Ala Pro Lys Ser Phe Tyr Ala Leu Asp Ser His 1010 1015 1020 Gly Asn Arg Arg Arg Ala His Tyr Asp Gly Leu Pro Ala Asp Phe 1025 1030 1035 Thr Ala Ala Ala Ile Thr Ala Leu Gly Ala Arg Val Thr Glu Gly 1040 1045 1050 Phe Glu Thr Tyr Asp Val Leu Asn Pro His Asp Asp Gly Ile Ser 1055 1060 1065 Leu Asp Glu Phe Val Asp Trp Leu Ile Glu Ser Gly His Ala Ile 1070 1075 1080 Asp Arg Ile Asp Asp Tyr Arg Asp Trp Phe Thr Arg Phe Glu Thr 1085 1090 1095 Ala Leu Arg Thr Leu Pro Glu His Gln Arg Gly Ala Ser Val Gln 1100 1105 1110 Pro Leu Leu His Ala Tyr Arg Arg Pro Gly Leu Pro Ile Ala Gly 1115 1120 1125 Ser Val Leu Pro Ala Lys Arg Phe Gln Ala Ala Val Gln Gln Ala 1130 1135 1140 Lys Leu Gly Pro Gly Gly Asp Ile Pro His Leu Thr Arg Glu Leu 1145 1150 1155 Ile Asp Lys Tyr Val Ala Asp Leu Lys Leu Arg Gly Leu Leu 1160 1165 1170 <210> 177 <211> 1054 <212> PRT <213> Artificial Sequence <220> <223> Acaromyces ingoldii <400> 177 Met Arg Leu Val Tyr Val Ile Glu Asn Ile Ile Lys Lys Tyr His Asp 1 5 10 15 Arg Pro Ala Ile Gly Glu Arg Val Lys Arg Cys Ile Lys Asp Ala Lys 20 25 30 Ser Lys Arg Ile Val Cys Gln Leu Thr Ala Lys Tyr Gln Thr Ile Thr 35 40 45 Tyr Gln Gln Leu Trp Ser Arg Ala Glu Ser Ile Ala Asn Glu Trp Tyr 50 55 60 Gln His Asp Gln Tyr Pro Leu Lys Ala Ser Asp Lys Val Ala Ile Leu 65 70 75 80 Ser Phe Ile His Ser Asp Tyr Ile Ala Ile Asn Leu Ala Cys Val Gln 85 90 95 Ile Asn Ala Ile Ile Val Pro Leu Gln Thr Asn Leu Ser Ile Lys Glu 100 105 110 Leu Thr Leu Ile Leu Gln Glu Ile Glu Pro Arg Ile Ile Ala Ala Ser 115 120 125 Ile Glu Tyr Leu Pro Ile Ala Val Glu Leu Ala Lys Asn Asn Asn Ser 130 135 140 Ile Lys Arg Ile Ile Val Phe Asp Tyr Asp Pro Ser His Asp Asn Ala 145 150 155 160 Glu Lys Leu Glu Gln Leu Gln Asn Gln Leu Ile Ile Lys Ile Glu Glu 165 170 175 Leu Pro Asn Ile Ile Arg Leu Gly Ser Gln Leu Pro Lys Val Pro Tyr 180 185 190 Pro Glu Asn Ser Asp Asp Thr Ser Ser Ile Ser Met Ile Ile Tyr Thr 195 200 205 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Ile Tyr Thr Glu Lys Phe 210 215 220 Val Ser Asn Met Trp Asp Ala Ser Leu Phe Ala Asn Asn Thr Asn Lys 225 230 235 240 Glu Asn Arg Thr Val Leu Tyr Leu Pro Ile Cys His Gly Leu Ala Ser 245 250 255 Gln Gln Leu Tyr Asn Gln Leu Ala Lys Gly Val Thr Cys Tyr Leu Val 260 265 270 Ala Lys Ser Asn Leu Ser Thr Leu Phe Glu Asp Ile Thr Leu Val Lys 275 280 285 Pro Thr Glu Leu Leu Leu Ile Pro Arg Val Ala Glu Met Ile Leu Gln 290 295 300 Leu Tyr Gln Ser Glu Leu Glu Gly Arg Lys Lys Thr Ile His Asp Pro 305 310 315 320 Leu Leu Asp Ser Lys Leu Lys Lys Glu Ile Arg Ile Asn Ile Phe Gly 325 330 335 Gly Arg Val Thr Gln Ile Phe Tyr Ser Ser Ala Pro Leu Thr Asn Lys 340 345 350 Leu Thr Asp Phe Ile Glu Ser Leu Phe Glu Val Lys Leu Leu Asn Met 355 360 365 Tyr Gly Ser Thr Glu Thr Leu Ala Ile Cys Ile Asn Asn Lys Ile Leu 370 375 380 Lys Pro Pro Val Glu Asp Tyr Lys Leu Ile Asp Val Pro Val Leu Gly 385 390 395 400 Tyr Tyr Ser Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Leu Leu Lys 405 410 415 Thr Ala Thr Ile Ile Pro Gly Tyr Tyr Lys His Pro Glu Leu Tyr Ser 420 425 430 Gln Leu Phe Asp Glu Gln Gly Tyr Tyr Met Thr Gly Asp Ile Val Lys 435 440 445 Glu Thr Ala Lys Asp His Leu Val Val Ile Glu Arg Lys Lys Asn Val 450 455 460 Ile Lys Leu Ser Gln Gly Glu Phe Ile Thr Thr Thr Met Leu Glu Thr 465 470 475 480 Leu Leu Lys Asp Ser Pro Leu Ile Lys Asp Ile Phe Ile Tyr Gly Asn 485 490 495 Ser Glu Trp Ser Tyr Leu Leu Ala Val Ile Ile Pro Ile Pro Glu Leu 500 505 510 Leu Tyr Arg Tyr Asn Lys Gln Gln Arg Glu Ile Lys Arg Leu Ile His 515 520 525 Gln Ser Leu Glu Lys Ile Ala Lys Asp Ser Gly Leu Lys Pro Tyr Glu 530 535 540 Val Pro Arg Asp Phe Leu Ile Asp Thr Glu Pro Phe Ser Gln Lys Asn 545 550 555 560 Gly Leu Leu Ser Glu Leu Gly Lys Pro Leu Lys Gln Lys Ile Glu Ala 565 570 575 His Tyr Ile Asp Asp Leu Asn Lys Leu Tyr Gln Glu Ile Cys Asn Tyr 580 585 590 Asp Phe Ser Lys Phe Ser Gln Gln Ile Asn Lys Glu Asn Ile Leu Glu 595 600 605 Thr Val Ile Lys Leu Thr Gln Tyr Leu Val Gly Ser Pro Gly Met Val 610 615 620 Ile Asn Ser Ala Ala Thr Phe Cys Gln Phe Gly Gly Asp Ser Leu Ser 625 630 635 640 Thr Leu Gln Phe Ser Leu Glu Leu Glu Lys Ile Trp Gly Val Met Ile 645 650 655 Pro Val Asp Met Ile Ala Asn Pro Thr Cys Thr Leu Asp Asp Ile Ala 660 665 670 Asp Tyr Ile Lys Ser Asn Gln His Ile Ile Asn Ser Cys Pro Thr Phe 675 680 685 Ala Thr Ile His Gly Ile Asp Lys Lys Lys Ile Tyr Ala Ser Gln Leu 690 695 700 Ala Leu Asp Lys Phe Ile Asp Pro Glu Ile Phe Gln Gln Ile Lys Asn 705 710 715 720 Ser Ser Arg Ser Leu Ser Ser Phe His Asn Val Leu Leu Thr Gly Ala 725 730 735 Asn Gly Tyr Leu Gly Lys Phe Leu Cys Leu Ala Leu Leu Glu Glu Leu 740 745 750 Asn Lys Thr Asp Gly Lys Leu Ile Cys Val Ile Arg Glu Lys Asp Asn 755 760 765 Glu Ser Ala Lys Gln Arg Leu Met Asn Thr Phe Ser Pro His Asn Asp 770 775 780 Gln Leu Ala Leu Lys Phe Lys Gln Leu Ala Asp Lys His Leu Thr Val 785 790 795 800 Tyr Ala Gly Asp Leu Thr Lys Pro Lys Leu Gly Leu Asp Glu Lys Thr 805 810 815 Trp His Tyr Leu Ser Gln Asn Ile Asp His Ile Phe His Ala Gly Ala 820 825 830 Leu Val Asn His Ile Leu Pro Tyr Gln His Leu Phe Glu Thr Asn Val 835 840 845 Leu Gly Thr Ala Glu Leu Ile Lys Leu Ala Leu Val Asn His Leu Lys 850 855 860 Pro Phe Ile Phe Ile Ser Ser Ile Ile Val Ala Ile Pro Ser Asp Asn 865 870 875 880 Thr Lys Pro Leu Asn Glu Asp Ala Asn Ile Cys Glu Ala Ile Pro Tyr 885 890 895 Gln Glu Ile Asn Asn Gln Tyr Ala Asn Gly Tyr Ala Ile Ser Lys Trp 900 905 910 Ala Ser Glu Ile Leu Leu Tyr Glu Ala Tyr Asn Arg Phe Lys Leu Pro 915 920 925 Val Thr Ile Phe Arg Pro Ser Met Ile Leu Ala His Arg Leu Tyr Asp 930 935 940 Thr Glu Phe Asn Ile Thr Asp Val Phe Thr Arg Leu Leu Leu Ser Ile 945 950 955 960 Ile Asn Thr Lys Ile Ala Pro Lys Ser Phe Tyr Gln Ser Asn Ser Asn 965 970 975 Leu Ser Pro His Tyr Asn Gly Leu Ala Val Asp Phe Val Val Ser Ser 980 985 990 Ile Ile Lys Leu Ser Lys Asn Asn His Asn Gln Arg Leu Thr Phe Asn 995 1000 1005 Met Val Asn Pro Gln Asn Asp Lys Val Ser Leu Asp Thr Ile Ile 1010 1015 1020 Asp Trp Leu Ile Asn Ser Gly Ile Asn Ile Lys Lys Ser Met Ile 1025 1030 1035 Met Lys Asn Gly Ile Asn Asn Leu Asn Trp Pro His Gly Lys Ile 1040 1045 1050 Thr <210> 178 <211> 1176 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. Leaf247 <400> 178 Met Thr Ser Thr Ile Thr Arg Glu His Asp Arg Ala Arg Lys Val Ser 1 5 10 15 Glu Arg Ile Ser Glu Leu Phe Ala Asp Asp Asp Glu Phe Arg Ala Ala 20 25 30 Ala Pro Asp Arg Ser Val Ser Asp Ala Ala Thr Glu Leu Ser Pro Asp 35 40 45 Leu Ile Arg Met Val Asp Glu Val Met Ser Arg Tyr Ala Ser Arg Pro 50 55 60 Ala Leu Gly Arg Arg Ala His Asp Val Thr Ala Asp Ala Asn Gly Arg 65 70 75 80 His Val Arg Ser Leu Leu Pro Arg Ile Asp Thr Val Thr Tyr Ala Asp 85 90 95 Leu Trp Ser Asp Ala Arg Ser Leu Ala Thr Ala Val Ala Asp Val Val 100 105 110 Thr Pro Gly Ser Phe Ile Ala Thr Leu Gly Phe Ala Ser Ala Glu Tyr 115 120 125 Val Val Ala Glu Leu Ala Thr Val Trp Ser Gly Ala Val Ser Val Pro 130 135 140 Leu Gln Ala Gly Ala Ala Ala Arg Arg Leu Val Asp Ile Thr Ala Glu 145 150 155 160 Val Glu Pro Val Val Leu Val Val Asp Ser Gly His Leu Pro Val Ala 165 170 175 Ser Asp Ile Val Ala Ala Cys Pro Thr Val Arg Arg Val Val Val Leu 180 185 190 Asp His Asp Ser Arg Val Asp Asp Asp Ala Asp Arg Leu Arg Thr Ala 195 200 205 Arg Glu Thr Val Ala Asp Ser Gly Val Val Val Glu Thr Leu Ala Glu 210 215 220 Ala Val Gln Arg Gly Ala Ala Ser Ala Pro Val Pro Arg Ala Glu Ser 225 230 235 240 Gly Asp Pro Glu Arg Ile Ala Thr Leu Val Tyr Thr Ser Gly Ser Thr 245 250 255 Gly Thr Pro Lys Gly Ala Ile His Thr Glu Arg Ile Val Ala Arg Gln 260 265 270 Trp Ser Thr Ala His Trp Tyr Ser Arg Ser Asp Asp Asp Ala Gly Glu 275 280 285 Asn Thr Pro Pro Val Ile Thr Leu Asp Tyr Leu Pro Met Ser His Leu 290 295 300 Ala Gly Arg Ala Leu Val Phe Thr Thr Leu Ala Ser Gly Gly Thr Val 305 310 315 320 His Phe Thr Ala Ser Ser Asp Leu Ser Thr Leu Leu Glu Asp Phe Ser 325 330 335 Leu Ala Arg Pro Thr Val Ala Met Leu Val Pro Arg Val Cys Asp Leu 340 345 350 Leu Arg Gln Thr Ala Leu Gly Arg Ile Asp Lys Glu Ala His Arg Thr 355 360 365 Gly Arg Ser Ala Asp Asp Val Arg Ser Glu Val Leu Ala Asp Met Arg 370 375 380 Ser Thr Thr Leu Gly Gly Arg Ile Leu Ser Ala Val Val Gly Thr Ala 385 390 395 400 Pro Thr Ser Pro Glu Val Val Glu Phe Met Ser Glu Leu Leu Glu Thr 405 410 415 Gln Val Gln Asn Asn Tyr Gly Ser Thr Glu Ala Gly Met Val Leu Phe 420 425 430 Asp Gly Val Val Gln Arg Pro Pro Val Thr Glu Tyr Arg Leu Asp Asp 435 440 445 Val Pro Glu Leu Gly Tyr Leu Thr Ser Asp Arg Pro His Pro Arg Gly 450 455 460 Glu Leu Leu Leu Lys Thr Thr Ser Leu Ile Pro Gly Tyr Tyr Lys Arg 465 470 475 480 Pro Asp Val Thr Ala Asp Met Leu Ser Asp Asp Gly Phe Tyr Arg Thr 485 490 495 Gly Asp Val Val Glu Glu Thr Ala Pro Asp His Leu Val Tyr Leu Asp 500 505 510 Arg Arg Lys Asn Val Leu Lys Leu Ala Gln Gly Glu Phe Val Ala Leu 515 520 525 Ser Arg Leu Glu Ser Ile Tyr Ala Ser Ala Asp Ala Val Asp Gln Ile 530 535 540 Phe Val His Gly Ser Gly Glu Arg Ala Tyr Leu Leu Ala Val Val Val 545 550 555 560 Pro Thr Asp Gly Ala Asp Ala Arg Glu Val Leu Ala Ser Val Gln Arg 565 570 575 Val Ala Arg Ala Glu Glu Leu Glu Ser Tyr Glu Ile Pro Arg Asp Val 580 585 590 Ile Leu Ala Asp Glu Pro Phe Thr Val Ala Asn Gly Leu Leu Ser Gly 595 600 605 Ala Asn Lys Gln Leu Arg Pro Ala Leu Thr Asp Thr Tyr Gly Ala Ala 610 615 620 Leu Glu Ala Arg Tyr Arg Asp Ile Asp Glu Gly Gln Ser Thr Lys Leu 625 630 635 640 Gly Glu Leu Arg Arg Arg Gly Pro Gly Ala Pro Val Ala Glu Thr Val 645 650 655 Ala Glu Ala Ala Ala Ala Leu Leu Gly Cys Ala Asp Thr Asp Val Glu 660 665 670 Pro Ser Ala Arg Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu 675 680 685 Thr Phe Ala Thr Val Leu His Asp Ile Phe Asp Ile Asp Val Pro Val 690 695 700 Ser Val Val Ile Ser Pro Thr Ser Asp Leu Ala Ala Val Ala Ala Tyr 705 710 715 720 Ile Glu Lys Thr Val Ala Ser Asp Ser Gly Thr Thr Thr Phe Ala Ser 725 730 735 Val His Gly Arg Gly Ala Thr Glu Val His Ala Asp Asp Leu Arg Pro 740 745 750 Asp Ala Phe Phe Asp Ala Glu Phe Leu Ser Ala Ala Glu Ser Ala Asp 755 760 765 Pro Val Arg Thr Glu Val Ser Thr Val Leu Leu Thr Gly Ala Asn Gly 770 775 780 Tyr Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Glu Arg Met Ala Ala 785 790 795 800 Val Asp Gly Thr Leu Leu Cys Val Val Arg Gly Arg Asp Ala Asp Asp 805 810 815 Ala Arg Ala Arg Leu Asp Ala Ala Phe Asp Ser Gly Asp Asp Glu Leu 820 825 830 Thr Ala Arg Tyr Arg Ala Leu Ala Glu Thr Thr Leu Gln Val Val Ala 835 840 845 Gly Asp Val Gly Asp Pro Met Phe Gly Met Ser Pro Glu Ala Trp Thr 850 855 860 Ala Leu Cys Thr Gly Val Asp Arg Ile Val His Pro Ala Ala Leu Val 865 870 875 880 Asn His Ala Leu Pro Tyr Glu Gln Leu Phe Gly Ser Asn Val Val Gly 885 890 895 Thr Ala Glu Val Ile Arg Leu Ala Leu Thr Asp His Val Lys Pro Val 900 905 910 Thr Tyr Leu Ser Thr Val Ala Val Ala Ala Gly Val Thr Asp Phe Val 915 920 925 Glu Asp Gly Asp Ile Arg Asp Val Ser Pro Ser Arg Pro Val Asp Gln 930 935 940 Ser Tyr Ala Asn Gly Tyr Gly Thr Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Asn Ala Phe Asp Arg Phe Ser Leu Pro Val Thr Val Phe Arg 965 970 975 Ser Asp Met Ile Leu Ala His Pro Arg Trp Thr Gly Gln Leu Asn Val 980 985 990 Pro Asp Ile Phe Thr Arg Thr Ile Leu Ser Val Ile Ala Thr Gly Ile 995 1000 1005 Ala Pro Glu Thr Phe Tyr Arg Thr Asp Thr Gly Val Pro Thr Asp 1010 1015 1020 Asp Ala Gly Arg Pro Arg Gly His Tyr Asp Gly Leu Pro Ala Asp 1025 1030 1035 Phe Thr Ala Ser Ala Ile Thr Glu Leu Gly Ser Arg Gly Val Asp 1040 1045 1050 Gly Tyr Arg Thr Phe Asp Ile Ile Asn Pro His Asp Asp Gly Val 1055 1060 1065 Ser Leu Asp Thr Val Val Asp Trp Ile Val Asp Ser Gly Arg Thr 1070 1075 1080 Ile Arg Arg Ile Ser Asp His Asp Glu Trp Phe Arg Glu Phe Ser 1085 1090 1095 Asp Ala Leu Ala Ala Leu Pro Ala Ser Gln Arg Thr His Ser Val 1100 1105 1110 Leu Pro Leu Val His Ala Tyr Ala His Pro Asp Thr Pro Thr Pro 1115 1120 1125 Gly Ser Pro Leu Pro Ala Glu Val Phe Arg Ala Ala Val Lys Glu 1130 1135 1140 Ala Gly Leu Gly Asp Ala Gly Glu Ile Pro His Val Thr Lys Asp 1145 1150 1155 Leu Ile Glu Lys Tyr Val Arg Asp Leu Glu Ser Leu Gly Leu Leu 1160 1165 1170 Ser Ala Arg 1175 <210> 179 <211> 1145 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces sp. Root1310 <400> 179 Met Pro Val Ala Gly Val His Glu Glu Ser Ala Gly Arg Arg Pro Arg 1 5 10 15 Leu Ser Glu Ile Val Arg Arg Ala Leu Ala Ala Tyr Ala Glu Arg Pro 20 25 30 Ala Leu Gly Glu Arg Ala Arg Gln Tyr Val Ser Val Asp Gly Arg Val 35 40 45 Thr Val Arg Leu Leu Pro Arg Phe Asp Thr Val Ser Tyr Gly Glu Leu 50 55 60 Trp Ser Arg Leu Ser Ala Val Ala Ala Asp Trp Tyr His His Pro Gln 65 70 75 80 His Pro Leu Arg Glu Gly Asp Phe Val Ala Ile Leu Gly Phe Ala Gly 85 90 95 Thr Asp Tyr Thr Thr Val Asp Leu Ala Cys Gly Gln Val Gly Ala Val 100 105 110 Ala Val Pro Leu His Thr Asn Ala Ser Val Asp His Ile Arg His Leu 115 120 125 Val Ala Glu Ala Ala Pro Arg Val Phe Ala Thr Ser Thr Asp Arg Leu 130 135 140 Ala Thr Val Leu Glu Ala Leu Ser Gly Gln Thr Cys Val His Arg Ile 145 150 155 160 Leu Val Phe Asp His His Pro Glu Leu Ala Glu His Arg Glu Ala Leu 165 170 175 Ala Ala Ala Gly Arg Leu Leu Ala Thr Thr Gly Ala Pro Met Ser Leu 180 185 190 Glu Leu Leu Ser Asp Val Val Gly Arg Ala Gly Ser Leu Pro Pro Val 195 200 205 Pro Glu Leu Pro Pro Asp Ser Ser Ala Asp Gly Ala Leu Ser Ala Leu 210 215 220 Val Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Val Met Phe Pro 225 230 235 240 Glu Ser Thr Val Ala Leu Met Trp Arg Pro Pro Glu Gly Pro Asp Asn 245 250 255 Arg Tyr Pro Leu Ile Thr Ala Asn Phe Leu Pro Gln Ser His Leu Val 260 265 270 Ala Arg Arg Leu Val Ile Lys Thr Leu Ala Thr Gly Gly Thr Ala Asn 275 280 285 Phe Val Ala Arg Ser Asp Leu Ser Thr Leu Leu Asp Asp Leu Ala Leu 290 295 300 Ile Arg Pro Thr Glu Ile Ala Met Val Pro Arg Val Cys Glu Leu Leu 305 310 315 320 Phe Glu Ser Tyr His Ala Arg Leu Asn Gln Arg Ala Ala Asn Gly Glu 325 330 335 Leu Arg Asp Ala Asp His Ala Glu Val Ile Ala His Leu Arg Asp His 340 345 350 Val Leu Gly Gly Arg Val Ile His Ala Pro Cys Gly Ser Ala Pro Leu 355 360 365 Ala Pro Glu Leu Ala Ala Phe Leu Arg Asp Ala Leu Asp Val Pro Leu 370 375 380 Leu Asp Ser Tyr Gly Thr Thr Glu Thr Gly Leu Val Met Leu Asp His 385 390 395 400 Arg Val Gln Ser Pro Pro Val Leu His Tyr Lys Leu Ala Asp Val Pro 405 410 415 Glu Leu Gly Tyr Ser Thr Ala Asp Ser Pro His Pro Arg Gly Glu Leu 420 425 430 Leu Val Arg Thr Ala Leu Ile Thr Pro Gly Tyr Tyr Arg Arg Ala Glu 435 440 445 Glu Thr Ala Glu Val Phe Asp Gln Asp Gly Tyr Tyr Arg Thr Gly Asp 450 455 460 Ile Met Ala Glu Thr Ala Pro Gly Glu Leu Val Tyr Val Asp Arg Arg 465 470 475 480 Lys Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Leu Ser Lys 485 490 495 Val Glu Ala Ala Leu Val Ala Ser Pro Leu Val Arg Gln Ile Phe Val 500 505 510 Tyr Gly Asn Ser Ser Arg Ala Tyr Leu Leu Ala Val Val Val Pro Thr 515 520 525 Pro Glu Ala Ile Ala Gln Ala Gly Asp Gly Ala Ala Leu Lys Ala Glu 530 535 540 Val Ser Arg Ser Leu Gln Ser Val Ala Ala Gln Ala Gly Leu Ala Pro 545 550 555 560 Tyr Glu Val Pro Arg Asp Leu Ile Val Glu Thr Val Pro Phe Ser Gln 565 570 575 Asp Asn Gly Leu Leu Thr Asp Ser Thr Lys Gln Leu Arg Pro Arg Leu 580 585 590 Lys Glu Arg Tyr Gly Glu Arg Leu Glu Arg Arg Tyr Ala Glu Leu Ala 595 600 605 Ala Gly Gln Ser Ala Glu Leu Arg Ala Val Trp Gln Glu Arg Asp Arg 610 615 620 Pro Val Ala Glu Thr Val Ala Arg Ala Ala Gln Ala Leu Leu Ala Gly 625 630 635 640 Leu Asp Val Glu Pro Gly Pro Glu Arg Arg Phe Thr Glu Leu Gly Gly 645 650 655 Asp Ser Leu Ser Ala Leu Ser Phe Ala Asn Leu Leu Arg Glu Ile Phe 660 665 670 Gly Val Glu Val Ser Val Gly Thr Leu Leu Gly Pro Ala Asn Ser Leu 675 680 685 Glu Gln Ile Ala Gly His Val Glu Arg Leu Arg Gly Thr Ala Thr Ala 690 695 700 Arg Arg Ala Thr Phe Ala Ser Val His Gly Glu His Ala Thr Ser Val 705 710 715 720 Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Ala Thr Leu 725 730 735 Ala Ala Cys Thr Ala Leu Pro Arg Pro Ala Gly Glu Pro Arg Thr Val 740 745 750 Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Leu Leu Cys Leu Glu 755 760 765 Trp Leu Gln Arg Leu Ala Pro Val Gly Gly Thr Leu Val Cys Leu Val 770 775 780 Arg Ala Ala Asp Asp Ser Ala Ala Arg Gln Arg Leu Glu Glu Ala Leu 785 790 795 800 Asp Ser Gly Asp Thr Ala Leu Lys Ser Arg Phe Ala Glu Leu Thr Ala 805 810 815 Asp Gly Ala Leu Arg Val Leu Ala Gly Asp Ile Gly Ala Thr Arg Leu 820 825 830 Gly Leu Ser Glu Gln Asp Trp Gln Gln Leu Thr Ala Thr Val Asp Leu 835 840 845 Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Arg Gln 850 855 860 Leu Phe Glu Pro Asn Val Ala Gly Thr Ala Glu Val Val Arg Ala Ala 865 870 875 880 Leu Thr Thr Arg Leu Lys Pro Val Val Tyr Val Ser Thr Val Ala Leu 885 890 895 Ala Ala His Gly Ala Ala Thr Ala Asp Glu Asp Thr Asp Ile Arg Val 900 905 910 Gly His Pro Gly His Ala Ile Asp Asp Ser His Ala Gly Gly Tyr Ala 915 920 925 Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu 930 935 940 Cys Gly Leu Pro Val Thr Val Leu Arg Ser Gly Met Ile Leu Ala His 945 950 955 960 Ala Arg Tyr Ala Gly Gln Leu Asn Val Pro Asp Ala Phe Thr Arg Leu 965 970 975 Leu Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Asp Ser Phe Tyr Asp 980 985 990 Gly Ala Glu Gly Gly Arg Arg Pro Arg Ala His Tyr Asp Gly Leu Pro 995 1000 1005 Gly Asp Phe Val Ala Ala Ala Val Ala Ala Leu Gly Phe Arg Thr 1010 1015 1020 Ala Gly Phe Arg Thr Phe Asn Val Val Asn Pro His Asp Asp Gly 1025 1030 1035 Val Ser Leu Asp Thr Val Val Asp Trp Leu Thr Asp Cys Gly Ile 1040 1045 1050 Thr Val Arg Arg Val Gly Gly His Arg Lys Trp Arg Glu Gln Phe 1055 1060 1065 Glu Ala Ala Leu Arg Thr Leu Pro Gln Ala Gln Arg Pro Tyr Ser 1070 1075 1080 Leu Leu Pro Leu Met Ala Ala Trp Arg Glu Pro Leu Val Pro Arg 1085 1090 1095 Thr Thr Ser Ala Leu Pro Ala Glu Arg Phe Arg Ala Ala Val Arg 1100 1105 1110 Thr Ala Gly Ile Gly Ala Glu Gln Asp Ile Pro His Leu Ser Arg 1115 1120 1125 Ser Leu Ile Glu Lys Tyr Val Ala Asp Leu Arg His Leu Gly Leu 1130 1135 1140 Ile Ser 1145 <210> 180 <211> 1181 <212> PRT <213> Artificial Sequence <220> <223> Sphingobium sp. MI1205 <400> 180 Met Ala Thr Glu Phe Asp Gln Ser His Leu Val Glu Lys Ala Val Ala 1 5 10 15 Arg Val Gln Gln Met Ser Ile Ser Asp Pro Glu Met Ala Ala Arg Ile 20 25 30 Pro Asp Pro Lys Val Thr Glu Ala Ile Lys Asp Pro Ala Leu Ser Tyr 35 40 45 Arg Gln Ile Ile Ala Thr Val Leu Glu Gly Tyr Ala Asp Arg Pro Ala 50 55 60 Phe Gly Ser Arg His Tyr Thr Leu Glu Gln Asp Ala Ala Gly Arg Thr 65 70 75 80 Val Arg Arg Tyr Asp Met Arg Phe Asp Thr Ile Ser Tyr Gly Glu Leu 85 90 95 Arg Arg Gln Val Glu Gly Ile Ala Asn Leu Trp Lys His His Pro Asp 100 105 110 His Arg Ala Ala Pro Gly Asp Lys Ile Ser Phe Ile Ala Phe Thr Gly 115 120 125 Ala Glu Met Ala Ala Val Asp Leu Ala Cys Asn Tyr Ala Gln Thr Val 130 135 140 Ser Val Pro Leu Gln Ala Asn Leu Pro Ala Pro Asp Met Arg Gln Ile 145 150 155 160 Leu Thr Asp Val Ala Pro Thr Val Leu Ala Ala Ser Ile Asp Asn Leu 165 170 175 Glu Leu Ala Val Gly Tyr Ala Ile Asp Gln Asp Thr Ile Arg Ser Leu 180 185 190 Ile Val Leu Asp Ala Asp Glu Arg Val Asp Asp Asp Arg Asp Ala Ile 195 200 205 Ala Ala Ala Arg Ala Thr Leu Ala Lys Ala Gly Gly Arg Val Ala Leu 210 215 220 Ile Thr Phe Asp Ala Ala Val Asp Tyr Gly Ser Ile His Glu Phe Gln 225 230 235 240 Pro Leu Ala Glu Thr Thr Pro Asp His Val Ser Met Ile Met Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Lys Pro Lys Gly Ala Ile Ile His Asp Ala Ile 260 265 270 Ser Ser Gln Phe Trp Asn Glu Thr Ile Pro Ala Tyr Arg Pro Thr Val 275 280 285 Gln Val Ala Tyr Ala Pro Met Asn His Phe Met Gly Arg Thr Met Val 290 295 300 His Ser Thr Leu Ala Gln Gly Gly Thr Ala Asn Phe Thr Leu Arg Ser 305 310 315 320 Asp Met Ser Thr Leu Phe Asp Asp Phe Arg Ile Thr Arg Pro Thr Met 325 330 335 Ile Leu Phe Ile Pro Arg Val Cys Glu Leu Ile Tyr Gln His Tyr Gln 340 345 350 Ser Glu Val Gln Arg Arg Val Thr Leu Gly Glu Lys Glu Ala Met Ala 355 360 365 Asp Ala Ala Val Arg Gln Glu Met Arg Ala Ser Tyr Leu Gly Asp Arg 370 375 380 Leu Cys Gly Gly Gly Val Gly Ser Ser Pro Thr Ala Pro Glu Val Arg 385 390 395 400 Arg Phe Ile Ala Glu Cys Trp Glu Met Pro Leu Val Glu Gly Tyr Gly 405 410 415 Gln Thr Glu Ala Gly Ala Ala Ala Met Thr Ser Glu Asn Arg Leu Thr 420 425 430 Ser Asn Met Ile Thr Glu Phe Lys Leu Val Asp Val Pro Glu Leu Gly 435 440 445 Tyr Phe Thr Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Tyr Val Lys 450 455 460 Thr Ser Lys Met Phe Gln Gly Tyr Phe Lys Arg Pro Glu Ala Thr Ala 465 470 475 480 Ala Val Phe Ser Glu Asp Asn Phe Leu Lys Thr Gly Asp Ile Met Glu 485 490 495 Gln Arg Gly Pro Asp His Leu Val Trp Val Asp Arg Arg Gly Asn Val 500 505 510 Ile Lys Leu Ser Gln Ala Glu Phe Val Ala Val Gly Pro Leu Glu Thr 515 520 525 Thr Tyr Leu Gly Asn Ser Ser Leu Ile Glu Gln Ile Phe Val Tyr Gly 530 535 540 Ser Ser Tyr Arg Ser Tyr Leu Leu Ala Val Val Val Pro Asp Leu Ser 545 550 555 560 Val Ala Arg Ala Met Leu Gly His Asp Pro Asn Glu Ala Glu Leu Arg 565 570 575 Glu Leu Ile Leu Ser Glu Phe Lys Thr Val Ala Arg Lys Ala Glu Leu 580 585 590 Lys Asn Phe Glu Ile Pro Arg Asp Val Leu Ile Glu His Glu Arg Phe 595 600 605 Thr Tyr Glu Asn Gly Leu Leu Ser Ser Ala Arg Lys Pro Leu Arg Pro 610 615 620 Asn Ile Lys Arg Lys Tyr Val Asp Gln Leu Glu Ser Met Tyr Glu Glu 625 630 635 640 Met Asp Lys Gln Gln Gln Val Glu Leu Ala Arg Leu Arg Ala Ser Ala 645 650 655 Asp Gly Thr Thr Ala Glu Arg Val Ala Gly Ala Phe Lys Ala Asn Leu 660 665 670 Gly Leu Pro Gln Val Asp Ala Asp Asn Pro Arg Ser Tyr Gly Asp Leu 675 680 685 Gly Gly Asp Ser Leu Gly Ala Val Gly Leu Ser Leu Leu Phe Glu Glu 690 695 700 Met Phe Gly Val Thr Val Pro Val Ser Ala Ile Leu His Pro Ala Ala 705 710 715 720 Thr Val Gln Trp Leu Ala Glu His Val Asp Arg Ala Gln Ser Gly Glu 725 730 735 Thr Val Arg Met Ser Asp Val His Pro Asp Pro Asp Leu Leu Arg Pro 740 745 750 Ser Asp Leu Lys Leu Tyr Lys Met Ile Asp Glu Ala Leu Leu Thr Asp 755 760 765 Ala Ser His Ala Ala Pro Pro Ala Ala Glu Ala Lys Asn Val Leu Val 770 775 780 Thr Gly Ala Asn Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu 785 790 795 800 Glu His Val Ala Pro Arg Gly Gly Thr Val Tyr Cys Leu Ala Arg Gly 805 810 815 Lys Thr Glu Ala Glu Ala Arg Ala Arg Leu Glu Ala Ala Phe Asp Arg 820 825 830 Gly Asp Ala Ala Leu Leu Ala Arg Phe Arg Gln Leu Ala Asp Arg His 835 840 845 Leu Arg Val Leu Cys Gly Asp Leu Ala Glu Lys Arg Phe Gly Leu Asp 850 855 860 Ser Glu Thr Tyr Asp Met Leu Thr Arg Glu Leu Asp Gln Ile Val His 865 870 875 880 Ser Ala Ala Leu Val Asn His Arg Leu Ser Tyr Ala Asn Leu Phe Ala 885 890 895 Pro Asn Val Leu Gly Thr Ala Glu Leu Ile Ala Leu Ala Leu Thr Ser 900 905 910 Lys Leu Lys Arg Phe Asp Tyr Ile Ser Thr Val Gly Val Pro Ala Leu 915 920 925 Leu Pro Ser Leu Thr Gly Ala Pro Glu Ala Thr Asp Val Arg Asp Val 930 935 940 Pro Asp Pro Val Arg Leu Ser Asp Gly Tyr Ala Asn Gly Tyr Ala Ala 945 950 955 960 Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala Asn Glu Leu Phe 965 970 975 Gly Leu Pro Val Asn Ile Phe Arg Pro Asn Met Ile Leu Pro His Arg 980 985 990 Asn Tyr Ser Gly Gln Tyr Asn Glu Thr Asp Met Ile Thr Arg Leu Leu 995 1000 1005 Phe Ser Leu Val Lys Thr Gly Leu Ala Pro Lys Ser Phe Tyr Ala 1010 1015 1020 Leu Asp Ala Asn Gly Asn Arg Pro Arg Ala His Tyr Asp Gly Leu 1025 1030 1035 Pro Val Asp Phe Leu Ala Ala Met Ile Arg Glu Val Gly Ala Glu 1040 1045 1050 Pro Tyr Thr Gly Phe Gln Ser Phe Asn Met Val Asn Asp His Asp 1055 1060 1065 Asp Gly Tyr Ser Leu Asp Ser Phe Ala Asp Trp Ile Glu Ser Ala 1070 1075 1080 Gly Tyr Arg Val Asp His Ile Ala Asp His Ser Ala Trp Ala Glu 1085 1090 1095 Arg Phe Glu Gly Lys Leu Arg Asn Leu Ser Glu Glu Asp Arg Gln 1100 1105 1110 Asn Ser Ser Ile Asn Ile Leu Ala His Phe Ala Gln Pro His Glu 1115 1120 1125 Ala Arg Glu Ser Pro Leu Asp Ser Ser Asp Phe Ala Lys Arg Val 1130 1135 1140 Lys Ser Leu Lys Val Gly Pro Val Met Pro His Leu Asp Glu Ala 1145 1150 1155 Tyr Ile His Lys Tyr Leu Ala Asp Met Gln Lys Arg Gly Leu Ile 1160 1165 1170 Ala Glu Pro Glu Ala Val Ala Ala 1175 1180 <210> 181 <211> 1132 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces yunnanensis <400> 181 Met Ala Glu Ile Met Glu Arg Tyr Ala Asp Arg Pro Ala Val Gly Glu 1 5 10 15 Arg Ala Arg Glu Phe Val Arg Asp Pro Glu Ser Gly Arg Leu Ser Leu 20 25 30 Asn Leu Leu Pro Arg Tyr Glu Leu Met Thr Phe Gly Glu Leu Trp Gly 35 40 45 Arg Ile Arg Ser Val Ala Ala Glu Trp His His His Pro Glu Ser Pro 50 55 60 Leu Arg Ala Gly Glu Arg Val Val Phe Leu Gly Phe Ser Ser Ile Glu 65 70 75 80 Tyr Ser Val Val Asp Leu Ala Cys Val His Leu Gly Ala Val Gly Val 85 90 95 Pro Leu Gln Thr Ser Ser Pro Val Ala Gln Leu Gly Ala Ile Val Glu 100 105 110 Glu Thr Glu Pro Ala Met Met Ala Thr Ser Leu Glu Arg Leu Asp Thr 115 120 125 Ala Val Glu Leu Thr Leu Lys Ser Pro Ser Val Arg Arg Ile Val Val 130 135 140 Phe Asp His Arg Pro Gln Leu Val Glu Glu Thr Glu Ala Phe Ala Ala 145 150 155 160 Ala Arg Glu Arg Leu Val Arg Gly Gly His Ala Ala Met Leu Asp Ala 165 170 175 Leu Pro Asp Ile Val Asp Arg Gly Ser Ala Leu Pro Ala Ala Pro Leu 180 185 190 Tyr Thr Pro Asp Asp Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 195 200 205 Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Arg Leu 210 215 220 Ala Ser Ala Met Trp Gly Gly Ala Trp Ala Lys Leu Phe Ser Asp Glu 225 230 235 240 His Ala Val Thr Phe His Tyr Met Pro Met Ser His Val Ala Gly His 245 250 255 Ser Ser Leu Lys Asn Thr Leu Ala Arg Gly Gly Ile Thr Tyr Phe Thr 260 265 270 Ala Ala Ser Asp Leu Ser Thr Phe Phe Asp Asp Ile Ala Leu Ala Arg 275 280 285 Pro Thr Glu Ile Ser Leu Val Pro Arg Val Cys Glu Met Leu Phe Gln 290 295 300 Lys Tyr Arg Ser Glu Leu Gly Pro Tyr Leu Gly Glu Gly Gly Gly Asp 305 310 315 320 Gly Asp Ser Asp Thr Val Gly Ala Glu Val Arg Lys His Met Arg Glu 325 330 335 Asn Ile Leu Gly Gly Arg Ile Ala Trp Ala Ser Cys Gly Ser Ala Pro 340 345 350 Leu Ser Asp Glu Leu Arg Glu Phe Val Glu Ser Leu Leu Gly Phe Asp 355 360 365 Leu Asn Ile Ile Tyr Gly Ser Thr Glu Ala Ala Ala Ile Ser Val Asn 370 375 380 Gly Glu Leu Ile Arg Pro Pro Val Val Asp Tyr Lys Leu Leu Asp Val 385 390 395 400 Pro Glu Leu Gly Tyr Phe Gly Thr Asp Thr Pro Tyr Pro Arg Gly Glu 405 410 415 Leu Leu Leu Lys Thr Asp Ala Ile Ile Pro Gly Tyr Tyr Lys Gln Pro 420 425 430 Glu Leu Ser Ala Glu Leu Leu Asp Asp Asp Gly Tyr Tyr Arg Thr Gly 435 440 445 Asp Ile Val Ala Glu Phe Ala Pro Gly Arg His Ser Val Val Asp Arg 450 455 460 Arg Asn Ser Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Thr Thr 465 470 475 480 His Leu Glu Ala Val Phe Ser Val Ser Pro Leu Val Arg Gln Ile Phe 485 490 495 Val Tyr Gly Asn Gly Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 500 505 510 Ser Gly Pro Leu Ala Glu Phe Gly Gly Glu Glu Glu Phe Arg Gly Leu 515 520 525 Leu Arg Asp Ser Phe Gln Arg Ile Ala Arg Asp Gln Gly Leu Asn Ser 530 535 540 Tyr Glu Ile Pro Arg Gly Phe Leu Val Glu Thr Glu Pro Phe Ser Gln 545 550 555 560 Ala Asn Gly Leu Leu Ser Asp His Arg Lys Arg Arg Arg Pro Gln Leu 565 570 575 Val Gln Arg Tyr Arg Glu Arg Leu Glu Ala Leu Tyr Ser Ala Ile Ala 580 585 590 Ala Glu Glu Ala Asp Glu Leu Thr Thr Val Arg Arg Leu Gly Ala Thr 595 600 605 Arg Pro Val Leu Glu Thr Val Gln Arg Ala Ala Arg Ala Leu Leu Gly 610 615 620 Gly Ala Leu Thr Glu Val Ser Pro Asp Ala His Phe Arg Asp Leu Gly 625 630 635 640 Gly Asp Ser Leu Ser Ala Val Ser Phe Ala Asn Leu Leu Arg Asp Thr 645 650 655 Phe Asp Val Arg Val Pro Val Asp Leu Val Ile Ser Pro Ala Thr Asp 660 665 670 Leu Arg Gln Leu Ala Ala His Ile Glu Ala Lys Arg Ala Ala Gly Pro 675 680 685 Pro Gln Val Thr Tyr Ala Ser Val His Gly Ala Glu Ser Pro Glu Val 690 695 700 His Ala Ala Asp Leu Thr Leu Glu Lys Phe Ile Asp Ala Asp Thr Val 705 710 715 720 Glu Ala Ala Gly Ser Leu Pro Arg Pro Ala Asp Glu Pro Arg Thr Val 725 730 735 Leu Leu Thr Gly Ala Ser Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu 740 745 750 Trp Leu Glu Arg Leu Ser Arg Thr Gly Gly Arg Leu Val Cys Val Val 755 760 765 Arg Gly Gly Ser Ala Val Ala Ala Arg Lys Arg Leu Asp Glu Ala Leu 770 775 780 Ser Ser Gly Asp Gln Thr Leu Thr Arg Arg Phe Gln Glu Leu Ala Asp 785 790 795 800 Ala His Leu Glu Val Val Ala Gly Glu Leu Ala Glu Pro Arg Leu Gly 805 810 815 Leu Asp Glu Glu Thr Trp Arg Arg Leu Ala Asp Glu Val Asp Thr Ile 820 825 830 Val His Ala Gly Ala Leu Val Asn His Val Leu Pro Tyr Gln His Leu 835 840 845 Phe Asp Ala Asn Val Val Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu 850 855 860 Thr Gly Arg Leu Lys Pro Phe Thr Tyr Val Ser Ser Val Ala Val Ala 865 870 875 880 Thr Ser Trp Thr Gly Gly Pro Ala Leu Asp Glu Asp Ser Asp Val Arg 885 890 895 Ala Ala Val Pro Val Gln Arg Val Glu Glu Gly Tyr Ala Ser Gly Tyr 900 905 910 Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 915 920 925 Arg Cys Gly Leu Pro Val Thr Thr Phe Arg Ser Asn Met Ile Leu Ala 930 935 940 His Ser Arg Tyr Pro Gly Gln Leu Asn Val Pro Asp Ala Phe Thr Arg 945 950 955 960 Leu Leu Phe Ser Leu Val Ala Thr Gly Ile Ala Pro His Thr Phe Tyr 965 970 975 Arg Ala Asp Glu Thr Gly Arg Pro Glu Arg Ala His Tyr Asp Gly Leu 980 985 990 Pro Val Asp Phe Thr Ala Thr Ala Val Val Ala Leu Gly Ala His Ala 995 1000 1005 Ala Thr Gly Tyr Arg Thr Phe Ser Leu Val Asn Pro His Asp Asp 1010 1015 1020 Gly Ile Ser Leu Asp Thr Phe Val Asp Trp Leu Asn Glu Ala Gly 1025 1030 1035 His Arg Ile Asp Arg Val Ala Asp Tyr Asp Gly Trp Leu Leu Arg 1040 1045 1050 Phe Glu Ser Ala Leu Arg Ala Leu Pro Glu Gln Arg Arg Gln His 1055 1060 1065 Ser Leu Leu Pro Leu Leu His Gly Tyr Ala Ser Pro Glu Pro Val 1070 1075 1080 Val Pro Gly Ser Ala Ile Pro Ser Thr Arg Phe Arg Ala Ala Val 1085 1090 1095 Leu Asn Ala Gly Ile Gly Gln Asp Gly Asp Ile Pro Arg Val Ser 1100 1105 1110 Ala Glu Leu Ile Arg Lys Tyr Ala Asp Asp Leu Arg Pro Phe Leu 1115 1120 1125 Ala Ala Gln Asp 1130 <210> 182 <211> 1174 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. KMS <400> 182 Met Ser Thr Glu Thr Arg Glu Ala Arg Leu Gln Gln Arg Ile Ala His 1 5 10 15 Leu Phe Ala Thr Asp Pro Gln Phe Ala Ala Ala Arg Pro Asp Pro Arg 20 25 30 Ile Ser Asp Ala Val Asp Arg Asp Asp Ala Arg Leu Thr Ala Ile Val 35 40 45 Ser Ala Val Met Ser Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Ala Glu Phe Val Thr Asp Pro Gln Thr Gly Arg Thr Thr Met Glu 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Arg Glu Leu Leu Asp Arg 85 90 95 Val Arg Ala Leu Thr Asn Ala Trp His Ala Asp Gly Val Arg Pro Gly 100 105 110 Asp Arg Val Ala Ile Leu Gly Phe Thr Gly Ile Asp Tyr Thr Val Val 115 120 125 Asp Leu Ala Leu Ile Gln Leu Gly Ala Val Ala Val Pro Leu Gln Thr 130 135 140 Ser Ala Ala Val Glu Ala Leu Arg Pro Ile Val Ala Glu Thr Glu Pro 145 150 155 160 Met Leu Ile Ala Thr Gly Val Asp His Val Asp Ala Ala Ala Glu Leu 165 170 175 Ala Leu Thr Gly His Arg Pro Ser Arg Val Val Val Phe Asp His Arg 180 185 190 Glu Gln Val Asp Asp Glu Arg Asp Ala Val Arg Ala Ala Thr Ala Arg 195 200 205 Leu Gly Asp Ala Val Pro Val Glu Thr Leu Ala Glu Val Leu Arg Arg 210 215 220 Gly Ala His Leu Pro Ala Val Ala Pro His Val Phe Asp Glu Ala Asp 225 230 235 240 Pro Leu Arg Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 245 250 255 Gly Ala Met Tyr Pro Glu Ser Lys Val Ala Gly Met Trp Arg Ala Ser 260 265 270 Ala Lys Ser Ala Trp Asn Asn Asp Gln Thr Ala Ile Pro Ser Ile Thr 275 280 285 Leu Asn Phe Leu Pro Met Ser His Val Met Gly Arg Gly Leu Leu Cys 290 295 300 Gly Thr Leu Ser Thr Gly Gly Thr Ala Tyr Phe Ala Gly Arg Ser Asp 305 310 315 320 Leu Ser Thr Leu Leu Glu Asp Leu Arg Leu Val Arg Pro Thr Gln Leu 325 330 335 Ser Phe Val Pro Arg Ile Trp Asp Met Leu Phe Gln Glu Phe Val Gly 340 345 350 Glu Val Asp Arg Arg Val Asn Asp Gly Ala Asp Arg Pro Thr Ala Glu 355 360 365 Ala Asp Val Leu Ala Val Gln Arg Arg Glu Leu Leu Gly Gly Arg Phe 370 375 380 Val Thr Ala Met Thr Gly Ser Ala Pro Ile Ser Leu Glu Met Lys Thr 385 390 395 400 Trp Val Glu Asn Leu Leu Asp Met His Leu Val Glu Gly Tyr Gly Ser 405 410 415 Thr Glu Ala Gly Ala Val Phe Val Asp Gly His Ile Gln Arg Pro Pro 420 425 430 Val Leu Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe Ser 435 440 445 Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Val Arg Cys Thr Gln 450 455 460 Leu Phe Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Glu Val Phe 465 470 475 480 Asp Asp Asp Gly Phe Tyr Arg Thr Gly Asp Ile Val Ala Glu Val Gly 485 490 495 Pro Asp Gln Val Gln Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu 500 505 510 Ala Gln Gly Glu Phe Val Thr Ile Ser Lys Leu Glu Ala Val Phe Ala 515 520 525 Gly Ser Ala Leu Val Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ala Arg 530 535 540 Ser Tyr Leu Leu Ala Val Val Val Pro Thr Asp Asp Ala Val Ala Arg 545 550 555 560 His Asp Pro Ala Ser Leu Lys Thr Ala Ile Ser Ala Ser Leu Gln Gln 565 570 575 Ala Ala Lys Thr Ala Gly Leu Gln Ser Tyr Glu Leu Pro Arg Asp Phe 580 585 590 Leu Val Glu Thr Gln Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly 595 600 605 Ile Arg Lys Leu Ala Arg Pro Lys Leu Lys Ala Arg Tyr Gly Asp Arg 610 615 620 Leu Glu Ala Leu Tyr Val Glu Leu Ala Glu Gly Gln Ala Gly Glu Leu 625 630 635 640 Arg Thr Leu Arg Arg Asp Gly Ala Lys Arg Pro Val Ala Glu Thr Val 645 650 655 Gly Arg Ala Ala Ala Ala Leu Leu Gly Ala Ala Ala Ala Asp Val Arg 660 665 670 Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu 675 680 685 Thr Phe Gly Asn Leu Leu Gln Glu Ile Phe Gly Val Asp Val Pro Val 690 695 700 Gly Val Ile Val Ser Pro Ala Ala Asp Leu Ala Ser Ile Ala Ala Tyr 705 710 715 720 Ile Glu Ala Glu Gln Ala Ser Thr Gly Lys Arg Pro Thr Tyr Ala Ser 725 730 735 Val His Gly Arg Asp Ala Glu Gln Val Arg Ala Arg Asp Leu Thr Leu 740 745 750 Asp Lys Phe Ile Asp Ala Glu Thr Leu Ser Ala Ala Thr Glu Leu Pro 755 760 765 Val Pro Ile Gly Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly 770 775 780 Phe Leu Gly Arg Tyr Leu Ala Leu Asp Trp Leu Glu Arg Met Ala Leu 785 790 795 800 Val Asp Gly Lys Val Ile Cys Leu Val Arg Ala Lys Asp Asp Ala Ala 805 810 815 Ala Arg Lys Arg Leu Asp Asp Thr Phe Asp Ser Gly Asp Pro Lys Leu 820 825 830 Leu Ala His Tyr Arg Lys Leu Ala Ala Asp His Leu Glu Val Leu Ala 835 840 845 Gly Asp Lys Gly Glu Ala Asp Leu Gly Leu Pro His Gln Val Trp Gln 850 855 860 Arg Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val 865 870 875 880 Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Ala Leu Gly 885 890 895 Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Thr Arg Ile Lys Pro Phe 900 905 910 Thr Tyr Val Ser Thr Ile Gly Val Gly Ala Gly Ile Glu Pro Gly Arg 915 920 925 Phe Thr Glu Asp Asp Asp Ile Arg Val Ile Ser Pro Thr Arg Ala Val 930 935 940 Asp Thr Gly Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val 965 970 975 Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu 980 985 990 Asn Leu Pro Asp Met Phe Thr Arg Met Met Val Ser Leu Val Thr Thr 995 1000 1005 Gly Ile Ala Pro Lys Ser Phe His Pro Leu Asp Ala Lys Gly His 1010 1015 1020 Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Val Ala 1025 1030 1035 Glu Ser Ile Ser Ala Leu Gly Ala Gln Ala Val Asp Glu Ala Gly 1040 1045 1050 Thr Gly Phe Ala Thr Tyr His Val Met Asn Pro His Asp Asp Gly 1055 1060 1065 Ile Gly Leu Asp Glu Phe Val Asp Trp Leu Val Glu Ala Gly Tyr 1070 1075 1080 Arg Ile Asp Arg Ile Asp Asp Tyr Ala Ala Trp Leu Gln Arg Phe 1085 1090 1095 Glu Thr Ala Leu Arg Ala Leu Pro Glu Arg Thr Arg Gln Tyr Ser 1100 1105 1110 Leu Leu Pro Leu Leu His Asn Tyr Gln Arg Pro Ala His Pro Ile 1115 1120 1125 Asn Gly Ala Met Ala Pro Thr Asp Arg Phe Arg Ala Ala Val Gln 1130 1135 1140 Glu Ala Lys Leu Gly Pro Asp Lys Asp Ile Pro His Val Thr Pro 1145 1150 1155 Gly Val Ile Val Lys Tyr Ala Thr Asp Leu Glu Leu Leu Gly Leu 1160 1165 1170 Ile <210> 183 <211> 1188 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium intracellulare ATCC 13950 <400> 183 Met Thr Asp Ile Val Thr Asp Pro Gly Arg Glu Gln Arg Leu Thr Glu 1 5 10 15 Arg Val Glu Gln Leu Tyr Ala Ser Asp Pro Gln Phe Arg Ala Ala Ala 20 25 30 Pro Ser Pro Glu Val Thr Glu Ala Ala His Arg Ala Gly Leu Arg Leu 35 40 45 Ala Glu Val Val Asp Ile Tyr Leu Ser Gly Tyr Ala Asp Arg Pro Ala 50 55 60 Leu Gly Gln Arg Ala Cys Glu Ala Thr Arg Asp Pro Ala Thr Gly Arg 65 70 75 80 Ala Ala Thr Ser Leu Leu Ser Gly Phe Glu Thr Ile Thr Tyr Arg Glu 85 90 95 Leu Gly Asp Arg Val Ala Ala Leu Ala Ala Ala Trp His Ser Gly Leu 100 105 110 Pro Gly Gly Leu Arg Pro Gly Asp Phe Val Gly Val Leu Gly Phe Thr 115 120 125 Ser Ile Asp Tyr Val Val His Tyr Leu Ala Cys Ile Arg Leu Gly Ala 130 135 140 Val Phe Val Pro Leu Gln Thr Ser Ser Thr Ala Ala Gln Leu Ala Pro 145 150 155 160 Ile Val Ala Glu Thr Ala Pro Arg Val Leu Ala Val Ser Val Glu Ser 165 170 175 Leu Gly Thr Ala Val Asp Val Val Leu Glu Ala Pro Ser Val Gln Arg 180 185 190 Leu Val Val Phe Asp Tyr Thr Gly Asp Asp Asp Glu Gln Arg Asp Arg 195 200 205 Tyr Asp Asp Ala Arg Ala Arg Leu Arg Gly Ala Gly His Arg Ala Gly 210 215 220 Val Val Ala Leu Ala Ala Glu Leu Ser Ser Gly Arg Gly Arg Pro Ala 225 230 235 240 Pro Asp Ala Tyr Val Pro Gly His Gly Glu Asn Pro Leu Ala Thr Leu 245 250 255 Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr 260 265 270 Ala Asp Met Met Thr Arg Ile Trp Gln Arg Pro His Ser Pro Ser Val 275 280 285 Asp Ile Gly Arg Val Val Pro Ala Ile His Leu Gln Tyr Met Pro Leu 290 295 300 Ser His Val Tyr Gly Leu Glu Trp Leu Ile Ala Thr Leu Ser Ser Gly 305 310 315 320 Gly Ile Gly Tyr Phe Ala Ala Lys Ser Asp Met Ser Thr Leu Phe Asp 325 330 335 Asp Ile Gly Leu Val Arg Pro Thr Ala Leu Asn Leu Val Pro Arg Val 340 345 350 Cys Asp Met Phe Phe Arg Arg Tyr Arg Lys Glu Leu Asp Gln Arg Ala 355 360 365 Gly Asp Asp Leu Gly Ala Glu Gln Arg Asp Asp Ala Val Lys Ala Glu 370 375 380 Leu Arg Gln Asp Phe Ile Gly Gly Arg Val Val Ser Ala Met Cys Gly 385 390 395 400 Ser Ala Pro Leu Ser Lys Gln Met His Ala Phe Met Glu Ser Leu Leu 405 410 415 Asp Val Thr Val Ala Asp Gly Tyr Gly Ala Thr Glu Thr Gly Gly Gly 420 425 430 Ile Met Arg Ser Gly Arg Ile Arg Arg Pro Pro Val Thr Asp Tyr Lys 435 440 445 Leu Val Asp Val Pro Glu Leu Gly Tyr Leu Thr Thr Asp Lys Pro Tyr 450 455 460 Pro Arg Gly Glu Leu His Leu Lys Ala Ser Asn Val Ile Pro Gly Tyr 465 470 475 480 Phe Lys His Pro Glu Leu Ser Ala Gln Ile Phe Asp Asp Glu Gly Phe 485 490 495 Tyr Lys Thr Gly Asp Ile Met Ala Glu Leu Ala Pro Asp His Leu Met 500 505 510 Tyr Leu Asp Arg Ser Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe 515 520 525 Val Ala Val Ser Gln Leu Glu Ala Thr Phe Ser Thr Ser Pro Tyr Ile 530 535 540 Arg Gln Ile Phe Leu Tyr Gly Ser Ser Glu Gln Pro Phe Leu Leu Ala 545 550 555 560 Val Ile Val Pro Asn Val Asp Ala Val Gly Gly Gly Asp Ala His Ala 565 570 575 Leu Ile Ala Glu Ser Leu Gln Gln Ile Ala Ala Asp Ser His Leu His 580 585 590 Pro Tyr Glu Val Pro Arg Asp Phe Leu Leu Glu Pro Gln Arg Phe Thr 595 600 605 Arg Asp Asn Gly Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Ala 610 615 620 Leu Lys Ala Arg Tyr Gly Glu Arg Leu Asp Ala Met Tyr Ala Glu Ile 625 630 635 640 Glu Ala Ser His Gly Asn Gln Leu Asp Glu Leu Arg Ser Ala Ser Arg 645 650 655 Glu Leu Pro Thr Ile Asp Thr Val Arg Arg Ala Ala Ala Ala Thr Leu 660 665 670 Gly Leu Pro Ala Asp Ala Ala Leu Arg Gly Asp Ala Lys Phe Ile Glu 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Phe Ser Phe Ala Thr Leu Leu Ser 690 695 700 Glu Ile Phe His Ile Asp Val Pro Val Gln Thr Ile Val Ser Pro Thr 705 710 715 720 Ala Thr Leu Ala Thr Val Ala Asn Tyr Val Asp Gly Glu Arg Thr Ser 725 730 735 Glu Ser Thr Arg Pro Thr Phe Ala Ser Val His Gly Arg Gly Ala Thr 740 745 750 Val Ala Arg Ala Ala Asp Leu Thr Leu Ala Arg Phe Ile Asp Asp Asp 755 760 765 Thr Leu Ala Ala Ala Pro His Leu Pro Ala Pro Thr Gly Ala Val Asn 770 775 780 Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys 785 790 795 800 Leu Asp Trp Leu Glu Arg Leu Ala Pro Thr Gly Gly Thr Val Ile Cys 805 810 815 Leu Ala Arg Gly Ala Asp Pro Thr Ala Gly Arg Gln Arg Ile Glu Ala 820 825 830 Ala Ile Asp Ser Gly Asp Ala Glu Leu Ser Arg Arg Phe Arg Gln Leu 835 840 845 Ala Asp His His Leu Gln Val Leu Val Gly Asp Val Gly Ala Ala Asn 850 855 860 Leu Gly Leu Asp Thr Pro Thr Tyr Glu Arg Leu Ala Arg Ser Val Asp 865 870 875 880 Leu Val Val His Ser Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Val Lys Leu 900 905 910 Ala Ile Ser Gln Arg Leu Lys Pro Ile Asn Tyr Ile Ser Thr Val Ala 915 920 925 Val Thr Thr Leu Pro Asp Gly Ser Phe Ile Gly Glu Asp Ala Asp Val 930 935 940 Arg Ser Ala Ser Pro Ser Arg Ser Leu Asp Glu Ser Tyr Ala Ser Gly 945 950 955 960 Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Val Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Asp Phe Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Val Ala Thr Gly Ile Ala Pro Arg Ser 1010 1015 1020 Phe Tyr Gln Leu Asp Ala Ser Gly His Arg Gln Arg Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Ala Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Ala Arg Thr Arg Gln Gly Tyr His Thr Tyr Asn Val Leu Asn 1055 1060 1065 Thr His Asp Asp Gly Val Ser Leu Asp Thr Phe Val Asp Trp Leu 1070 1075 1080 Ile Ala Asp Gly His Lys Ile Glu Arg Val Asp Asp Tyr Asp Glu 1085 1090 1095 Trp Leu Ala Arg Phe Thr Ala Ala Met Lys Ser Leu Pro Asp Asn 1100 1105 1110 Gln Arg Lys Ser Ser Leu Leu Pro Leu Met Ser Ala Tyr Ala Lys 1115 1120 1125 Pro Gly Gln Pro Thr His Gly Thr Gly Met Pro Ala Glu Lys Phe 1130 1135 1140 Arg Ala Ala Val Gln Ser Ala Gly Ile Gly Arg Asp Ser Asp Val 1145 1150 1155 Pro His Val Thr Gln Ala Leu Ile Asp Lys Tyr Val Ala Asp Leu 1160 1165 1170 Gln Arg Leu Gly Leu Leu Arg Thr Arg Ala Gly Ala His Ala Gly 1175 1180 1185 <210> 184 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium celeriflavum <400> 184 Met Thr Ser Asp Thr Arg Glu Thr Arg Met Ala Arg Arg Ile Ser Asp 1 5 10 15 Leu Phe Ala Thr Asp Pro Gln Phe Ala Ala Ala Arg Pro Asn Asp His 20 25 30 Ile Ala His Ala Ile Glu Ala Ser Glu Leu Thr Leu Pro Gln Val Leu 35 40 45 Arg Thr Ile Leu Asp Ala Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Val Glu Phe Ile Thr Asp Ala Asp Thr Gly Arg Thr Ser Ala Arg 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Arg Glu Leu Ser Asp Arg 85 90 95 Val Asp Ala Val Ala Ala Ala Leu Thr His Asn Gly Val Gln Pro Gly 100 105 110 Glu Arg Val Ala Ile Leu Gly Phe Thr Ser Ile Asp Tyr Thr Thr Val 115 120 125 Asp Met Ala Leu Leu His Leu Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Pro Val Gly Gln Leu Arg Pro Val Val Ala Glu Thr Glu Pro 145 150 155 160 Val Ala Ile Ala Ser Ser Val Asp Leu Leu Asp Asp Ala Val Glu Val 165 170 175 Met Leu Thr Gly His Leu Pro Gln Arg Leu Met Val Phe Asp Tyr His 180 185 190 Ala Glu Leu Asp Asp His Arg Ala Ala Leu Ala Ala Ala Arg Ser Arg 195 200 205 Leu Ala Glu Thr Thr Val Ala Val Glu Thr Leu Gly Asp Thr Leu Ala 210 215 220 Arg Gly Arg Asp Leu Pro Thr Pro Thr Pro Phe Asp Phe Gly Asp Asp 225 230 235 240 Asp Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys 245 250 255 Gly Ala Met Tyr Pro Ala Lys Met Val Ala Gly Ser Trp Arg Arg Ser 260 265 270 Ser Met Ala Met Trp Gly Thr Gly Glu Ala Leu Pro Ser Ile Thr Leu 275 280 285 Asn Phe Met Pro Met Ser His Met Met Gly Arg Gly Ile Leu Tyr Ala 290 295 300 Thr Leu Gly Ala Gly Gly Ile Gly Tyr Phe Val Ala Ser Ser Asp Leu 305 310 315 320 Ser Thr Leu Leu Glu Asp Leu Ala Leu Val Arg Pro Thr Gln Leu Asn 325 330 335 Phe Val Pro Arg Ile Trp Asp Met Ile Phe Gln Gln Phe Gln Ser Glu 340 345 350 Val Asp Arg Arg Thr Thr Asp Gly Ile Asp Arg Thr Ala Ala Glu Thr 355 360 365 Glu Val Leu Ala Asp Leu Arg Glu Asn Leu Leu Gly Gly Arg Phe Val 370 375 380 Ser Ala Met Thr Gly Ser Ala Pro Ile Ser Ala Glu Met Thr Thr Phe 385 390 395 400 Val Glu Ser Leu Leu Asp Leu His Leu Thr Asp Gly Tyr Gly Ser Thr 405 410 415 Glu Ala Gly Ala Ile Phe Val Asp Gly Gln Val Ala Arg Pro Pro Val 420 425 430 Ile Asp Tyr Lys Leu Ala Asp Val Pro Asp Leu Gly Tyr His Arg Thr 435 440 445 Asp Arg Pro His Pro Arg Gly Glu Leu Leu Ile Lys Ser Glu Thr Met 450 455 460 Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Thr Thr Ala Glu Val Phe Asp 465 470 475 480 Ala Glu Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Gly Pro 485 490 495 Asp Arg Leu Val Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Thr Val Ser Lys Leu Glu Ala Ala Phe Asp Thr 515 520 525 Ser Pro Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Leu Leu Ala Val Ile Val Pro Thr Asp Asp Ala Leu Ala Arg His 545 550 555 560 Asp Asp Asp Ser Leu Lys Thr Ala Ile Thr Glu Ser Leu Gln Asp Val 565 570 575 Ala Arg Thr Ala Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile 580 585 590 Val Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile 595 600 605 Arg Lys Leu Ala Arg Pro Lys Leu Lys Glu Cys Tyr Gly Asp Gln Leu 610 615 620 Glu Gln Leu Tyr Ser Gln Leu Ala Asp Ser Gln Ala Ser Glu Leu Arg 625 630 635 640 Ala Leu Arg Arg His Gly Ala Asp Arg Pro Val Ile Glu Thr Ile Ser 645 650 655 Arg Ala Ala Gly Ala Leu Leu Gly Ala Ala Ala Ala Asp Val His Pro 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Gly Asn Leu Leu Thr Glu Ile Tyr Asp Ile Asp Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Asn Asp Leu Thr Ala Leu Ala Asn Tyr Val 705 710 715 720 Glu Ala Ala Arg Arg Gly Ser Val Arg Pro Thr Phe Ala Ser Val His 725 730 735 Gly Arg Asp Ala Val Glu Ala His Ala Gly Asp Leu Val Leu Glu Lys 740 745 750 Phe Ile Asp Ala Glu Thr Leu Ala Ala Pro Pro Ser Leu Pro Gly Pro 755 760 765 Ala Ser Glu Ile Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu 770 775 780 Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Ala Met Val Asp 785 790 795 800 Gly Lys Val Ile Cys Leu Val Arg Ala Lys Asp Asn Ala Ser Ala Arg 805 810 815 Ala Arg Leu Asp Asp Thr Phe Asp Ser Gly Asp Pro Glu Leu Leu Gly 820 825 830 His Tyr Arg Glu Leu Ala Ala Asp His Leu Glu Val Ile Ala Gly Asp 835 840 845 Lys Gly Glu Ala Asp Leu Gly Leu Asp Arg Arg Thr Trp Gln Arg Leu 850 855 860 Ala Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala 885 890 895 Glu Leu Ile Arg Met Ala Leu Thr Thr Lys Ile Lys Pro Phe Val Tyr 900 905 910 Val Ser Thr Ile Gly Val Gly Ala Gly Ile Thr Pro Gly Gln Phe Thr 915 920 925 Glu Asp Gly Asp Ile Arg Val Ile Ser Ala Thr Arg Lys Val Asp Asp 930 935 940 Ser Tyr Ala Asn Gly Tyr Ser Asn Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Glu Ala His Asp Leu Ser Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Leu Ile Leu Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Phe Ser Phe Tyr Glu Val Asp Gly Asp Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala Glu Ala 1025 1030 1035 Ile Ser Thr Leu Gly Ala Gln Val Gly His Glu Pro Gly Ala Ala 1040 1045 1050 Phe Glu Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Leu Gly 1055 1060 1065 Leu Asp Glu Phe Val Asp Trp Leu Ile Asp Ala Gly Tyr Arg Ile 1070 1075 1080 Glu Arg Val Gly Gly Tyr Ala Thr Trp Leu Arg Arg Phe Asp Thr 1085 1090 1095 Ala Val Arg Ala Leu Pro Glu Arg Gln Arg Gln Ala Ser Leu Leu 1100 1105 1110 Pro Leu Leu His Asn Tyr Gln Arg Pro Glu Val Ala Ile Arg Gly 1115 1120 1125 Ser Ile Ala Pro Thr Glu Arg Phe Arg Thr Ala Val Gln Asp Ala 1130 1135 1140 Lys Ile Gly Pro Asp Lys Asp Ile Pro His Val Thr Arg Glu Val 1145 1150 1155 Ile Val Lys Tyr Val Thr Asp Leu Gln Leu Leu Gly Leu Val Leu 1160 1165 1170 <210> 185 <211> 1166 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium fallax <400> 185 Met Ser Ser Asp Pro Arg Glu Asp Ala Val Ala Arg Arg Met Met Glu 1 5 10 15 Val Tyr Ser Gly Asp Pro Glu Val Arg Ala Ala Met Ala Val Glu Ser 20 25 30 Val Ser Ala Glu Ile Arg Arg Pro Gly Leu His Leu Ala Glu Val Val 35 40 45 Glu Thr Val Met Ser Ser Tyr Ala Glu Arg Pro Ala Leu Gly Arg Arg 50 55 60 Ala Phe Glu Tyr Thr Val Asp Pro Ala Thr Gly Arg Cys Ala Ala His 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Gly Glu Leu Trp Glu Arg 85 90 95 Val Arg Ala Ile Ala Gly Ala Trp His His Asp Pro Glu Ile Ala Leu 100 105 110 Val Pro Gly Asp Phe Val Ala Ile Val Gly Phe Thr Ser Ser Asp Tyr 115 120 125 Val Ala Leu Asp Leu Ala Cys Ile Tyr Leu Gly Ala Val Val Ala Pro 130 135 140 Leu Pro Ala Thr Ala Gly Ala Glu Glu Leu Arg Gly Tyr Leu Ala Glu 145 150 155 160 Ile Glu Pro Arg Ile Leu Ala Val Thr Pro Asp Leu Leu Glu Thr Ala 165 170 175 Val Ala Ala Ile Gly Asp Gly Leu Ser Lys Ser Val Arg Leu Ile Val 180 185 190 Phe Asp Arg Cys Pro Gly Asp Asp Ala Glu Arg Glu Arg Ile Glu Ser 195 200 205 Ala Ala Ser Met Leu Asp Asn Gly Lys Ile Leu Asp Thr Leu Glu Asp 210 215 220 Val Val Glu Arg Gly Ala Arg Tyr Pro Val Pro Ala Met Phe Ser His 225 230 235 240 Ser Asp Ser Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Ser Pro Lys Gly Ala Leu Tyr Thr Glu Arg Leu Cys Leu Arg 260 265 270 Ala Trp Leu Val Gly Pro Gly Ala Gly Ala Ala Ile Thr Val Asn Tyr 275 280 285 Met Pro Leu Ser His Ile Gly Gly Arg Met Thr Leu Phe Gly Val Leu 290 295 300 Ala Arg Gly Gly Thr Asn Tyr Phe Thr Ala Ala Ser Asp Leu Ser Gln 305 310 315 320 Ile Phe Asp Asp Ile Ala Leu Val Arg Pro Thr Glu Leu Thr Leu Val 325 330 335 Pro Arg Leu Cys Asp Met Ala Leu Gln Thr Tyr His Asn Glu Leu Asn 340 345 350 Arg Arg Ser Ala Glu Glu Ile Asp Val Ser Arg Leu Glu Ala Glu Val 355 360 365 Arg Glu Asn Leu Arg Asp Lys Phe Phe Gly Gly Arg Leu Leu Ile Ala 370 375 380 Gly Phe Gly Ser Ala Pro Leu Ala Gly Gln Met Arg Thr Phe Ile Glu 385 390 395 400 Ser Val Leu Glu Val Pro Leu Arg Asp Gly Tyr Gly Ser Thr Glu Ala 405 410 415 Gly Gly Gly Ile Val Leu Asp Asn Gln Val Gln Arg Pro Pro Val Ile 420 425 430 Asp Tyr Met Leu Ala Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp 435 440 445 Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Ser Thr Gln Ile 450 455 460 Pro Gly Tyr Phe Lys Arg Pro Asp Leu Ser Ala Thr Met Ile Asp Ser 465 470 475 480 Asp Gly Tyr Tyr His Thr Gly Asp Val Met Ala Gln Ile Gly Pro Asp 485 490 495 Arg Leu Thr Tyr Ile Asp Arg Arg Ser Asn Val Val Lys Leu Ser Gln 500 505 510 Gly Glu Phe Val Thr Ile Ala Arg Val Glu Ala Val Leu Ala Thr Ala 515 520 525 Arg Trp Val Arg Gln Ile Phe Val Tyr Gly Ser Ser Glu Arg Ala Tyr 530 535 540 Leu Leu Ala Val Val Val Pro Thr Gly Ser Ala Leu Arg Glu Tyr Cys 545 550 555 560 Asp Pro Ala Glu Leu Lys Glu Ala Val Thr Lys Ser Leu Arg Thr Ala 565 570 575 Ala Ala Val Ala Asp Leu Arg Pro Tyr Glu Ile Pro Arg Asp Val Leu 580 585 590 Ile Glu Thr Glu Pro Phe Ala Val Ala Asn Ala Leu Leu Ser Gly Leu 595 600 605 Gly Lys Leu Leu Arg Pro Glu Leu Val Arg Arg Tyr Gly Ala Ser Leu 610 615 620 Gln Gln Met Tyr Ala Asp Leu Glu His Ala Glu Arg Gln Ala Leu Arg 625 630 635 640 Ser Ile Gln Ala Gln Val Arg Phe Arg Pro Val Arg Glu Ile Val Gly 645 650 655 Arg Val Ala Ser Ala Leu Leu Gly Ser Pro Ala Ala Thr Leu Arg Gly 660 665 670 Asp Val Arg Phe Val Glu Met Gly Gly Asp Ser Leu Thr Ala Val Ala 675 680 685 Leu Ser Lys Gln Leu Gly Glu Leu Tyr Gly Val Asp Val Pro Val Ala 690 695 700 Leu Val Ile Asp Pro Thr Ile Asp Leu Asp Arg Leu Ser Asp Tyr Val 705 710 715 720 Gln Arg Gln Arg Ser Ser Asn Asp Met His Gly Pro Arg Phe Glu Ser 725 730 735 Val His Gly Ser Pro Ala Asp Val Arg Ala Ala Asp Leu Val Leu Asp 740 745 750 Gln Phe Ile Ala Pro Ala Ala Leu Gly Ala Ala Glu Ser Ala Ala Pro 755 760 765 Pro Thr Ala Ala Pro His Val Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Ser Arg Leu Gln Arg Asp 785 790 795 800 Gly Gly Thr Leu Ile Cys Leu Val Arg Gly Asp Asp Ala Glu His Ala 805 810 815 Arg Val Arg Leu Glu Ser Ala Phe Glu Ser Thr Pro Pro Leu Ala Glu 820 825 830 Gln Phe Arg Lys Leu Ser Val Asp Arg Leu Glu Val Val Ala Gly Asp 835 840 845 Val Thr Ala Arg Glu Leu Gly Leu Pro Pro Arg Ile Trp Asp Glu Leu 850 855 860 Ala Cys Arg Val Asp Ser Val Val His Ala Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Glu Asp Leu Phe Gly Pro Asn Thr Val Gly Thr Ala 885 890 895 Glu Leu Ile Arg Phe Ala Ile Thr Ser Arg Arg Lys Arg Phe Ser Tyr 900 905 910 Val Ser Thr Val Gly Val Ala Ala Val Ala Gly Ser Thr Val Phe Asp 915 920 925 Glu Asp Ser Asp Val Arg Gln Trp Asn Pro Ala Pro Asp Asp Arg Ala 930 935 940 Asn Tyr Ala Thr Gly Tyr Ser Thr Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Asp Ala His Asp Arg Tyr Gly Leu Pro Val Thr Val Phe Arg 965 970 975 Ser Ala Met Ile Leu Ala His Arg His Tyr Pro Gly Gln Val Asn Val 980 985 990 Ser Asp Arg Phe Thr Arg Leu Leu His Gly Val Leu Thr Thr Gly Leu 995 1000 1005 Ala Pro Ala Thr Phe Tyr Ser Thr Arg Pro Gly Ser Val Arg Ala 1010 1015 1020 His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Glu Ala Met Val 1025 1030 1035 Thr Leu Ala Arg Lys Ala Gln Gly Asp Phe Arg Thr Tyr His Val 1040 1045 1050 Val Asn Pro His Asp Asp Gly Ile Asp Leu Asp Ser Phe Val Asp 1055 1060 1065 Trp Met Ile Asp Ala Gly Phe Arg Ile Thr Arg Ile Asp Asp Tyr 1070 1075 1080 Ala Val Trp Val Glu Arg Val Ala Val Val Leu Ser Gly Leu Ser 1085 1090 1095 Gly Glu His Arg Gln Asn Ser Leu Leu Pro Leu Leu Asp Ser Tyr 1100 1105 1110 Arg Asn Pro Glu Thr Pro Val Ala Gly Ser Ala Leu Pro Ala Thr 1115 1120 1125 Ala Phe Val Ala Gly Val Arg Ala Gln Arg Ile Gly Asp His Gly 1130 1135 1140 Glu Ile Pro Arg Ile Thr Pro Asp Leu Ile Leu Glu Tyr Ala Asp 1145 1150 1155 Asp Leu Arg Arg Arg Ala Leu Leu 1160 1165 <210> 186 <211> 1157 <212> PRT <213> Artificial Sequence <220> <223> Nocardia terpenica <400> 186 Met Val Asp Glu Arg Val Val Glu Arg Ile Ala Glu Leu Glu Ala Thr 1 5 10 15 Asp Ala Gln Tyr Ala Gly Ala Arg Ser Asp Arg Ala Val Ala Ala Arg 20 25 30 Val Asn Asp Pro Glu Leu Arg Leu Pro Glu Val Val Arg Ala Ala Leu 35 40 45 Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Ala Arg Ala Val Glu Val 50 55 60 Val Ala Glu Pro Gly Thr Gly Arg Arg Val Ala Arg Leu Thr Arg Arg 65 70 75 80 Leu Glu Thr Val Thr Tyr Arg Glu Leu Gly Glu Arg Ile Ala Ala Val 85 90 95 Ala Gly Gly Leu Arg Arg Asp Pro Asp Gly Asn Ser Leu Val Ser Pro 100 105 110 Gly Asp Arg Val Val Ile Leu Gly Phe Thr Ser Ile Asp Tyr Thr Val 115 120 125 Val Asp Leu Ala Leu Thr Gln Leu Gly Ala Val Ser Val Pro Leu Gln 130 135 140 Ala Ser Ser Ser Ala Gln Gln Leu Arg Pro Ile Val Val Glu Thr Glu 145 150 155 160 Pro Arg Val Ala Ala Ala Ser Ile Asp His Leu Leu Asp Ala Val Glu 165 170 175 Leu Ala Leu Thr Gly Phe Ala Pro Ala Arg Leu Val Val Phe Asp Tyr 180 185 190 Leu Pro Glu Val Asp Ala Gln Arg Glu Leu Phe Asp Thr Ala Ala Glu 195 200 205 Arg Leu Ala Gly Ser Gly Val Val Leu Glu Ser Leu Ala Ala Val Ala 210 215 220 Asp Arg Gly Ala Gly Gly Phe Thr Pro Glu Pro Pro Val Thr Asp Asp 225 230 235 240 Pro Leu Ser Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 245 250 255 Gly Ala Met Tyr Pro Glu Ser Leu Ala Ile Arg Leu Trp Arg Gly Gly 260 265 270 Phe Gly Leu Glu Asp Glu Asp Arg Ala Pro Gly Ala Trp Ile Thr Leu 275 280 285 Asn Phe Met Pro Met Ser His Val Met Gly Arg Ala Thr Val Phe Gly 290 295 300 Thr Leu Gly Arg Gly Gly Ile Ala Tyr Phe Gly Gly Ser Ser Asp Met 305 310 315 320 Ser Thr Phe Leu Glu Asp Leu Ala Leu Ile Arg Pro Thr Gln Leu Gln 325 330 335 Phe Val Pro Arg Val Trp Glu Leu Leu Phe Gln Glu Tyr Gln Arg Ala 340 345 350 Leu Asp Arg Tyr Thr Pro Asp Glu Ala Leu Thr Val Leu Arg Arg Asp 355 360 365 Val Leu Gly Gly Arg Ala Leu Ala Gly Leu Thr Gly Ser Ala Pro Ile 370 375 380 Ser Ala Glu Val Tyr Glu Phe Ala Asp Arg Leu Leu Gly Thr His Val 385 390 395 400 Ile Glu Leu Tyr Gly Ser Thr Glu Ala Gly Gly Ile Phe Val Asp Gly 405 410 415 Arg Val Leu Arg Pro Pro Val Arg Asp Tyr Lys Leu Ala Asp Val Pro 420 425 430 Asp Leu Gly Tyr Tyr Ser Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu 435 440 445 Leu Leu Leu Thr Glu Thr Leu Phe Pro Gly Tyr Phe Arg Arg Pro Glu 450 455 460 Val Thr Ala Glu Val Ile Asp Glu Gln Gly Tyr Tyr His Thr Gly Asp 465 470 475 480 Val Val Ala Glu Val Ala Pro Asp Glu Leu Arg Tyr Leu Asp Arg Arg 485 490 495 Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Thr Val Ser Lys 500 505 510 Leu Glu Ala Ala Phe Ala Ala Ser Pro Val Ile Glu Gln Ile Tyr Val 515 520 525 Tyr Gly Asn Ser Ser Arg Pro Tyr Leu Leu Ala Val Val Val Pro Thr 530 535 540 Glu Lys Ala Leu Ala Gly Asp Glu Ala Ala Val Lys Ser Arg Val Thr 545 550 555 560 Glu Gly Leu Arg Ala Ile Ala Ala Glu Val Gly Leu Gln Ser Tyr Glu 565 570 575 Val Pro Arg Asp Phe Leu Ile Glu Thr Thr Pro Phe Thr Val Glu Asn 580 585 590 Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala Arg Pro Lys Leu Lys Gln 595 600 605 His Tyr Gly Glu Arg Leu Glu Gln Leu Tyr His Asp Leu Ala Gln Gly 610 615 620 Gln Ala Ala Glu Leu Arg Ala Leu His Glu Gly Ala Ala Asp Arg Pro 625 630 635 640 Thr Leu Glu Thr Val Thr Arg Ala Ala Ala Ala Leu Leu Gly Val Ala 645 650 655 Val Ala Asp Val Ala Ala Asp Ala Arg Phe Thr Asp Leu Gly Gly Asp 660 665 670 Ser Leu Ser Ala Leu Thr Phe Gly Asn Thr Leu Asn Ser Ile Phe Glu 675 680 685 Val Glu Val Pro Val Gly Val Ile Val Gly Pro Ala Thr Asp Leu Arg 690 695 700 Ala Leu Ala Glu Tyr Ile Glu His Glu Ser Ala Thr Arg Gly Ala Arg 705 710 715 720 Pro Thr Phe Ala Ser Val His Gly Ala Thr Ala Thr Glu Val Arg Ala 725 730 735 Ser Asp Leu Thr Leu Asp Arg Phe Ile Asp Pro Ala Val Leu Ala Ala 740 745 750 Ala Pro Ser Leu Pro Arg Ala Thr Gly Pro Val Arg Thr Val Leu Leu 755 760 765 Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu 770 775 780 Glu Arg Val Ala Gln Gln Asp Gly Thr Val Ile Cys Leu Val Arg Ala 785 790 795 800 Thr Asp Asp Ala Ala Ala Arg Glu Arg Leu Asp Arg Val Phe Asp Ser 805 810 815 Gly Asp Pro Ala Leu Trp Glu Arg Tyr Arg Gly Leu Ala Gln Arg His 820 825 830 Leu Arg Val Leu Ala Gly Asp Lys Gly Ser Ala Asn Leu Gly Leu Asp 835 840 845 Glu Gln Thr Trp Arg Glu Leu Ala Asp Thr Val Asp Leu Ile Val Asp 850 855 860 Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Glu Leu Phe Gly 865 870 875 880 Pro Asn Val Ile Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Gly 885 890 895 Arg Ile Lys Ser Tyr Asp Tyr Ile Ser Thr Val Gly Val Gly Asp Gln 900 905 910 Ile Glu Pro Ala Ala Phe Thr Glu Asp Ala Asp Val Arg Ala Ile Ser 915 920 925 Ala Val Arg Arg Ile Asp Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser 930 935 940 Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Val Gly 945 950 955 960 Leu Pro Val Ala Val Phe Arg Cys Asp Met Ile Leu Ala Asp Gly Val 965 970 975 Ser Ile Gly Gln Leu Asn Leu Pro Asp Met Phe Thr Arg Leu Met Leu 980 985 990 Ser Leu Val Ala Thr Gly Ile Ala Pro Glu Ser Phe Tyr Glu Leu Asp 995 1000 1005 Ala Asp Gly His Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val 1010 1015 1020 Asp Phe Ile Ala Ala Ala Val Ala Glu Leu Gly Val Gly Glu Gly 1025 1030 1035 Phe Ser Thr Tyr His Val Met Asn Pro His Asp Asp Gly Ile Gly 1040 1045 1050 Leu Asp Gln Tyr Val Asp Trp Leu Val Glu Ala Gly Tyr Arg Ile 1055 1060 1065 Asp Arg Ile Ala Asp Tyr Arg Ser Trp Leu Glu Gln Phe Glu Thr 1070 1075 1080 Lys Leu Arg Ala Leu Pro Glu Arg Gln Arg Lys Ala Ser Leu Leu 1085 1090 1095 Pro Leu Leu His Asn Tyr Gln His Pro Thr Pro Pro Leu Asn Gly 1100 1105 1110 Ala Ile Ala Val Thr Asp Arg Phe Arg Ala Ala Val Gln Glu Ala 1115 1120 1125 Lys Ile Gly Pro Asp Lys Asp Ile Pro His Val Gly Pro Ala Val 1130 1135 1140 Val Val Gly Tyr Val Thr Asn Leu Glu His Leu Gly Leu Leu 1145 1150 1155 <210> 187 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium peregrinum <400> 187 Met Pro Thr Asp Thr Arg Glu Glu Gln Gln Val Arg Arg Val Ala Glu 1 5 10 15 Leu Tyr Ala Thr Asp Gln Gln Phe Ala Asp Ala Arg Pro Asp Ala Thr 20 25 30 Ile Ser Asp Leu Val Lys Arg Ala Gly Ser Arg Leu Pro Glu Ile Val 35 40 45 Arg Thr Val Met Glu Gly Tyr Ala Glu Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Val Arg Phe Val Glu Asn Pro Ala Thr Gly Arg Thr Ser Thr Glu 65 70 75 80 Leu Leu Pro Arg Phe Glu Thr Leu Thr Tyr Arg Gln Met Ala Asp Arg 85 90 95 Val Gly Ala Val Ala Ala Ala Trp Ala Gly Asp Pro Ile Lys Pro Gly 100 105 110 Asp Arg Val Cys Met Val Gly Phe Ala Ser Val Asp Tyr Ala Thr Val 115 120 125 Asp Leu Ala Leu Val Leu Leu Asn Ala Val Pro Val Pro Leu Gln Ala 130 135 140 Asn Ala Ala Val Ala Gln Leu Arg Pro Val Val Ala Glu Thr Glu Pro 145 150 155 160 Thr Val Ile Ala Ala Ser Val Asp Tyr Leu Ser Val Ala Val Gly Leu 165 170 175 Val Ser Thr Glu His Ala Pro Ala Arg Leu Val Val Phe Asp Tyr His 180 185 190 Ser Gln Val Asp Asp His Arg Glu Ala Val Asp Ala Ala Arg Ala Arg 195 200 205 Leu Ala Glu Met Gly Ser Pro Val Val Val Glu Leu Leu Ala Asp Leu 210 215 220 Val Glu Arg Gly Thr Met Leu Pro Ser Pro Glu Ile Glu Cys Gly Asp 225 230 235 240 Asp Asp Ser Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr 245 250 255 Pro Lys Gly Ala Met Tyr Gln Arg Asp Leu Val Ala Leu Thr Trp Leu 260 265 270 Ser Ser Ser Trp Pro Ala Thr His Glu Glu His Val Ala Pro Ser Ile 275 280 285 Thr Leu Asn Phe Arg Pro Leu Ser His Val Val Gly Arg Ala Met Leu 290 295 300 Tyr Gly Thr Leu Gly Val Gly Gly Thr Ala Tyr Phe Ala Ala Ser Arg 305 310 315 320 Asp Leu Ser Thr Phe Leu Glu Asp Leu Ala Leu Val Arg Pro Thr Gln 325 330 335 Leu Asp Phe Val Pro Arg Val Trp Glu Met Leu Phe Glu Glu Phe Arg 340 345 350 Arg Glu Val Asp Ala Arg Ser Gly Pro His Arg Asp Arg Ala Thr Val 355 360 365 Glu Ala Gln Val Met Ala Glu Gln Arg Gln Asn Val Leu Gly Gly Arg 370 375 380 Tyr Val Ala Ala Ser Thr Gly Ser Ala Pro Met Ser Ala Asp Leu Arg 385 390 395 400 Ala Trp Ala Glu Ser Phe Thr Gly Met His Leu Thr Asp Ile Phe Gly 405 410 415 Leu Thr Glu Ser Val Leu Leu Leu Ile Asp Gly Arg Val Gln Arg Pro 420 425 430 Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe 435 440 445 Gly Ser Asp Arg Pro Phe Pro Arg Gly Glu Leu Ala Val Lys Ser Thr 450 455 460 Thr Gln Phe Ala Gly Tyr Tyr Lys Arg Pro Glu Leu Thr Ala Ala Ala 465 470 475 480 Phe Asp Ser Asp Gly Tyr Tyr Leu Thr Gly Asp Ile Met Ala Glu Arg 485 490 495 Gly Pro Asp Gln Leu Thr Tyr Val Asp Arg Arg Asn Asn Val Leu Lys 500 505 510 Leu Ser Gln Gly Glu Phe Ile Thr Val Ser Lys Leu Glu Thr Leu Phe 515 520 525 Ser Gly Ser Ala Leu Val Arg Gln Ile Tyr Ile Tyr Ala Asn Ser Ala 530 535 540 Arg Ser Tyr Ser Leu Ala Val Val Val Pro Thr Glu Asp Ala Leu Lys 545 550 555 560 Gln His Asp Val Gln Ser Leu Lys Pro Ala Ile Thr Glu Ala Leu Arg 565 570 575 Asp Ile Ala Lys Ala Ala Asp Leu Gln Ser Tyr Glu Leu Pro Arg Asp 580 585 590 Ile Val Val Glu Thr Thr Pro Phe Thr Ala Ala Asn Gly Leu Leu Thr 595 600 605 Asp Leu Gly Lys Pro Ala Arg Lys Lys Ile Gln Gln His Tyr Gly Glu 610 615 620 Arg Leu Glu Arg Leu Tyr Ala Asp Leu Ala Glu Asp Gln Thr Lys Lys 625 630 635 640 Leu Arg Ala Leu Arg Asp Gly Ala Ala Asp Arg Pro Leu Ser Asp Thr 645 650 655 Ile Ser Gln Ala Ala Ala Ala Val Leu Gly Thr Val Asp Val Ala Leu 660 665 670 Gln Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala 675 680 685 Leu Thr Phe Gly Asn Leu Leu Arg Asp Ile Phe Gly Ile Asp Val Pro 690 695 700 Val Gly Val Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Ile Ala Asp 705 710 715 720 Tyr Ile Asp Ala Glu Arg Asn Gly Ser Lys Arg Pro Thr Phe Ala Ala 725 730 735 Val His Gly Arg Gly Ala Thr Glu Val Arg Ala Arg Asp Leu Thr Leu 740 745 750 Asp Lys Phe Leu Asp Glu Thr Thr Leu His Ala Ala Pro Ser Leu Pro 755 760 765 Thr Pro Ala Thr Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly 770 775 780 Phe Leu Gly Arg Tyr Leu Met Leu Glu Trp Leu Gln Arg Met Glu Met 785 790 795 800 Val Gly Gly Thr Val Ile Ala Leu Val Arg Ala Lys Thr Asp Ala Glu 805 810 815 Ala Arg Ala Arg Leu Asp Arg Thr Phe Asp Ser Gly Asp Pro Lys Leu 820 825 830 Leu Ala His Tyr Arg Lys Leu Ala Ala Asp His Leu Glu Val Ile Ala 835 840 845 Gly Asp Lys Gly Glu Ala Asp Leu Gly Leu Asp Pro Gln Thr Trp Arg 850 855 860 Arg Leu Ala Asp Thr Val Asp Val Ile Val Asp Ser Ala Ala Leu Val 865 870 875 880 Asn His Ile Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala Leu Gly 885 890 895 Thr Ala Glu Leu Ile Arg Ile Ala Leu Thr Ser Lys Leu Lys Pro Tyr 900 905 910 Thr Tyr Val Ser Thr Ile Gly Val Gly Asp Gln Ile Asp Pro Gly Arg 915 920 925 Phe Val Glu Asp Ala Asp Ile Arg Gln Ile Ser Ala Thr Arg Ala Ile 930 935 940 Asn Asp Asn Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Leu Arg Glu Ala Asn Gly Arg Cys Gly Leu Pro Val Ser Val 965 970 975 Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Ser Tyr Ala Gly Gln Leu 980 985 990 Asn Leu Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr 995 1000 1005 Gly Ile Ala Pro Glu Ser Phe Tyr Glu Leu Asp Ala Asp Gly Asn 1010 1015 1020 Arg Gln Arg Ala His Tyr Gly Gly Leu Pro Val Glu Phe Ile Ala 1025 1030 1035 Ala Ala Ile Ser Thr Leu Gly Thr Gln Ile Leu Asp Ser Asp Asn 1040 1045 1050 Gly Phe Gln Thr Tyr His Val Thr Asn Pro His Asp Asp Gly Ile 1055 1060 1065 Gly Leu Asp Glu Tyr Val Asp Trp Leu Ile Asp Ala Gly Tyr Gln 1070 1075 1080 Ile Ala Arg Val Ala Asp Tyr Gly Asp Trp Val Gln Arg Ile Glu 1085 1090 1095 Thr Ala Leu Arg Ala Leu Pro Glu Lys Gln Arg Gln Ala Ser Leu 1100 1105 1110 Leu Pro Leu Leu His Tyr Tyr Gln Lys Pro Gln Pro Pro Ile Pro 1115 1120 1125 Gly Ser Met Ala Pro Ala Asp Arg Phe Arg Asp Ala Val His Glu 1130 1135 1140 Ala Lys Val Gly Pro Asp Asn Asp Ile Pro His Ile Gly Gln Ser 1145 1150 1155 Thr Ile Val Lys Tyr Ala Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 188 <211> 1184 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. E1386 <400> 188 Met Leu Ala Asp Ser His Thr Glu Lys Leu Ala Arg Arg Val Ala Asp 1 5 10 15 Leu Leu Thr Asn Asp Ala Gln Phe Ala Ala Ala Leu Pro Arg Glu Asp 20 25 30 Val Ser Arg Ala Ile Leu Arg Pro Gln Ile Gly Leu Ala Gly Leu Met 35 40 45 Arg Thr Val Ala Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Arg Arg 50 55 60 Ala Val Glu Val Val Arg Glu Ala Ser Thr Gly Ala Gln Arg Leu Glu 65 70 75 80 Met Leu Pro Trp Phe Asp Phe Val Thr Tyr Arg Glu Leu Trp Gln Arg 85 90 95 Val Ser Ala Val Ala Ser Ala Leu Ala Asp Gly Ala Val Ser Ala Gly 100 105 110 Asp Arg Val Ala Thr Leu Gly Phe Cys Ser Val Asp Tyr Thr Thr Ile 115 120 125 Asp Leu Ala Ala Pro Leu Met Ser Ala Val Ser Val Pro Leu His Ala 130 135 140 Gly Ala Pro Val Gly Gln Leu Arg Arg Ile Val Glu Glu Ile Glu Pro 145 150 155 160 Ser Val Ile Ala Cys Ser Ala Ala Tyr Leu Asn Asp Gly Val Glu Leu 165 170 175 Ala Leu Gly Ala Ala Thr Pro Ala Ile Leu Val Val Phe Asp Arg His 180 185 190 Pro Gln Leu Asp Glu His Gln Arg Asn Leu Asp Glu Ala Arg Ala Arg 195 200 205 Leu Ala Ala Ala Gly Ser Ser Val Val Leu Glu Thr Ile Glu Glu Leu 210 215 220 Leu Gln Arg Gly Ala Ala Arg Pro Leu Pro Pro Glu Pro Pro Ala Asp 225 230 235 240 Asp Asp Arg Leu Ala Ala Ile Val Tyr Thr Ser Gly Ser Ser Gly Ser 245 250 255 Pro Lys Gly Ala Met Gln Pro Glu Gly Leu Ala Lys Gly Val Trp Thr 260 265 270 Val Thr Ala Ala Val Leu Thr Glu Arg Gly Phe Ala Ile Pro Ala Ile 275 280 285 Thr Leu Asn Tyr Met Pro Met Ser His Thr Ala Gly Arg Ala Met Leu 290 295 300 Tyr Ser Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Thr Ala Lys Ser 305 310 315 320 Asp Leu Ser Thr Phe Leu Asp Asp Leu Ser Leu Val Arg Pro Thr Gln 325 330 335 Leu Asn Phe Val Pro Arg Ile Trp Glu Met Leu His Gly Glu Tyr Arg 340 345 350 Asn Glu Leu Arg Ala Arg Gly Gly Gly Ala Ala Thr Ala Gly Pro Thr 355 360 365 Glu Glu Asp Ile Leu Ala Asp Leu Arg Thr Arg Val Leu Gly Gly Arg 370 375 380 Tyr Ile Ser Ala Leu Thr Gly Ser Ala Pro Ile Ser Ala His Leu Ala 385 390 395 400 Asp Trp Val Glu Arg Leu Leu Asp Ser His Leu Met Asn Ala Leu Gly 405 410 415 Ala Thr Glu Ser Gly Ser Val Val Ile Asp Cys Lys Val Gln Arg Pro 420 425 430 Pro Val Thr Ala Tyr Lys Leu Ala Asp Val Pro Glu Leu Gly Tyr Phe 435 440 445 Ser Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Ile Lys Ser Asn 450 455 460 Thr Leu Phe Arg Gly Tyr Tyr Lys Arg Pro Glu Leu Thr Ala Glu Val 465 470 475 480 Phe Asp Glu Asp Gly Phe Tyr Arg Thr Gly Asp Val Val Glu Glu Leu 485 490 495 Gly Pro Asp Glu Leu Arg Tyr Val Asp Arg Arg Asn Asn Val Ile Lys 500 505 510 Leu Ser Gln Gly Glu Phe Val Thr Ile Ser Lys Leu Glu Ala Val Tyr 515 520 525 Ala Asp Cys Asp Leu Ile His Gln Ile Tyr Val Tyr Gly Asn Gly Glu 530 535 540 Arg Pro Tyr Leu Leu Ala Val Val Val Pro Thr Glu Ala Ala Leu Ala 545 550 555 560 Gln Arg Asp Ile Asp Ala Leu Lys Pro Met Leu Ile Arg Ser Leu Gln 565 570 575 Glu Ala Ala Arg Asp Ala Asp Leu Arg Ser Tyr Glu Val Pro Arg Asp 580 585 590 Ile Ile Val Glu Pro Tyr Pro Phe Thr Leu Asp Asn Gly Leu Leu Ser 595 600 605 Gly Ile Arg Lys Pro Ser Arg Pro Asn Leu Leu Arg His Tyr Gly Ala 610 615 620 Arg Leu Glu Gln Leu Tyr Asp Glu His Ala Gln Ala Gln Asn Thr Arg 625 630 635 640 Leu Gly Glu Leu Arg Asp Arg Ala Ala Thr Gln Pro Ile Val Glu Thr 645 650 655 Val Cys Ala Ala Ala Ser Ala Leu Leu Gly Val Pro Gly Ala Thr Pro 660 665 670 Pro Ser Ser Val Arg Phe Thr Asp Leu Gly Gly Asp Ser Leu Thr Ala 675 680 685 Leu Thr Phe Ala Asp Ala Leu Asn Asp Ile Phe Ala Val Asp Val Pro 690 695 700 Val Asp Val Leu Ile Ser Pro Ala Asn Asp Leu Gln Ser Val Ala Asn 705 710 715 720 Phe Ile Glu Ala Gln Arg Ala Thr Asp Thr Arg Arg Pro Thr Phe Ala 725 730 735 Ser Val His Gly Ala Gly Ala Thr Val Ala Asp Thr Arg Asp Leu Thr 740 745 750 Leu Asp Lys Phe Leu Asp Ser Ala Thr Leu Glu Gly Ala His Ala Leu 755 760 765 Ala Gly Pro Asn Ser Asp Val Arg Thr Val Leu Leu Thr Gly Ala Thr 770 775 780 Gly Tyr Leu Gly Arg Tyr Leu Leu Leu Glu Trp Leu Gln Arg Met Ala 785 790 795 800 Leu Val Asp Gly Thr Val Ile Cys Leu Val Arg Ala Lys Asp Asp Ala 805 810 815 Ala Ala Arg Thr Arg Leu Asp Asn Thr Phe Asp Ser Gly Asp Ala Asn 820 825 830 Leu Leu Ser Arg Tyr Arg Arg Leu Ala Ala Asp His Leu Glu Val Leu 835 840 845 Ala Gly Asp Lys Gly Asp Ala Asp Leu Gly Leu Ala Gln Ala Ser Trp 850 855 860 Gln His Leu Ala Asp Thr Val Asp Leu Ile Ile Asp Pro Ala Ala Leu 865 870 875 880 Val Asn His Met Leu Pro Tyr Arg Glu Leu Phe Gly Pro Asn Val Leu 885 890 895 Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Thr Arg Gln Lys Leu 900 905 910 Ile Ala Tyr Val Ser Ser Val Gly Val Gly Ala Thr Ile Asp Ser Ala 915 920 925 Lys Phe Thr Glu Asp Ala Asp Ile Arg Thr Ile Ser Pro Thr Arg Leu 930 935 940 Val Asp Asp Thr Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Ala 945 950 955 960 Glu Val Leu Leu Arg Glu Ala Asn Asp His Cys Glu Leu Pro Val Arg 965 970 975 Val Phe Arg Cys Asp Met Ile Met Ala Glu Thr Thr Tyr Arg Gly Gln 980 985 990 Leu Asn Val Pro Asp Met Val Thr Arg Leu Ile Leu Ser Ile Ala Ala 995 1000 1005 Thr Gly Leu Ala Pro Lys Ser Phe Tyr Leu Pro Asp His Asp Gly 1010 1015 1020 Arg Arg Ala Arg Ala His Phe Asp Ala Leu Pro Val Asp Phe Val 1025 1030 1035 Ala Glu Ser Ile Ser Thr Leu Thr Ala Ile Ala Ala Gly Glu Ala 1040 1045 1050 Lys Gly Phe Gln Thr Phe His Ile Val Asn Pro His Asp Asp Ala 1055 1060 1065 Ile Gly Leu Asp Glu Tyr Val Asp Trp Met Ile Glu Thr Gly Cys 1070 1075 1080 Pro Ile Glu Arg Ile Gly Asp His Asp Gln Trp Phe Gly Arg Phe 1085 1090 1095 Asp Ser Ala Leu Arg Asn Leu Pro Glu Lys Gln Arg Gln Ala Ser 1100 1105 1110 Leu Leu Pro Leu Met Ala Thr Tyr Arg His Pro Leu Pro Pro Thr 1115 1120 1125 Arg Gly Ala Phe Ala Pro Ala Asp Arg Phe Arg Ala Ala Val Ile 1130 1135 1140 Asp Val Ala Ile Gly Pro Ala Gly Asp Ile Pro His Val Gly Lys 1145 1150 1155 Pro Ile Ile Glu Lys Tyr Leu Thr Asp Leu Glu Ala Leu Gly Leu 1160 1165 1170 Leu Asp Pro Cys Pro Gly Ala Pro Gly Glu Glu 1175 1180 <210> 189 <211> 1187 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. abscessus <400> 189 Met Thr Val Thr His Asp Ile Asp Pro Gln Gln Glu Gln Leu Ala Arg 1 5 10 15 Arg Ile Glu Asn Leu Arg Asp Ser Asp Pro Gln Phe Arg Ala Thr Gln 20 25 30 Pro Asp Pro Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu 35 40 45 Ser Glu Ala Ile Ala Thr Leu Met Thr Gly Tyr Ala Glu Arg Pro Ala 50 55 60 Leu Gly Glu Arg Ala Arg Glu Leu Val Thr Asp Asp Asp Gly Arg Thr 65 70 75 80 Val Leu Arg Leu Leu Pro Arg Phe Asp Thr Val Thr Tyr Gly Glu Leu 85 90 95 Trp Ser Arg Thr Thr Ser Val Ala Ala Ser Trp His His Asp Pro Ala 100 105 110 His Pro Val Lys Ser Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser 115 120 125 Ile Asp Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val 130 135 140 Ala Val Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Trp Thr Thr Ile 145 150 155 160 Leu Ala Glu Ala Glu Pro Asn Thr Leu Ala Val Ser Ile Glu Leu Ile 165 170 175 Gly Thr Ala Leu Glu Ser Val Leu Ala Thr Pro Thr Val Lys Gln Val 180 185 190 Val Val Phe Asp Tyr Thr Pro Glu Val Asp Glu Gln Arg Glu Ala Phe 195 200 205 Glu Ala Ala Gly Ala Arg Leu Ala Gly Thr Gly Ile Ala Ile Glu Thr 210 215 220 Leu Asp Ser Val Val Thr Arg Gly Ala Glu Leu Pro Ala Ala Pro Leu 225 230 235 240 Tyr Ala Pro Ser Ala Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile 260 265 270 Val Arg Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn 275 280 285 Leu Pro Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly 290 295 300 Arg Gly Thr Leu Thr Ala Thr Leu Ser Thr Gly Gly Leu Gly Tyr Phe 305 310 315 320 Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile 325 330 335 Arg Pro Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe 340 345 350 Gln Arg Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Gly Gly Gln Ala 355 360 365 Ala Asp Ala Glu Ala Val Ala Ala Gln Val Lys Ala Glu Ile Arg Asp 370 375 380 Asn Leu Phe Gly Gly Arg Val Leu Ala Val Met Val Gly Ser Ala Pro 385 390 395 400 Leu Ser Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu His 405 410 415 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp 420 425 430 Gly Ile Val Gln Arg Pro Pro Val Asn Asp Tyr Lys Leu Val Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro His Pro Arg Gly Glu 450 455 460 Leu Leu Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Gly Val Phe Asp Glu Asn Gly Tyr Tyr Met Thr Gly 485 490 495 Asp Ile Val Ala Glu Leu Ala Pro Asp Asn Ile Gln Ile Ile Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 515 520 525 Thr Leu Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr 530 535 540 Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 545 550 555 560 Thr Pro Glu Ala Val Ala Ala Ala Lys Gly Asp Glu Ala Ala Leu Lys 565 570 575 Ala Thr Leu Ala Asp Ser Leu Gln Asp Ile Ala Lys Glu Ile Gln Leu 580 585 590 Gln Ser Tyr Glu Val Pro Arg Asp Phe Ile Ile Glu Pro Gln Pro Phe 595 600 605 Thr Gln Gly Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro 610 615 620 Asn Leu Lys Ala His Tyr Gly Glu Arg Leu Glu Gln Met Tyr Ala Asp 625 630 635 640 Ile Ala Glu Gln Gln Ala Ala Glu Leu Arg Ala Leu His Gly Val Asp 645 650 655 Pro Asp Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala Leu 660 665 670 Leu Gly Val Ser Ser Ala Glu Leu Ala Ala Asp Ala His Phe Thr Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Asp Leu Leu Arg 690 695 700 Asp Ile Phe Ala Val Glu Val Pro Val Gly Val Ile Val Ser Ala Ala 705 710 715 720 Asn Asp Leu Gly Gly Val Ala Lys Phe Ile Asp Glu Gln Arg His Ser 725 730 735 Gly Gly Thr Arg Pro Thr Ala Asp Ser Val His Gly Ala Val His Thr 740 745 750 Glu Ile Arg Ala Thr Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala 755 760 765 Thr Leu His Ala Ala Pro Ser Leu Pro Lys Ala Val Gly Ile Pro His 770 775 780 Thr Val Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly His Tyr Leu Ala 785 790 795 800 Leu Glu Trp Leu Glu Arg Leu Asp Lys Thr Asp Gly Lys Leu Ile Val 805 810 815 Ile Val Arg Gly Lys Asn Ala Glu Ala Ala Tyr Arg Arg Leu Glu Glu 820 825 830 Ala Phe Asp Thr Gly Asp Thr Gln Leu Leu Ala His Phe Arg Ser Leu 835 840 845 Ala Gly Lys His Leu Glu Val Leu Ala Gly Asp Ile Gly Asp Pro Asn 850 855 860 Leu Gly Leu Asp Ala Ala Thr Trp Gln His Leu Ala Asp Thr Val Asp 865 870 875 880 Val Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Lys Leu 900 905 910 Ala Ile Thr Thr Lys Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ala 915 920 925 Val Ala Ala Tyr Val Asp Pro Thr Thr Phe Asp Glu Glu Ser Asp Ile 930 935 940 Arg Leu Ile Ser Ala Val Arg Pro Val Asp Glu Leu Tyr Ala Asn Gly 945 950 955 960 Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Arg Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Gly Ser 1010 1015 1020 Phe Tyr Gln Ala His Ala Thr Gly Glu Arg Pro Arg Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Gly Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Thr Gln Val Pro Glu Gly Ser Glu Gly Phe Val Thr Tyr Asp 1055 1060 1065 Cys Val Asn Pro His Ala Asp Gly Ile Ser Leu Asp Asn Phe Val 1070 1075 1080 Asp Trp Leu Ile Asp Ala Gly Tyr Arg Ile Gln Arg Ile Asp Asn 1085 1090 1095 Tyr Thr Glu Trp Phe Asn Arg Phe Asp Thr Ala Ile Arg Gly Leu 1100 1105 1110 Pro Glu Lys Gln Lys Gln His Ser Leu Leu Pro Leu Leu His Ala 1115 1120 1125 Phe Glu Gln Pro Ser Gly Ala Glu Asp His Gly Val Val Pro Ala 1130 1135 1140 Lys Arg Phe Gln His Ala Val Gln Val Ala Lys Ile Gly Pro Ala 1145 1150 1155 Asp Gln Ser Gly Asn Thr Asp Ile Pro His Leu Ser Glu Glu Leu 1160 1165 1170 Ile Val Lys Tyr Ala Lys Asp Leu Glu Gln Leu Gly Leu Leu 1175 1180 1185 <210> 190 <211> 1149 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. SWH-M1 <400> 190 Met Pro Thr Asp Thr Arg Glu Glu Arg Leu Ala His Arg Ile Asp Asp 1 5 10 15 Leu Ser Ala Thr Asp Pro Gln Phe Ala Ala Ala Leu Pro Asp Glu Ala 20 25 30 Ile Ala Glu Ala Ile Glu Asp Pro Gln Leu Arg Leu Pro Gln Ile Ile 35 40 45 Ala Thr Val Leu Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Val Arg Leu Val Ala Asp Pro Gln Thr Gly Arg Thr Glu Ala Gln 65 70 75 80 Leu Leu Pro His Phe Asp Thr Ile Thr Tyr Gly Glu Leu Ser Thr Arg 85 90 95 Ile His His Leu Leu Thr Ala Leu Thr Asp Val Asp Pro Gly Asp Arg 100 105 110 Val Ala Ile Leu Gly Phe Thr Ser Val Asp Tyr Thr Val Ile Asp Thr 115 120 125 Thr Leu Val Leu Arg Gly Ala Val Ser Val Pro Leu Gln Thr Ser Ala 130 135 140 Pro Ala Ala Thr Leu Arg Pro Ile Val Ala Glu Thr Glu Pro Val Val 145 150 155 160 Phe Ala Ala Ser Val Asp His Leu Ser Asp Ala Val Asp Leu Val Ala 165 170 175 Asp Ala Glu Ser Val Gly Arg Leu Ile Val Phe Asp Tyr Arg Ala Glu 180 185 190 Val Asp Asp His Arg Asp Ala Ile Ala His Ala Arg Ala Arg Leu Ala 195 200 205 Asp Ala Gly Arg Ser Ile Glu Ile Val Thr Leu Ser Glu Val Leu Ala 210 215 220 His Gly Ala Thr Leu Pro Ala Ala Gln Pro Phe Thr Ser Pro Asp Asp 225 230 235 240 Asp Pro Leu Leu Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro 245 250 255 Lys Gly Ala Met Tyr Pro Glu Arg Leu Ile Thr Asn Ala Trp Arg Arg 260 265 270 Ser Gly Arg Ser Ala Trp Gly Gly Glu Gln Thr Thr Pro Ser Ile Thr 275 280 285 Leu Asn Phe Met Pro Met Ser His Met Met Gly Arg Gly Val Leu Tyr 290 295 300 Gly Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Ala Ala Arg Ser Asp 305 310 315 320 Leu Ser Thr Phe Leu Asp Asp Leu Ala Leu Val Arg Pro Thr Gln Leu 325 330 335 Ser Phe Val Pro Arg Ile Trp Asp Thr Ile Ala Ala Glu Val Ala Lys 340 345 350 Glu Val Asp Arg Arg Pro Asp Asp Leu Ala Asp Val Tyr Ala Asp Leu 355 360 365 Arg Gln Ser Leu Leu Gly Gly Arg His Val Met Ala Met Ser Gly Ser 370 375 380 Ala Pro Leu Ser Pro Glu Met Arg Thr Phe Val Glu Asp Leu Ile Asp 385 390 395 400 Ile His Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Ala Val Phe 405 410 415 Val Asp Gly Gln Val Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val 420 425 430 Asp Val Pro Asp Leu Gly Tyr Phe Thr Thr Asp Arg Pro His Pro Arg 435 440 445 Gly Glu Leu Leu Val Lys Ser Glu Thr Leu Phe Pro Gly Tyr Tyr Lys 450 455 460 Arg Pro Glu Val Thr Ala Glu Met Phe Asp Pro Asp Gly Tyr Tyr Arg 465 470 475 480 Thr Gly Asp Val Val Ala Glu Thr Gly Pro Asp Gln Leu Val Tyr Leu 485 490 495 Asp Arg Arg Asn Asn Val Gln Lys Leu Ser Gln Gly Glu Phe Val Thr 500 505 510 Val Ser Lys Leu Glu Ala Val Phe Gly Asp Ser Pro Arg Val Arg Gln 515 520 525 Ile Tyr Val Tyr Gly Asn Ser Ala Arg Ser Tyr Leu Leu Ala Val Val 530 535 540 Val Pro Thr Glu Asp Val Leu Gly Arg Asp Asp Ala Lys Ala Leu Val 545 550 555 560 Ala Glu Ser Leu Gln Asn Val Ala Arg Ala Ala Gly Leu Gln Ser Tyr 565 570 575 Glu Ile Pro Arg Asp Phe Leu Ile Glu Pro Thr Pro Phe Thr Leu Glu 580 585 590 Asn Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala Arg Pro Arg Leu Lys 595 600 605 Glu His Tyr Gly Glu Gln Leu Glu Ala Leu Tyr Ala Glu Leu Ala Asp 610 615 620 Gly Gln Ala Asp Glu Met Arg Thr Leu Arg Ala Asp Gly Ala Asn Arg 625 630 635 640 Pro Val Leu Glu Thr Val Gly Arg Ala Ala Ala Ala Leu Leu Gly Thr 645 650 655 Ala Ala Thr Asp Val Gln Pro Asp Ala His Phe Thr Asp Leu Gly Gly 660 665 670 Asp Ser Leu Ser Ala Leu Thr Phe Gly Asn Leu Leu Arg Asp Ile Phe 675 680 685 Asp Val Glu Val Pro Val Gly Val Ile Val Ser Pro Ala Thr Asp Leu 690 695 700 Ala Ser Leu Ala Ala Tyr Ile Glu Ala Gln Arg Gln Pro Gly Ala Lys 705 710 715 720 Arg Pro Thr Phe Thr Ala Val His Gly Ala Gly Ala Thr Glu Ala Arg 725 730 735 Ala Arg Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Glu Thr Leu Ser 740 745 750 Ala Ala Pro Ser Leu Pro Gly Pro Asn Thr Glu Val Arg Thr Val Leu 755 760 765 Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Asp Trp 770 775 780 Leu Glu Arg Met Asp Leu Val Asp Gly Lys Val Ile Cys Leu Val Arg 785 790 795 800 Ala Lys Asp Asp Asp Ala Ala Arg Ala Arg Leu Asp Ala Thr Phe Asp 805 810 815 Ser Gly Asp Glu Thr Leu Leu Ala His Tyr Arg Glu Leu Ala Ala Asp 820 825 830 His Leu Glu Val Leu Ala Gly Asp Lys Gly Glu Ala Asp Leu Gly Leu 835 840 845 Asp Pro Gln Val Trp Gln Arg Leu Ala Asp Thr Val Asp Leu Ile Val 850 855 860 Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Glu Leu Phe 865 870 875 880 Gly Pro Asn Ala Val Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr 885 890 895 Thr Arg Ile Glu Pro Gly Lys Phe Val Glu Asp Gly Asp Ile Arg Gln 900 905 910 Ile Ser Ala Val Arg Gln Ile Asp Glu Ser Tyr Ala Asn Gly Tyr Gly 915 920 925 Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu 930 935 940 Cys Gly Leu Pro Val Ser Val Phe Arg Cys Asp Met Ile Leu Ala Asp 945 950 955 960 Thr Thr Tyr Ala Gly Gln Leu Asn Leu Pro Asp Met Phe Thr Arg Leu 965 970 975 Met Phe Ser Leu Val Ala Thr Gly Val Ala Pro Glu Ser Phe Tyr Gln 980 985 990 Leu Asp Ala Asp Gly Gln Arg Pro Arg Ala His Tyr Asp Gly Leu Pro 995 1000 1005 Val Glu Phe Ile Ala Glu Ala Ile Ser Thr Leu Gly Ala Ala Val 1010 1015 1020 Ala Arg Glu Ser Lys Ser Gly Phe Glu Thr Tyr His Val Met Asn 1025 1030 1035 Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu Phe Val Asp Trp Leu 1040 1045 1050 Ile Glu Ala Gly Tyr Pro Val His Arg Val Gly Asp Tyr Ala Ala 1055 1060 1065 Trp Leu Ala Arg Phe Thr Ala Ala Ile Asn Ala Leu Pro Glu Arg 1070 1075 1080 Lys Arg Gln Ala Ser Leu Leu Pro Leu Leu His Asn Tyr Gln Arg 1085 1090 1095 Pro Glu Ile Pro Ile Ser Gly Ser Ile Ala Pro Thr Asp Arg Phe 1100 1105 1110 Arg Thr Ala Val Gln Glu Ala Lys Ile Gly Pro Asp Lys Asp Ile 1115 1120 1125 Pro His Ile Thr Pro Ala Val Ile Val Gln Tyr Val Ser Asn Leu 1130 1135 1140 Glu Leu Leu Gly Leu Leu 1145 <210> 191 <211> 1184 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. bolletii <400> 191 Met Thr Val Thr Asn Glu Thr Asn Pro Gln Gln Glu Gln Leu Ser Arg 1 5 10 15 Arg Ile Glu Ser Leu Arg Glu Ser Asp Pro Gln Phe Arg Ala Ala Gln 20 25 30 Pro Asp Pro Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu 35 40 45 Ser Glu Ala Ile Ala Ala Leu Met Thr Gly Tyr Ala Glu Arg Pro Ala 50 55 60 Leu Gly Glu Arg Ala Arg Glu Leu Val Thr Asp Gln Asp Gly Arg Thr 65 70 75 80 Thr Leu Arg Leu Leu Pro Arg Phe Asp Thr Thr Thr Tyr Gly Glu Leu 85 90 95 Trp Ser Arg Thr Thr Ser Val Ala Ala Ala Trp His His Asp Ala Ala 100 105 110 His Pro Val Gln Ala Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser 115 120 125 Ile Asp Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val 130 135 140 Ala Val Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Trp Thr Thr Ile 145 150 155 160 Leu Ala Glu Ala Glu Pro Asn Thr Leu Ala Val Ser Ile Glu Leu Ile 165 170 175 Gly Ala Ala Leu Glu Ser Val Arg Ala Thr Pro Ser Ile Lys Gln Val 180 185 190 Val Val Phe Asp Tyr Thr Pro Glu Val Asp Asp Gln Arg Glu Ala Phe 195 200 205 Glu Ala Ala Asn Thr Gln Leu Ala Gly Thr Gly Ile Ala Ile Glu Thr 210 215 220 Leu Gly Ala Val Ile Ala Arg Gly Ala Ala Leu Pro Ala Ala Pro Leu 225 230 235 240 Tyr Ala Pro Ser Ala Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile 260 265 270 Val Arg Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn 275 280 285 Leu Pro Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly 290 295 300 Arg Gly Thr Leu Thr Ser Thr Leu Ser Thr Gly Gly Thr Gly Tyr Phe 305 310 315 320 Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile 325 330 335 Arg Pro Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe 340 345 350 Gln Arg Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Ser Gly Asp Ala 355 360 365 Ala Ser Ala Glu Ala Val Ala Ala Glu Val Lys Ala Asp Ile Arg Asp 370 375 380 Asn Leu Phe Gly Gly Arg Val Ser Ala Val Met Val Gly Ser Ala Pro 385 390 395 400 Leu Ser Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu Asn 405 410 415 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp 420 425 430 Gly Ile Val Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro His Pro Arg Gly Glu 450 455 460 Leu Leu Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Gly Val Phe Asp Ala Asp Gly Phe Tyr Met Thr Gly 485 490 495 Asp Ile Val Ala Glu Leu Ala His Asp Asn Ile Glu Ile Ile Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 515 520 525 Thr Leu Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr 530 535 540 Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 545 550 555 560 Thr Pro Glu Ala Val Ala Ala Ala Lys Gly Asp Ala Ala Ala Leu Lys 565 570 575 Thr Thr Ile Ala Asp Ser Leu Gln Asp Ile Ala Lys Glu Ile Arg Leu 580 585 590 Gln Ser Tyr Glu Val Pro Arg Asp Phe Ile Ile Glu Pro Gln Pro Phe 595 600 605 Thr Gln Asp Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro 610 615 620 Asn Leu Lys Ala His Tyr Gly Pro Arg Leu Glu Gln Met Tyr Ala Glu 625 630 635 640 Ile Ala Glu Gln Gln Ala Ala Glu Leu Arg Ala Leu His Gly Val Asp 645 650 655 Pro Asp Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala Leu 660 665 670 Leu Gly Val Ser Ser Ala Glu Leu Ala Ala Asp Ala His Phe Thr Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Asp Leu Leu Arg 690 695 700 Asp Ile Phe Ala Val Glu Val Pro Val Gly Val Ile Val Ser Ala Ala 705 710 715 720 Asn Asp Leu Gly Gly Val Ala Lys Phe Val Asp Glu Gln Arg Tyr Ser 725 730 735 Gly Gly Thr Arg Pro Thr Ala Glu Thr Val His Gly Ala Gly His Thr 740 745 750 Glu Ile Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala 755 760 765 Thr Leu His Ala Ala Pro Ser Leu Pro Lys Ala Val Gly Ile Pro His 770 775 780 Thr Val Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly His Tyr Leu Ala 785 790 795 800 Leu Glu Trp Leu Glu Arg Leu Asp Lys Thr Asp Gly Thr Leu Ile Ala 805 810 815 Ile Val Arg Gly Lys Asn Ala Glu Ala Ala Tyr Arg Arg Leu Glu Glu 820 825 830 Ala Phe Asp Thr Gly Asp Thr Gln Leu Leu Ala His Phe Arg Ser Leu 835 840 845 Ala Asp Lys His Leu Glu Val Leu Ala Gly Asp Ile Gly Asp Pro Asn 850 855 860 Leu Gly Leu Asp Ala Asp Thr Trp Gln Arg Leu Ala Asp Thr Val Asp 865 870 875 880 Val Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Val Lys Leu 900 905 910 Ala Ile Thr Thr Lys Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ala 915 920 925 Val Ala Ala Tyr Val Asp Pro Ser Thr Phe Asp Glu Glu Ser Asp Ile 930 935 940 Arg Ala Ile Ser Ala Val Arg Pro Val Asp Glu Leu Tyr Ala Asn Gly 945 950 955 960 Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Arg Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Gly Ser 1010 1015 1020 Phe Tyr Gln Ala Gln Ala Thr Gly Glu Arg Pro Pro Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Gly Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Thr Gln Val Ile Asp Ser Tyr Glu Thr Tyr Asp Cys Val Asn 1055 1060 1065 Pro His Ala Asp Gly Val Ser Leu Asp Asn Phe Val Asp Trp Leu 1070 1075 1080 Ile Glu Ala Gly Tyr Pro Ile Ala Arg Ile Asp Asn Tyr Ala Gln 1085 1090 1095 Trp Phe Thr Arg Phe Asp Thr Ala Ile Arg Gly Leu Pro Glu Lys 1100 1105 1110 Gln Lys Gln His Ser Leu Leu Pro Leu Leu His Ala Phe Glu Gln 1115 1120 1125 Pro Ser Ala Ala Glu Asn His Gly Val Val Pro Ala Lys Arg Phe 1130 1135 1140 Gln His Ala Val Gln Ala Ala Gly Ile Gly Ala Ile Gly Gln Asp 1145 1150 1155 Gly Thr Thr Asp Ile Pro His Leu Ser Arg Pro Leu Ile Val Lys 1160 1165 1170 Tyr Ala Lys Asp Leu Glu Gln Leu Gly Leu Leu 1175 1180 <210> 192 <211> 1175 <212> PRT <213> Artificial Sequence <220> <223> Curtobacterium sp. MCBA15_012 <400> 192 Met Glu Gln Pro Val Gln Ala His Asp Val Gln Gly Arg Gly Glu Gln 1 5 10 15 Gly Leu Val Asp Thr Ser Val Glu Ala Val Phe Ala Gln His Ala Asp 20 25 30 Arg Pro Ala Leu Arg His Arg Asp Gly Ala Thr Val Thr Asp Thr Ser 35 40 45 Tyr Arg Glu Leu Trp Glu Arg Ala Gly Ala Val Ala Ala Ala Leu Gly 50 55 60 Glu Thr Val Thr Pro Gly Asp Arg Ile Ala Val Leu Gly Ala Pro Thr 65 70 75 80 Ala Asp Leu Leu Thr Leu Asp Leu Ala Ala Trp Ile Leu Gly Ala Val 85 90 95 Ser Val Pro Leu Gln Ala Ser Ala Pro Val Gly Ala Leu Arg Ala Ile 100 105 110 Val Asp Glu Thr Glu Pro Val Trp Leu Gly Val Thr Ala Glu His Ala 115 120 125 Ala Thr Ala Arg Ala Val Thr Glu Glu Thr Asp Ala Asp Val Arg Thr 130 135 140 Val Leu Leu Asp Gly Thr Gly Ser Glu Asp Gly Asp Gly Asp Gly Ser 145 150 155 160 Gly Asp Ser Ala Gly Ser Ala Asp Gly Asp Gly Ser Asp Thr Ala Ala 165 170 175 Ala Pro Ala Thr Leu Glu Ala Leu Val Arg Arg Gly Ala Gly Arg Pro 180 185 190 Arg Pro Thr Pro Trp Gln Pro Ala Pro Gly Glu Asp Pro Leu Ala Leu 195 200 205 Leu Leu Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr 210 215 220 Thr Arg Ala Met Val Glu Arg Leu Trp His Ala Leu Arg Pro Asp Pro 225 230 235 240 Ala Ala Pro Asp Ala Thr Thr Ala Pro Ala Glu Ala Ala Pro Ala Ala 245 250 255 Asp Val Val Gly Tyr Ala Tyr Leu Pro Met Ser His Leu Thr Gly Arg 260 265 270 Ala Ala Val Leu Ala Thr Leu Gly Arg Gly Gly Thr Val Ala Leu Ala 275 280 285 Thr Ser Thr Asp Leu Ser Thr Leu Phe Asp Asp Leu Arg Val Tyr Thr 290 295 300 Pro Thr Glu Leu Val Leu Val Pro Arg Val Ala Glu Met Ile Arg Gln 305 310 315 320 Glu Gly Glu Arg Glu Glu Gln Arg Arg Thr Ala Ala Ala Gly Ala Asp 325 330 335 Ser Asp Pro Ala Ala Val Arg Ala Ala Val Gln Ala Asp Leu Arg Val 340 345 350 Arg Ala Leu Gly Gly Arg Val Arg Gln Ala Ile Cys Ala Ser Ala Pro 355 360 365 Leu Thr Pro Glu Leu Arg Ala Tyr Ile Glu Gly Cys Leu Gly Thr Thr 370 375 380 Leu His Asp Leu Tyr Gly Ser Thr Glu Ala Gly Ser Ile Leu Arg Asp 385 390 395 400 Gly Val Val Gln Gln Pro Pro Val Thr Glu His Lys Leu Val Asp Val 405 410 415 Pro Glu Leu Gly Tyr Arg Val Thr Asp Arg Pro His Pro Arg Gly Glu 420 425 430 Leu Leu Val Lys Ser Thr Ala Val Ile Pro Gly Tyr Phe Arg Arg Pro 435 440 445 Asp Val Thr Ala Ala Val Phe Asp Glu Asp Gly Phe Tyr Arg Thr Gly 450 455 460 Asp Val Met Ala Gln Thr Gly Pro Asp Thr Tyr Glu Tyr Leu Asp Arg 465 470 475 480 Arg Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 485 490 495 Ala Leu Glu Ala Val Tyr Gly Gly Thr Pro Glu Val Arg Gln Val Ala 500 505 510 Leu His Gly Asp Ser Arg His Ala Phe Leu Leu Ala Val Val Val Pro 515 520 525 Glu Asp Pro Ala Ala Thr Glu His Asp Val Leu Ala Ala Leu Gln Arg 530 535 540 Thr Ala Arg Glu Asn Gly Leu Ala Pro Tyr Glu Val Pro Arg Gly Val 545 550 555 560 Ile Val Glu Pro Asp Pro Phe Thr Val Glu Asn Gly Met Leu Ser Asp 565 570 575 Ala Arg Lys Leu Leu Arg Pro Arg Phe Thr Glu Arg Tyr Gly Glu Arg 580 585 590 Phe Ala Ala Val Tyr Asp Ala Val Ala Glu Gln Gln Ser Gly Ile Leu 595 600 605 Val Ala Ala Leu Arg Glu His Val Ala Asp Glu Pro Thr Val Asp Thr 610 615 620 Val Val Arg Ala Ala Arg Glu Phe Leu Gly Ala Glu Val Ser Thr Glu 625 630 635 640 Thr Ala Ala Ala Ala Arg Phe Ser Asp Leu Gly Gly Asp Ser Leu Ser 645 650 655 Ala Leu Thr Phe Ser Gly Ile Leu Glu Asp Val Phe Glu Ala Glu Val 660 665 670 Pro Val Gly Val Ile Thr Asp Pro Thr Asn Asp Leu Ala Ala Val Ala 675 680 685 Ala Tyr Val Glu Arg Thr Ala Ala Glu Asp Arg Pro Thr Val Thr Arg 690 695 700 Val His Gly Ala Asp Pro Thr Val Leu Arg Ala Glu Asp Leu Arg Leu 705 710 715 720 Asp Arg Leu Leu Gly Thr Val Pro Glu Pro Val Thr Arg Ala Thr Ser 725 730 735 Glu Gly Gln Gly Pro Thr Ser Thr Ser Thr Ser Thr Asp Pro Asp Thr 740 745 750 Ser Ala Gly Thr Gly Ala Gly Thr Thr Pro Arg Thr Val Leu Leu Thr 755 760 765 Gly Ala Asn Gly Tyr Leu Gly Arg Phe Thr Ala Ile Asp Trp Leu Glu 770 775 780 Arg Leu Ala Pro Val Gly Gly Thr Leu Val Cys Leu Val Arg Gly Ala 785 790 795 800 Asp Asp Ala Asp Ala Arg Arg Arg Leu Glu Ala Ala Phe Thr Ala Asp 805 810 815 Pro Ala Phe Ala Ala Arg Phe Ala Glu Leu Gly Gly Ala Leu Glu Val 820 825 830 Val Ala Gly Asp Val Ser Glu His Leu Leu Gly Leu Asp Glu Gly Arg 835 840 845 Trp His Asp Leu Ala Ala Arg Val Asp Leu Val Ala His Val Ala Ala 850 855 860 Leu Val Asn His Val Leu Pro Tyr Thr Ala Leu Phe Gly Pro Asn Val 865 870 875 880 Val Gly Thr Ala Glu Val Leu Arg Leu Ala Ile Ala Ala Gly Ser Val 885 890 895 Pro Val Thr Phe Val Ser Ser Val Ala Val Ala Gly Gly Ala Arg Pro 900 905 910 Ser Ala Thr Glu Asp Val Ala Pro Asp Val Pro Ala Ala Leu Leu Glu 915 920 925 Arg Ala Asp Val Arg Thr Thr Ile Pro Thr Trp Thr Ile Ala Asp Glu 930 935 940 Tyr Ala Asn Gly Tyr Gly Ala Ser Lys Trp Ala Ser Glu Val Leu Leu 945 950 955 960 His Asp Ala His Glu Arg Tyr Gly Val Pro Val Ala Val Phe Arg Ser 965 970 975 Asp Met Val Leu Ala His Pro Arg Trp Arg Gly Gln Val Asn Leu Pro 980 985 990 Asp Val Phe Thr Arg Leu Val Trp Ser Val Leu Ala Thr Gly Leu Ala 995 1000 1005 Pro Ala Ser Phe Val Gln Pro Ala Pro Asp Gly Gly Arg Gln Arg 1010 1015 1020 Ser His Tyr Asp Gly Leu Pro Ala Asp Phe Thr Ala Ala Ala Ile 1025 1030 1035 Asp Ala Ile Gly Ala Ala Val Thr Glu Gly Tyr Arg Thr Phe Asn 1040 1045 1050 Val Val Asn Pro His Asp Asp Gly Val Ser Leu Asp Thr Phe Val 1055 1060 1065 Asp Trp Leu Val Glu Asp Gly His Pro Val Glu Arg Val Ala Asp 1070 1075 1080 His Ala Glu Trp Val Thr Arg Phe Arg Asp Ala Leu Thr Ala Leu 1085 1090 1095 Pro Glu Glu Asp Arg Ala Arg Ser Val Leu Pro Leu Leu His Ala 1100 1105 1110 Phe Ala Ala Pro Glu Ala Pro His Ala Asp Ser Ser Ile Pro Ala 1115 1120 1125 Asp Asp Phe Ala Ala Ala Val Arg Asp Val Arg Pro Leu Gly Ser 1130 1135 1140 Pro Glu Ile Pro Pro Leu Asp His Ala Leu Ile Ser Lys Val Ala 1145 1150 1155 Asp Asp Leu Thr Tyr Leu Gly Leu Leu Ala Pro Ala His Val Gly 1160 1165 1170 Ala Arg 1175 <210> 193 <211> 1183 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. abscessus <400> 193 Met Thr Ile Asp Ala Thr Ala Asp Asn Thr Lys Glu Ala Arg Arg Gln 1 5 10 15 Arg Leu Gly Asp Arg Ile Arg Arg Leu Phe Thr Asp Asp Glu Gln Phe 20 25 30 Arg Ala Ala Lys Pro Asp Thr Ala Val Asp Thr Ala Val Ala Gln Pro 35 40 45 Gly Leu Arg Leu Ala Gln Val Val Ala Thr Ile Met Asn Gly Tyr Ala 50 55 60 Asp Arg Pro Ala Leu Gly His Arg Val Gln Glu Leu Val Ala Asp Ala 65 70 75 80 Ala Gly Arg Ser Thr Leu Arg Pro Leu Pro Glu Phe Glu Thr Val Thr 85 90 95 Tyr Gly Glu Leu Trp Gly Met Ala Arg Ala Leu Ala Ser Thr Trp Tyr 100 105 110 His Asp Pro Ala Ala Pro Val Arg Ala Gly Asp Phe Val Ala Met Leu 115 120 125 Gly Phe Thr Ser Val Asp Tyr Thr Ala Val Asp Leu Ala Cys Ile His 130 135 140 Leu Gly Ala Val Ala Val Pro Leu Gln Thr Ser Ala Ser Ala Ser Asn 145 150 155 160 Trp Thr Ala Ile Leu Ala Glu Ser Gly Pro Ala Val Leu Ala Val Ser 165 170 175 Ala Glu Leu Leu Asp Thr Ala Met Glu Ser Val Leu Ala Thr Pro Ser 180 185 190 Leu Arg His Ile Thr Val Phe Asp Tyr His Pro Gly Val Asp Val Gln 195 200 205 Arg Glu Ser Leu Glu Ser Ala Gln His Arg Ile Ala Glu Ala Gly Leu 210 215 220 Pro Ile Ser Val Asp Pro Ile Ser Leu Ala Ile Gly His Gly Arg Ala 225 230 235 240 Leu Pro Asp Ala Pro Leu Phe Thr Ala Glu Glu Gly Thr Asp Pro Leu 245 250 255 Ala Leu Val Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 260 265 270 Thr Tyr Ser Glu Lys Met Val Ala Lys Pro Trp Leu Arg Ala Asp Thr 275 280 285 Leu Ser Ser Lys Ala Glu Ile Pro Leu Ile Asn Leu Asn Phe Met Pro 290 295 300 Met Ser His Val Met Gly Arg Gly Ser Leu Val Thr Ala Leu Ala Cys 305 310 315 320 Gly Gly Leu Ala Tyr Phe Ala Ala Ser Ser Asp Met Ser Thr Leu Phe 325 330 335 Glu Asp Ile Thr Leu Thr Arg Pro Thr Val Val Thr Leu Val Pro Arg 340 345 350 Val Cys Asp Met Leu Phe Gln Arg Tyr Arg Asn Glu Val Glu Arg Arg 355 360 365 Ala Gly Leu Asp Pro Ala Ala Asp Leu Ala Thr Leu Asp Ala Asp Val 370 375 380 Lys Thr Asp Ile Arg Glu Asn Leu Phe Gly Gly Arg Val Leu Thr Ile 385 390 395 400 Val Cys Gly Ser Ala Pro Leu Ser Glu Glu Leu Ala Ala Phe Ile Glu 405 410 415 Ser Cys Leu Asp Ala Arg Ile Thr Asp Gly Tyr Gly Ser Thr Glu Ala 420 425 430 Gly Val Ile Val Arg Asn Gly Arg Ile Gln Arg Pro Pro Val Ile Asp 435 440 445 Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys 450 455 460 Pro His Pro Arg Gly Glu Leu Leu Val Lys Ala Glu Ser Val Phe Gly 465 470 475 480 Gly Tyr Phe Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Pro Asp 485 490 495 Gly Tyr Tyr Lys Thr Gly Asp Ile Val Ala Glu Leu Glu Pro Asp Lys 500 505 510 Ile Gln Ile Val Asp Arg Arg Asn Asn Val Ile Lys Leu Ser Gln Gly 515 520 525 Glu Phe Val Ala Ile Ala Asn Leu Glu Ala Glu Phe Ala Asn Ser Pro 530 535 540 Leu Val His Gln Ile Cys Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu 545 550 555 560 Leu Ala Val Val Val Pro Thr Ala Glu Ala Tyr Glu Gln Ser Gly Gly 565 570 575 Asp Glu Asp Leu Leu Lys Arg Leu Ile Ala Asp Ser Leu Ala Gln Val 580 585 590 Ala Arg Glu Ala Gln Leu Gln Ser Tyr Glu Val Pro Arg Asp Phe Leu 595 600 605 Leu Glu Thr Glu Pro Phe Thr Ala Ala Asn Gly Leu Leu Thr Gly Ile 610 615 620 Ala Lys Leu Ala Arg Pro Lys Leu His Glu Lys Tyr Gly Ala Arg Leu 625 630 635 640 Glu Gln Leu Tyr Ser Asp Ile Ala Ala Ala Gln Ala Leu Glu Leu Gln 645 650 655 Ala Leu His Ser Ala Gly His Glu Asp Lys Pro Val Leu Asp Thr Val 660 665 670 Gln Arg Ala Val Thr Ala Leu Leu Gly Leu Ser Ala Ala Glu Val Ser 675 680 685 Pro Asp Ala His Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu 690 695 700 Ala Phe Ser Asp Leu Leu Arg Asp Ile Phe Thr Val Glu Val Pro Val 705 710 715 720 Gly Asp Ile Val Ser Ala Ala Asn Asp Leu Thr Ala Ile Ala Arg Thr 725 730 735 Val Glu Arg His Arg Glu Ala Asp Gly His Ser Val Thr Pro Thr Ala 740 745 750 Glu Ser Val His Gly Ala Gly His Arg Glu Ile Arg Ala Ala Asp Leu 755 760 765 Thr Leu Asp Lys Phe Ile Asp Ala Asp Thr Leu Arg Ala Ala Pro Ala 770 775 780 Leu Ser Thr Phe Thr Gly Thr Pro His Thr Val Leu Leu Thr Gly Ala 785 790 795 800 Asn Gly Tyr Leu Gly Arg Phe Leu Ala Leu Glu Trp Leu Glu Arg Leu 805 810 815 Asp Lys Ile Gly Gly Thr Leu Ile Val Ile Val Arg Gly Lys Asn Ala 820 825 830 Glu Ala Ala Tyr Arg Arg Leu Glu Glu Ala Phe Asp Ser Gly Asp Ala 835 840 845 Gly Leu Leu Ala His Phe Arg Ser Leu Ala Arg Gln His Leu Glu Val 850 855 860 Leu Pro Gly Asp Ile Gly Asp Pro Asp Leu Gly Leu Asp Ala Asp Thr 865 870 875 880 Trp Gln Arg Leu Ala Glu Thr Val Asp Val Ile Val His Pro Ala Ala 885 890 895 Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val 900 905 910 Val Gly Thr Ala Glu Ile Ile Lys Leu Ala Leu Thr Thr Lys Ile Lys 915 920 925 Pro Ile Thr Tyr Leu Ser Thr Val Ala Val Ala Ile Ser Val Asp Pro 930 935 940 Lys Val Phe Asp Glu Asp Ser Asp Ile Arg Thr Ile Ser Ala Val Arg 945 950 955 960 Pro Ile Asn Asp Gly Tyr Ala Asn Gly Tyr Gly Asn Ala Lys Trp Ala 965 970 975 Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val 980 985 990 Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Arg Arg Tyr Thr Gly 995 1000 1005 Gln Leu Asn Val Pro Asp Gln Phe Thr Arg Leu Ile Leu Ser Leu 1010 1015 1020 Ile Ala Thr Gly Val Ala Pro Gly Ser Phe Tyr Gln Ala His Ala 1025 1030 1035 Thr Gly Glu Arg Pro Leu Ala His Tyr Asp Gly Leu Pro Ala Asp 1040 1045 1050 Phe Thr Ala Ser Ala Ile Thr Ala Leu Gly Pro Ile Glu Gly Phe 1055 1060 1065 His Thr Tyr Asp Ser Val Asn Pro His Ala Asp Gly Ile Ser Leu 1070 1075 1080 Asp Asn Phe Val Asp Trp Leu Ile Glu Ala Gly Tyr Pro Ile Ala 1085 1090 1095 Arg Ile Asp Asn Tyr Thr Glu Trp Phe Thr Arg Phe Asp Thr Ala 1100 1105 1110 Ile Arg Gly Leu Pro Glu Lys Gln Lys Gln His Ser Leu Leu Pro 1115 1120 1125 Leu Leu His Ala Tyr Arg His Pro Gln His Pro His Asn Gly Ala 1130 1135 1140 Phe Leu Pro Ala Ile Arg Phe Ser Glu Gly Val Gln Ala His Leu 1145 1150 1155 Asn Ala Asp Ile Pro His Leu Thr Arg Glu Leu Ile Ala Lys Tyr 1160 1165 1170 Ala Ala Asp Leu Lys Gln Leu Gly Leu Leu 1175 1180 <210> 194 <211> 1188 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium colombiense <400> 194 Met Thr Glu Thr Val Thr Asp Ser Ala Arg Glu Gln Arg Ile Ala Glu 1 5 10 15 Arg Val Glu Gln Leu Tyr Ala Asn Asp Pro Gln Phe Arg Ala Ala Ala 20 25 30 Ser Leu Pro Glu Val Thr Asp Ala Ala His Arg Pro Gly Leu Arg Leu 35 40 45 Ala Glu Val Val Asp Thr Tyr Leu Ser Gly Tyr Ala Asp Arg Pro Ala 50 55 60 Leu Gly Gln Arg Ala Cys Glu Val Val Arg Asp Ala Ser Thr Asp Arg 65 70 75 80 Ala Ala Thr Thr Leu Leu Ser Gly Phe Glu Thr Ile Thr Tyr Arg Glu 85 90 95 Leu Gly Asp Arg Val Ala Ala Leu Ala Ala Ala Trp Gln Ser Gly Leu 100 105 110 Ala Gly Gly Phe Ser Pro Gly Asp Phe Val Gly Val Leu Gly Phe Thr 115 120 125 Ser Ile Asp Tyr Val Val His Tyr Leu Ala Cys Ile Arg Leu Gly Ala 130 135 140 Val Phe Val Pro Leu Gln Thr Ser Ser Thr Ala Ala Gln Leu Gly Pro 145 150 155 160 Ile Val Ala Glu Thr Ala Pro Arg Val Leu Ala Val Ser Val Glu Ser 165 170 175 Leu Thr Thr Ala Val Asp Val Val Ala Gly Ala Pro Ser Val Glu Arg 180 185 190 Leu Val Val Phe Asp Tyr Thr Ser Asp Asp Asp Glu Gln Arg Gly His 195 200 205 Tyr Asp Asp Ala Arg Ala Arg Leu Arg Asp Ala Gly His Arg Ala Glu 210 215 220 Val Val Ser Leu Ser Thr Glu Leu Asp Ser Gly Gly Arg Leu Ala Ala 225 230 235 240 Pro Pro Val Phe Ala Pro Lys Asp Gly Glu Asn Pro Leu Ala Thr Leu 245 250 255 Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr Thr 260 265 270 Ala Asp Met Met Thr Arg Ile Trp Arg Arg Pro His Ser Pro Ser Val 275 280 285 Asp Ile Gly Arg Pro Ile Pro Ala Ile His Leu Gln Tyr Met Pro Leu 290 295 300 Ser His Val Tyr Gly Leu Glu Trp Leu Ile Ala Thr Leu Ser Ser Gly 305 310 315 320 Gly Ile Gly Tyr Phe Ala Ala Lys Ser Asp Met Ser Thr Leu Phe Asp 325 330 335 Asp Ile Gly Leu Val Arg Pro Thr Ala Leu Asn Leu Val Pro Arg Val 340 345 350 Cys Asp Met Phe Phe Arg Arg Tyr Arg Lys Glu Leu Asp Glu Arg Ser 355 360 365 Gly Asp Glu Leu Thr Gly Asp Gln Leu Asp Asp Ala Val Lys Ala Glu 370 375 380 Leu Arg Gln Asp Phe Ile Gly Gly Arg Val Ile Ser Ala Met Cys Gly 385 390 395 400 Ser Ala Pro Leu Ser Lys Gln Met His Ala Phe Met Glu Ser Leu Leu 405 410 415 Asp Ile Pro Val Ala Asp Gly Tyr Gly Ala Thr Glu Thr Gly Gly Gly 420 425 430 Ile Met Arg Ser Gly Arg Ile Arg Arg Pro Pro Val Thr Asp Tyr Lys 435 440 445 Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Thr Thr Asp Lys Pro Tyr 450 455 460 Pro Arg Gly Glu Leu His Leu Lys Ala Ser Asn Val Ile Pro Gly Tyr 465 470 475 480 Phe Lys His Pro Glu Leu Ser Ala Lys Ile Phe Asp Asp Glu Gly Phe 485 490 495 Tyr Arg Thr Gly Asp Ile Met Ala Glu Leu Gly Pro Asp His Leu Met 500 505 510 Tyr Leu Asp Arg Ser Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe 515 520 525 Val Ala Val Ser Gln Leu Glu Ala Thr Phe Ser Thr Ser Pro Tyr Ile 530 535 540 Arg Gln Ile Phe Leu Tyr Gly Ser Ser Glu Gln Pro Phe Leu Leu Ala 545 550 555 560 Val Ile Val Pro Asn Ser Asp Ala Val Gly Asp Gly Asp Ala Arg Ala 565 570 575 Leu Ile Ala Asp Ser Leu Gln Arg Ile Ala Ala Asp Asn His Leu Gln 580 585 590 Pro Tyr Glu Ile Pro Arg Asp Phe Leu Leu Glu Ser Gln Arg Phe Thr 595 600 605 Arg Asp Asn Gly Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Ala 610 615 620 Leu Lys Ala His Tyr Gly Asp Arg Leu Asp Ala Met Tyr Asp Asp Ile 625 630 635 640 Glu Ala Ser His Gly Asn Gln Leu Asp Glu Leu Arg Ala Ala Ser Thr 645 650 655 Glu Leu Pro Thr Ile Asp Thr Val Arg Arg Ala Ala Ala Ala Thr Leu 660 665 670 Gly Leu Pro Ala Asp Thr Ala Leu Arg Ala Asp Ala Lys Phe Ile Glu 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Phe Ser Phe Ala Thr Leu Leu Ser 690 695 700 Glu Ile Phe His Ile Asp Val Pro Val Gln Thr Ile Val Ser Pro Thr 705 710 715 720 Ala Asp Leu Thr Thr Val Ala Asn Phe Val Asp Gly Glu Arg Thr Ser 725 730 735 Val Ser Thr Arg Pro Thr Phe Ala Ser Val His Gly Arg Gly Ala Ala 740 745 750 Val Ala Arg Ala Ala Asp Leu Thr Leu Asp Asn Phe Ile Asp Ala Glu 755 760 765 Thr Leu Ala Ala Ala Pro Arg Leu Pro Ala Ala Thr Gly Thr Ile Asn 770 775 780 Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys 785 790 795 800 Leu Asp Trp Leu Glu Arg Leu Ala Pro Gly Gly Gly Thr Val Ile Cys 805 810 815 Leu Ala Arg Gly Ala Asp Pro Thr Ala Gly Arg Gln Arg Ile Glu Ala 820 825 830 Ala Ile Asp Ser Gly Asp Ala Glu Leu Ser Asp Arg Phe Arg Arg Leu 835 840 845 Ala Asp Lys His Leu Arg Val Leu Val Gly Asp Val Gly Ala Pro Asn 850 855 860 Leu Gly Leu Asn Thr Pro Thr Tyr Gln Arg Leu Ala Glu Ser Val Asp 865 870 875 880 Leu Val Val His Ser Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Val Lys Leu 900 905 910 Ala Ile Thr Lys Arg Leu Lys Pro Ile Asn Tyr Ile Ser Thr Val Ala 915 920 925 Val Thr Ala Leu Pro Asp Gly Ser Phe Ile Gly Glu Asp Val Asp Val 930 935 940 Arg Ser Ala Ser Pro Ala Arg Ser Leu Asp Glu Ser Tyr Ala Ser Gly 945 950 955 960 Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Val Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Asn Phe Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Val Ala Thr Gly Ile Ala Pro Arg Ser 1010 1015 1020 Phe Tyr Gln Leu Asp Ala Ser Gly Asn Pro Gln Arg Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Ala Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Ala Arg Ala Arg Gln Gly Tyr His Thr Tyr Asn Val Leu Asn 1055 1060 1065 Thr His Asp Asp Gly Val Ser Leu Asp Thr Phe Val Asp Trp Leu 1070 1075 1080 Ile Ala Asp Gly His Arg Ile Glu Arg Ile Asp Asp Tyr Arg Gln 1085 1090 1095 Trp Leu Ala Arg Phe Thr Glu Ala Met Glu Ala Leu Pro Glu Lys 1100 1105 1110 Gln Arg Lys Ser Ser Leu Leu Pro Leu Met Asn Ala Tyr Ala Lys 1115 1120 1125 Pro Gly Glu Pro Thr His Gly Thr Gly Met Pro Ala Glu Lys Phe 1130 1135 1140 Arg Ala Ala Val Gln Ser Ala Gly Ile Gly Ala Asp Lys Asp Val 1145 1150 1155 Pro His Val Thr Glu Pro Leu Ile Asp Lys Tyr Val Thr Asp Leu 1160 1165 1170 Gln Arg Leu Gly Leu Leu Arg Thr Arg Thr Gly Ala His Ala Gly 1175 1180 1185 <210> 195 <211> 1129 <212> PRT <213> Artificial Sequence <220> <223> Williamsia sterculiae <400> 195 Met Val Pro Gly Ser Leu Leu Pro Ala Ser Ala Ile Asp Thr Ala Gly 1 5 10 15 Ala Asp Pro Ala Val Val Glu Arg Val Ser Ala Glu Thr Ser Val Ser 20 25 30 Gly Ile Val Ser Val Leu Ala Asp Gly Tyr Gly Asp Arg Ala Ala Met 35 40 45 Ala Trp Arg Pro Gly Asn Ala Arg Ala Trp Arg Thr Leu Thr Tyr Ala 50 55 60 Gln Leu Ala Ser Arg Val Asp Ala Val Ala Thr Ser Leu Val Thr Arg 65 70 75 80 Phe Gly Leu Gly Gln Gly Asp Thr Val Ala Ile Leu Gly Phe Thr Ser 85 90 95 Pro Gly Tyr Ser Ile Val Asp Leu Ala Val Thr Gly Pro Ala Gly Gly 100 105 110 Val Ser Val Pro Leu Gln Thr Gly Ala Ser Pro Ser Ser Trp Gln Gln 115 120 125 Ile Leu Glu Glu Thr Ala Pro Arg Val Leu Ala Val Ala Ala Glu His 130 135 140 Leu Pro Ala Val Thr Gly Ile Leu Ala Ala Met Arg Arg Thr Thr Val 145 150 155 160 Glu His Leu Leu Ile Phe Asp Thr Glu Asp Val Asp Val Asp Asp Leu 165 170 175 Asp Arg Arg Arg Arg Glu Ile Glu Gly Thr Val Ala Gln Leu Thr Thr 180 185 190 Thr Leu His Asp Asp Leu Thr His Asp Val Val Ala Pro Val Arg Arg 195 200 205 Asp Arg Asp Pro Asp Ala Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 210 215 220 Thr Gly Thr Pro Lys Gly Ala Met Tyr Arg Gln Ser Ala Val Ala Arg 225 230 235 240 Met Leu Arg Asn Gly Phe Gly Leu Ala Phe Ser Arg Asp Asp Pro Leu 245 250 255 Arg Trp Val Thr Leu Asn Phe Met Pro Met Ser His Val Met Gly Arg 260 265 270 Thr Thr Leu Leu Gln Thr Leu Gly Asn Gly Gly Thr Ala Phe Phe Thr 275 280 285 Ala Gln Ser Asp Leu Ser Gln Leu Leu Asp Asp Leu Ala Glu Val His 290 295 300 Pro Thr Gln Leu Gln Phe Val Pro Arg Val Trp Glu Met Leu Tyr Arg 305 310 315 320 Glu Tyr Leu Ala Asp Arg Ala Arg Gly Ala Asp Asp Ala Thr Ala Leu 325 330 335 Ser Asp Leu Arg Thr Arg Tyr Leu Gly Ala Gly Glu Val Arg Ala Val 340 345 350 Thr Gly Ser Ala Pro Ile Ser Pro Asp Val Ala Thr Phe Val Gly Asp 355 360 365 Leu Leu Gly Glu Pro Leu Ile Glu Gly Tyr Gly Ser Thr Glu Ser Gly 370 375 380 Gly Val Leu Leu Asn Gly His Ile Thr Arg Pro Pro Val Ile Ala Tyr 385 390 395 400 Arg Leu Arg Asp Val Pro Glu Leu Gly Tyr Arg Ser Thr Asp Arg Pro 405 410 415 His Pro Arg Gly Glu Leu Leu Val Lys Thr Thr Asp Ile Phe Ala Gly 420 425 430 Tyr Tyr Arg Arg Pro Glu Leu Thr Ala Glu Ala Phe Asp Glu Asp Gly 435 440 445 Phe Tyr Arg Thr Gly Asp Ile Val Ala Glu Ile Ala Pro Asp Glu Leu 450 455 460 Arg Tyr Leu Asp Arg Arg Asn Asn Val Ile Lys Leu Ser Gln Gly Glu 465 470 475 480 Phe Val Thr Val Ser His Ala Glu Ala Ala Leu Val Ala Pro Pro Val 485 490 495 Glu Gln Ile Tyr Val Tyr Gly Asn Ser Ser Arg Pro Tyr Leu Leu Ala 500 505 510 Val Val Val Pro Thr Ala Gly Ala Val Val Asp Ala Gly Gly Asp Asp 515 520 525 Asp Ile Leu Arg Ala Arg Val Asn Thr Ala Leu Arg Asp Ile Gly Arg 530 535 540 Asp Ala Gly Leu Ser Ala Val Glu Ile Pro Arg Glu Val Ile Ile Glu 545 550 555 560 Arg Asp Pro Phe Ser Gln His Asn Gly Leu Leu Thr Asn Thr Ala Lys 565 570 575 Leu Ala Arg Pro Ala Leu Lys Ala Arg Tyr Gly Asn Ala Leu Glu Ala 580 585 590 Leu Tyr Gly Glu Leu Glu Ala Gly Arg Asp Asp Lys Leu Arg Leu Ala 595 600 605 Arg Glu Gln Ala Ser Glu Arg Pro Ala Glu Gln Thr Val Ile Asp Val 610 615 620 Ala Thr Ala Leu Leu Asp Leu Ala Glu Gly Asp Ile Gly Pro Gln Ser 625 630 635 640 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Thr Ala Val Thr Leu Gly 645 650 655 Thr Glu Leu Arg Glu Ile Phe Asp Val Glu Val Pro Val Gly Val Ile 660 665 670 Thr Ser Pro Thr Thr Asp Met Ser Gly Leu Ala Ala Phe Val Ala Ala 675 680 685 Pro Gly Gly Gln Arg Pro Thr Ala Ala Ser Ile His Gly Asp Gly Glu 690 695 700 Thr Ile Arg Ala Thr Asp Leu Thr Leu Asp Ala Phe Leu Asp Pro Ser 705 710 715 720 Thr Ile Ala Arg Ala Ser Asp Leu Pro Pro Ala Pro Gly Glu Pro Arg 725 730 735 Thr Val Leu Val Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala 740 745 750 Leu Asp Trp Leu Arg Arg Met Asp Met Ser Gly Gly Thr Val Ile Cys 755 760 765 Leu Val Arg Ala Ser Asp Ala Asp Ala Gly Arg Ile Arg Leu Asp Asp 770 775 780 Ala Phe Asp Thr Gly Asp Asp Glu Leu Leu Ala Glu Tyr His Arg Leu 785 790 795 800 Ala Gly Arg His Leu Arg Val Val Val Ala Asp Lys Ser Ala Arg His 805 810 815 Leu Gly Leu Asp Asp Asp Thr Trp Gln Glu Leu Ala Glu Thr Val Asp 820 825 830 Leu Ile Val Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr His 835 840 845 Glu Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Leu Ile Glu Leu 850 855 860 Ala Leu Thr Glu Cys Val Lys Pro Tyr Val Tyr Val Ser Thr Val Gly 865 870 875 880 Val Ala Thr Gln Ile Ala Pro Ala Glu Phe Val Glu Asp Ala Asp Ile 885 890 895 Arg Glu Ile Ser Ala Thr Arg Arg Leu Asp His Gly Tyr Ala Ser Gly 900 905 910 Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 915 920 925 Glu His Leu Ser Leu Pro Val Thr Val Phe Arg Cys Asp Met Ile Leu 930 935 940 Ala Asp Asp His Asp Leu Gly Gln Leu Asn Leu Pro Asp Met Phe Thr 945 950 955 960 Arg Leu Leu Met Ser Val Leu Ala Thr Gly Leu Ala Pro Arg Ser Phe 965 970 975 His Glu Leu Gly Pro Asp Gly Ser Pro Ile Pro Ser His Tyr Asp Ala 980 985 990 Leu Pro Val Asp Phe Leu Ala Ala Ala Ile Asn Ala Leu Val Asp Asp 995 1000 1005 Asp Gly Phe Ser Thr Tyr His Ala Met Asn Pro His Glu Asp Gly 1010 1015 1020 Val Gly Leu Asp Arg Tyr Val Asp Trp Leu Ile Asp Asp Gly Ala 1025 1030 1035 Glu Ile Thr Arg Val Asp Asp Tyr Asp Glu Trp Phe Thr Arg Phe 1040 1045 1050 Gly Glu Ala Ile Thr Asn Leu Pro Asp Thr Gln Arg Arg His Ser 1055 1060 1065 Leu Leu Pro Leu Leu Asp Asn Tyr Ala Arg Pro Thr Ser Ala Val 1070 1075 1080 Ile Gly Gly Ile Ala Pro Ala Asp Arg Phe Arg Asp Ala Val Arg 1085 1090 1095 Arg Ala Lys Val Gly Arg His Lys Asp Ile Pro His Ile Thr Pro 1100 1105 1110 Gly Ile Ile Ala Asn Tyr Ala Arg Gly Leu Arg His Leu Gly Leu 1115 1120 1125 Thr <210> 196 <211> 1194 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides chelonae <400> 196 Met Thr Val Thr Asn Glu Thr Asp Pro Gln Leu Glu Gln Leu Ala Arg 1 5 10 15 Arg Ile Glu Asn Leu Arg Glu Ser Asp Pro Gln Phe Arg Ala Thr Ala 20 25 30 Pro Asp Arg Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu 35 40 45 Ser Glu Ala Ile Ala Thr Leu Met Thr Gly Tyr Ala Glu Arg Pro Ala 50 55 60 Leu Gly Glu Arg Ala Arg Glu Leu Ala Thr Asp His Glu Gly Arg Ser 65 70 75 80 Val Leu Arg Leu Leu Pro Arg Phe Asp Thr Thr Thr Tyr Gly Glu Leu 85 90 95 Trp Ser Arg Thr Thr Ser Val Ala Ala Tyr Trp His His Asp Ala Ala 100 105 110 His Ser Val Asn Ser Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser 115 120 125 Val Asp Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val 130 135 140 Ala Val Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Trp Thr Thr Ile 145 150 155 160 Leu Ala Glu Thr Glu Pro Asn Thr Leu Ala Val Ser Val Glu Leu Ile 165 170 175 Gly Thr Ala Leu Glu Ser Val Leu Ala Thr Pro Ser Val Lys Gln Val 180 185 190 Val Val Phe Asp Tyr Thr Pro Glu Val Asp Ala Gln Arg Glu Ala Phe 195 200 205 Asp Ala Ala Ser Ala Gln Leu Ala Gly Thr Gly Ile Thr Ile Glu Thr 210 215 220 Leu Asp Ala Val Ile Ala Arg Gly Ala Gln Leu Pro Ala Ala Pro Leu 225 230 235 240 Tyr Ala Pro Ser Asp Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile 260 265 270 Val Arg Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn 275 280 285 Leu Pro Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly 290 295 300 Arg Gly Thr Leu Thr Ser Thr Leu Ser Thr Gly Gly Leu Gly Tyr Phe 305 310 315 320 Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile 325 330 335 Arg Pro Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe 340 345 350 Gln Arg Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Ser Gly His Ala 355 360 365 Ala Asp Ser Asp Ala Val Ala Ala Glu Val Lys Ala Glu Ile Arg Asp 370 375 380 Asn Leu Phe Gly Gly Arg Val Leu Ala Val Met Val Gly Ser Ala Pro 385 390 395 400 Leu Ser Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu His 405 410 415 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp 420 425 430 Gly Val Val Gln Arg Pro Pro Val Ile Glu Tyr Lys Leu Val Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Gln Pro His Pro Arg Gly Glu 450 455 460 Leu Leu Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Gly Val Phe Asp Glu Asp Gly Phe Tyr Met Thr Gly 485 490 495 Asp Ile Val Ser Glu Leu Thr His Asp Asn Ile Gln Ile Val Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 515 520 525 Thr Leu Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr 530 535 540 Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 545 550 555 560 Thr Pro Glu Ala Val Ala Ala Ala Lys Gly Asp Thr Ala Ala Leu Lys 565 570 575 Val Thr Ile Ala Asp Ser Leu Gln Asp Ile Ala Arg Glu Ile Gln Leu 580 585 590 Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile Val Glu Pro Gln Pro Phe 595 600 605 Thr Gln Gly Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro 610 615 620 Asn Leu Lys Ser His Tyr Gly Asp Arg Leu Glu Gln Met Tyr Ala Asp 625 630 635 640 Ile Ala Glu Gln Gln Ser Leu Glu Met His Arg Leu Arg Ser Asp Tyr 645 650 655 Asp Pro Asp Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala 660 665 670 Leu Leu Gly Val Ser Ser Ala Glu Leu Ala Val Leu Pro Ser Asp Ala 675 680 685 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser 690 695 700 Asp Leu Leu Arg Asp Ile Phe Ala Val Glu Val Pro Val Gly Val Ile 705 710 715 720 Val Ser Ala Ala Asn Asp Leu Ser Gly Ile Ala Lys Phe Val Asp Glu 725 730 735 Gln Arg His Ser Gly Gly Asn Arg Pro Thr Ala Glu Thr Val His Gly 740 745 750 Ala Gly His Thr Glu Ile Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe 755 760 765 Ile Asp Glu Ala Thr Leu Gln Ala Ala Pro Ser Leu Pro Arg Ala Val 770 775 780 Gly Val Pro Gln Thr Val Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly 785 790 795 800 His Tyr Leu Ala Leu Glu Trp Leu Glu Arg Leu Asp Lys Thr Glu Gly 805 810 815 Lys Leu Ile Val Ile Val Arg Gly Lys Asp Ala Asp Ala Ala Tyr Arg 820 825 830 Arg Leu Glu Glu Ala Phe Asp Thr Gly Asp Thr Glu Leu Leu Ala His 835 840 845 Phe Arg Thr Leu Ala Glu Lys His Leu Glu Val Leu Ala Gly Asp Ile 850 855 860 Gly Asp Pro Asn Leu Gly Leu Glu Ala Asp Thr Trp Gln Arg Leu Ala 865 870 875 880 Asp Thr Val Asp Val Ile Val His Pro Ala Ala Leu Val Asn His Val 885 890 895 Leu Pro Tyr Lys Gln Leu Phe Gly Pro Asn Val Val Gly Thr Gly Glu 900 905 910 Ile Ile Lys Leu Ala Leu Thr Thr Lys Ile Lys Pro Ile Thr Tyr Leu 915 920 925 Ser Thr Val Ala Val Ala Ala Tyr Val Asp Pro Ala Thr Phe Asp Glu 930 935 940 Glu Ser Asp Ile Arg Leu Ile Ser Ala Val Arg Pro Val Asp Glu Leu 945 950 955 960 Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu 965 970 975 Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser 980 985 990 Asp Met Ile Leu Ala His Ser His Tyr Thr Gly Gln Leu Asn Val Pro 995 1000 1005 Asp Gln Phe Thr Arg Leu Ile Leu Ser Val Ile Ala Thr Gly Ile 1010 1015 1020 Ala Pro Gly Ser Phe Tyr Gln Ala Gln Ala Thr Ala Glu Arg Pro 1025 1030 1035 Arg Ala His Tyr Asp Gly Leu Pro Gly Asp Phe Thr Ala Glu Ala 1040 1045 1050 Ile Thr Thr Leu Gly Thr Gln Val Pro Glu Gly Pro Asp Ala Thr 1055 1060 1065 Asp Ala Tyr Val Thr Tyr Asp Cys Val Asn Pro His Ser Asp Gly 1070 1075 1080 Val Ser Leu Asp Asn Phe Val Asp Trp Leu Ile Asp Ala Gly Tyr 1085 1090 1095 Pro Ile Gln Arg Ile Asp Asn Tyr Asn Glu Trp Phe Asp Arg Phe 1100 1105 1110 Asp Thr Ala Ile Arg Gly Leu Pro Glu Lys Gln Lys Gln His Ser 1115 1120 1125 Leu Leu Pro Leu Leu His Ala Phe Glu Gln Pro Ser Gly Ala Glu 1130 1135 1140 Asp His Gly Val Val Pro Ala Lys Arg Phe Gln His Ala Val Gln 1145 1150 1155 Ala Ala Gly Ile Gly Pro Val Gly Gln Asp Gly Thr Thr Asp Ile 1160 1165 1170 Pro His Leu Ser Arg Gln Leu Ile Val Lys Tyr Ala Lys Asp Leu 1175 1180 1185 Glu Gln Leu Gly Leu Leu 1190 <210> 197 <211> 1167 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. AT1 <400> 197 Met Ala Thr Asp Ala Val Ser Asp Thr Lys Ser Arg Ile Asp Asp Leu 1 5 10 15 Arg Asn Thr Asp Ala Gln Phe Ala Asp Ala Phe Pro Leu Pro Ala Val 20 25 30 Val Glu Ala Val Ser Lys Pro Gly Leu Pro Val Ser Lys Met Leu Ala 35 40 45 Thr Val Met Glu Gly Tyr Ala Asp Arg Pro Ala Ala Gly Gln Arg Val 50 55 60 Arg Thr Pro Val Thr Asp Asp Ala Thr Gly Arg Thr Thr Phe Glu Leu 65 70 75 80 Arg Ser Glu Phe Glu Thr Val Thr Tyr Gly Gln Leu Trp Ala Arg Ala 85 90 95 Ser Ala Leu Ala Ala Gln Trp His His Asp Ser Thr Asp Pro Leu Val 100 105 110 Ser Gly Asp Val Val Ala Leu Leu Gly Phe Thr Gly Ile Asp Tyr Thr 115 120 125 Thr Ala Glu Leu Ala Cys Ile His Ser Gly Ala Val Ser Val Pro Leu 130 135 140 Gln Thr Ser Ala Ser Val Ser Gln Arg Ala Ala Ile Val Asp Glu Thr 145 150 155 160 Leu Pro Lys Ile Leu Ala Val Gly Ile Asp Tyr Leu Ala Gly Ala Val 165 170 175 Asp Val Val Leu Glu Ala Ala Thr Pro Pro Ala Arg Val Val Val Phe 180 185 190 Asp Tyr Asp Ala Arg Ile Asp Asp Gln Arg Asp Gly Phe Asp Glu Ala 195 200 205 Ala Arg Arg Leu Ala Glu Ala Gln Ser Pro Val Arg Leu Glu Thr Phe 210 215 220 Glu Ser Val Val Arg Gln Gly Val Glu Gln Pro Ala Ala Pro Leu Phe 225 230 235 240 Val Pro Glu Glu Gly Glu Asn Pro Leu Ala Thr Leu Thr Tyr Thr Ser 245 250 255 Gly Ser Thr Gly Thr Pro Lys Gly Val Met Gly Ser Glu Arg Thr Phe 260 265 270 Arg Gly Met Trp Leu Gly Gln Ser Pro Ile Pro Ser Ile Thr Leu Ser 275 280 285 Tyr Leu Pro Met Ser His Ser Tyr Gly Arg Ser Gln Val Phe Ser Ser 290 295 300 Leu Ala Asn Gly Gly Thr Val Tyr Phe Thr Ala Arg Ser Asp Met Ser 305 310 315 320 Thr Leu Leu Ala Asp Phe Thr Leu Val Arg Pro Thr Met Val Ser Leu 325 330 335 Val Pro Arg Ile Cys Glu Ile Val Phe Gln Arg Tyr Leu Ser Asp Val 340 345 350 Asp Arg Tyr Ala Gly Asn Glu Ser Asp Pro Ala Ala Ile Glu Ala Glu 355 360 365 Val Lys Thr Arg Leu Arg Glu Glu Val Leu Gly Gly Arg Val Leu Ser 370 375 380 Ala Phe Cys Gly Ser Ala Pro Leu Pro Lys Glu Thr Glu Ala Phe Met 385 390 395 400 Glu Ser Thr Leu Gly Val His Leu Thr Ile Gly Tyr Gly Ala Ser Glu 405 410 415 Ile Gly Ser Val Leu Ile Asp Ser Gln Val Gln Arg Pro Pro Val Ile 420 425 430 Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Asn Thr Asp 435 440 445 Lys Pro His Pro Arg Gly Glu Leu Leu Val Lys Thr Glu Gln Phe Met 450 455 460 Asp Gly Tyr Tyr Lys Arg Pro Glu Leu Ser Ala Glu Met Leu Asp Glu 465 470 475 480 Asp Gly Tyr Tyr Lys Thr Ser Asp Ile Met Ala Glu Ile Gly Pro Asp 485 490 495 Gln Leu Val Phe Val Asp Arg Arg Asn Asn Val Val Lys Leu Ala Gln 500 505 510 Gly Glu Phe Val Ala Val Ser Arg Leu Glu Ser Leu Tyr Thr Met Ser 515 520 525 Pro Gln Ile Ala Gln Ile Tyr Val Tyr Gly Ser Gly Glu Arg Ser Tyr 530 535 540 Leu Leu Ala Val Val Val Pro Ser Asp Asp Leu Ile Thr Gln Leu Thr 545 550 555 560 Asp Asp Glu Asn Ala Asp Arg Val Gln Ser Val Ile Ser Arg Ala Leu 565 570 575 Gln Arg Ile Ala Ala Asp Asn Gly Leu Asn Gly Tyr Glu Val Pro Arg 580 585 590 Lys Val Ile Ile Glu Thr Glu Pro Phe Ser Gln Glu Asn Gly Leu Leu 595 600 605 Thr Gly Ile Gly Lys Leu Gln Arg Pro Asn Leu Lys Ala Arg Tyr Gly 610 615 620 Asp Arg Leu Glu Ser Val Tyr Ser Glu Leu Ala Asp Asp Gln Val Asn 625 630 635 640 Glu Thr Lys Ala Leu Arg Thr Gly Gly Ala Asp Arg Pro Val Ile Glu 645 650 655 Thr Val Thr Arg Ala Val Gln Ala Leu Leu Gly Leu Ser Ala Ala Asp 660 665 670 Val Asp Ala Asp Ser Arg Phe Gly Asp Leu Gly Gly Asp Ser Leu Ser 675 680 685 Ala Leu Ser Phe Ser Asn Leu Leu Glu Asp Ile Tyr Gly Ile Glu Val 690 695 700 Pro Val Gly Val Ile Ile Asn Pro Ala Ser Asp Leu Thr Arg Leu Ala 705 710 715 720 Glu Tyr Ile Glu Thr Gln Arg Ser Ser Gly Val Thr Gln Thr Thr Phe 725 730 735 Ala Ser Val His Gly Ala Gly Ser Thr Glu Val Tyr Ala Arg Asp Ile 740 745 750 Thr Leu Asp Glu Phe Ile Asp Ala Asp Thr Leu Thr Thr Ala Arg Ser 755 760 765 Leu Pro Ala Pro Asp Gly Thr Thr Asp Thr Val Leu Leu Thr Gly Ser 770 775 780 Thr Gly Phe Leu Gly Ser Arg Leu Thr Leu Glu Trp Leu Gln Arg Gln 785 790 795 800 Ala Asp Cys Gly Gly Thr Leu Ile Cys Ile Ala Arg Gly Ser Asp Ala 805 810 815 Ala Gln Ala Arg Glu Arg Ile Glu Ser Ala Leu Asp Ser Asp Pro Glu 820 825 830 Leu Ile Asp Thr Phe Arg Ala Leu Ala Ser Glu Asn Leu Glu Val Leu 835 840 845 Ala Gly Asp Leu Gly Glu Pro Arg Leu Gly Leu Asp Glu Ala Thr Trp 850 855 860 Asn Arg Leu Ala His Thr Val Asp Leu Ile Val His Pro Ala Ala His 865 870 875 880 Val Asn His Val Leu Pro Tyr Asn Gln Leu Phe Asn Ala Asn Val Val 885 890 895 Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Val Lys Leu Lys Pro 900 905 910 Ile Asn Tyr Val Ser Ser Met Gly Val Thr Thr Leu His Asn Glu Val 915 920 925 Ile Ala Glu Asp Ala Asp Ile Arg Glu Ala Val Ser Val Ala Lys Leu 930 935 940 Asp Asp Gly Tyr Gly Asn Gly Tyr Ala Leu Thr Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Met Arg Glu Val Asn Asp Trp Cys Gly Leu Pro Val Ala Val 965 970 975 Phe Arg Ser Gly Met Ile Leu Ala Asp Arg Lys Tyr Ala Gly Leu Leu 980 985 990 Asn Val Pro Asp Ile Phe Thr Arg Leu Leu Leu Thr Val Val Ser Thr 995 1000 1005 Gly Ile Ala Pro Glu Thr Phe Tyr Ala Ala Asn Gly Ala Asp Gly 1010 1015 1020 Arg Pro Arg Ala Asn Tyr Ser Gly Leu Thr Val Asp Phe Leu Ala 1025 1030 1035 Glu Ser Ile Ala Asp Leu Gly Val Asp Met Thr Glu Gly Thr Phe 1040 1045 1050 Arg Thr Tyr Asn Thr Asp Gly Gly Tyr Asp Asp Gly Ile Ser Leu 1055 1060 1065 Asp Thr Ile Val Asp Trp Val Ile Glu Ala Gly Phe Pro Ile Gln 1070 1075 1080 Arg Val Asp Glu Tyr Asp Glu Trp Val Thr Arg Cys Glu Thr Ala 1085 1090 1095 Met Arg Gly Leu Ser Glu Gln Gln Arg Gln His Ser Leu Ile Asn 1100 1105 1110 Val Met Asp Ala Tyr Arg His Pro Gln Gln Val Ala Ala Gly Ser 1115 1120 1125 Ala Val Pro Ser Gly Arg Phe Gln Ala Ala Leu His Ala Val Gly 1130 1135 1140 Leu Glu Pro Pro His Met Ser Lys Thr Leu Ile Asp Lys Tyr Ile 1145 1150 1155 Asn Asp Leu Lys Leu Leu His Leu Val 1160 1165 <210> 198 <211> 1159 <212> PRT <213> Artificial Sequence <220> <223> Brevibacterium casei <400> 198 Met Asn Leu Lys Gly Lys Thr Pro Met Leu Leu Asn Thr Gln Met Thr 1 5 10 15 Ser Ile Phe Glu Arg Phe Ser Gly Arg Pro Ala Leu Ala Asp Arg Arg 20 25 30 Pro Ile Pro Arg Ser Asn Gly Asp Arg Asp Leu Phe Asp Ser Glu Val 35 40 45 Leu Asp Trp Tyr Glu Thr Leu Ser Tyr Glu Glu Leu Arg Arg Arg Val 50 55 60 Leu Ala Ala Ala Ala Gln Leu His Gly Arg Arg Met Val Lys Gly Pro 65 70 75 80 Leu Ala Ser Gly Asp Arg Leu Ala Leu Leu Gly Phe Pro Gly Ile Asp 85 90 95 Phe Thr Thr Ile Asp Phe Ala Cys Asn Leu Ala Gly Val Thr Thr Val 100 105 110 Pro Leu Gln Thr Ser Gly Ser Leu Glu Gln His Arg Ser Ile Ile Gly 115 120 125 Glu Thr Ser Pro Arg Ala Leu Val Ile Ser Ile Ser Leu Leu Asn Lys 130 135 140 Ala Glu Ser Ile Leu Ser His Ala Asp Ser Ile Asp Arg Leu Ile Val 145 150 155 160 Leu Asp Tyr Arg Gly Gly Asp Leu Ser His Arg Arg Ile Leu Glu Ser 165 170 175 Ala Ala Asn Ser Leu Pro Ile Ala Pro Glu Leu Leu Glu Leu Asp Pro 180 185 190 Asp Pro Gly Asp Ala Phe Gly Asp Ile Cys Asp Asp His Leu Ser Met 195 200 205 Leu Leu Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr 210 215 220 Ser Ala Arg Leu Val Arg Glu Met Trp Gly Gly Glu Gly Trp Ser Glu 225 230 235 240 Phe Phe Ala Glu Gln Asp Glu Ile Ala Ser Phe His Tyr Met Pro Met 245 250 255 Ser His Val Ala Gly His Ser Ser Val Arg Ser Thr Leu Ser Arg Gly 260 265 270 Gly Val Thr Tyr Phe Ser Ser Thr Pro Asn Leu Ala Asn Phe Phe Asp 275 280 285 Asp Leu Ala Leu Ala Arg Pro Thr Glu Leu Ser Leu Val Pro Arg Val 290 295 300 Cys Glu Leu Leu His Gln Glu Tyr Gln Arg Arg Ala Glu Ser Arg Arg 305 310 315 320 Asp Asp Thr Asp Gly Tyr Ala Ser Gln Ala Val Leu Glu Asp Met Arg 325 330 335 Thr Ser Val Leu Gly Gly Arg Val Glu Trp Ala Ser Cys Thr Ser Ala 340 345 350 Pro Val Ser Ala Glu Leu Lys Ala Phe Met Glu Arg Leu Leu Gly Ile 355 360 365 Glu Leu His Glu Leu Tyr Gly Thr Thr Glu Ile Gly Gly Val Leu Ala 370 375 380 Asp Gly Arg Phe Leu Thr Pro Pro Val Ile Asp Tyr Arg Leu Asp Asp 385 390 395 400 Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Arg Pro Ser Ala Arg Gly 405 410 415 Glu Leu Leu Val Lys Ser Thr Ser Thr Val Pro Gly Tyr Phe Asn Arg 420 425 430 Pro Asp Leu Asn Ala Glu Ile Phe Thr Glu Asp Gly Tyr Tyr Arg Thr 435 440 445 Gly Asp Ile Ala Ala Val Asp Ser Asn Gly Thr Val Arg Ile Ile Asp 450 455 460 Arg Lys Asn Ser Ile Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Leu 465 470 475 480 Pro Ser Leu Glu Ala Thr Phe Val Ala Gly Ser Thr Leu Ile Arg Gln 485 490 495 Val Phe Leu Tyr Gly Arg Ser Asp Trp Ser Ala Leu Val Ala Val Val 500 505 510 Val Pro Thr Asp Leu Ala Gln Ser Ala Ala Ala Asp Asp Glu Arg Asn 515 520 525 Gln Thr Met Ala Lys Leu Met Leu Asp Glu Leu Arg His Val Ala Glu 530 535 540 Arg Glu His Leu Asn Ser Tyr Glu Val Pro Ala Ala Val Ile Val Glu 545 550 555 560 Ser Glu Pro Phe Ser Glu Glu Asn Gly Leu Leu Ser Asp His Arg Lys 565 570 575 Pro Val Arg Pro Arg Leu His Asp Lys Tyr Gln Ser Gln Leu Glu Ala 580 585 590 Ile Tyr Glu Gln Ile Val Ala Ala Arg Asp Asp Ala Leu Thr Asp Leu 595 600 605 Ile Ala His Gly Ala Glu Asn Asp Thr Ala Ser Thr Ile Arg Asp Ala 610 615 620 Ala Ala Leu Thr Leu Gln Ile Glu Pro Ala Thr Val Ser Ile Asp Ala 625 630 635 640 Lys Phe Arg Asn Leu Gly Gly Asp Ser Leu Thr Ala Val His Leu Ser 645 650 655 Arg Leu Leu Asn Gln Ile Tyr Gly Leu His Ile Pro Val Asp Val Leu 660 665 670 Val Ser Glu Ala Arg Thr Phe Ala Asp Leu Gly Glu Tyr Met Asp Gly 675 680 685 Lys Arg Gly Gln Arg Glu Trp Leu Ala Thr Phe Glu Glu Ile His Thr 690 695 700 Ser Asp Met Arg Pro Leu Tyr Ala Glu Glu Leu Thr Val Glu Arg Phe 705 710 715 720 Leu Ser Ser Arg Ala Thr Ile Asn Pro Ser Ser Thr Arg Tyr Gly Ala 725 730 735 Pro Gln Gly Val Leu Ile Thr Gly Ala Ser Gly Phe Leu Gly Arg Phe 740 745 750 Leu Cys Leu Glu Trp Leu Arg Arg Phe Ala Gly Thr Thr Arg Arg Val 755 760 765 Thr Cys Leu Val Arg Ala Asn Ser His Ala Ala Ala Arg Ala Arg Leu 770 775 780 Arg Ala Thr Tyr Ser Ser Ser Pro Glu Leu Leu Ala Glu Phe Asp Arg 785 790 795 800 Leu Ala Gly Asn Leu Asp Val Val Ala Gly Asp Leu Ala Glu Pro Arg 805 810 815 Leu Gly Leu Asp Glu Gln Ile Trp Lys Ser Leu Ser Gln Asp Ile Thr 820 825 830 His Ile Ile His Ala Gly Ala Met Val Asn His Ala Leu Gly Tyr Arg 835 840 845 Glu Leu Phe Ala Ser Asn Val Ala Gly Thr Ala Glu Val Leu His Leu 850 855 860 Ala Leu Thr Gly Pro Leu Lys Arg Ile Thr Phe Met Ser Ser Ile Ala 865 870 875 880 Thr Ala Leu Leu Gln Gln Ala Gly Gly Pro Met Thr Glu Arg Val Asp 885 890 895 Ile Arg Glu Ala Leu Ser Gln Ile Glu Asp Ala Gly Gly Ile Val Asp 900 905 910 Gly Tyr Ala Ala Thr Lys Trp Ala Ser Glu Val Leu Leu Arg Asn Ala 915 920 925 Asn Glu Gln Phe Gly Val Pro Val Thr Val Phe Arg Ser Ser Met Ile 930 935 940 Leu Ala His Ser Arg Tyr Arg Gly Gln Ile Asn Val Pro Asp Thr Tyr 945 950 955 960 Thr Arg Leu Leu Phe Ser Val Leu Gln Ser Gly Ile Thr Pro Ser Ser 965 970 975 Phe Tyr Ala Ala Asn Gly Glu His Ala His Tyr Asp Gly Leu Pro Val 980 985 990 Asp Val Val Ser Glu Ala Ile Ala Ser Leu Ala Gln Asp Glu Thr Arg 995 1000 1005 Glu Tyr Arg Thr Tyr His Leu Val Asn Pro Phe Asp Asp Gly Ile 1010 1015 1020 Ser Leu Asp Arg Phe Val Glu Trp Leu Ile Glu Ala Gly Val Ser 1025 1030 1035 Leu Val Arg Val Gly Glu Tyr Gly Leu Trp Met Glu Arg Phe Lys 1040 1045 1050 Met Ala Leu Ser Val Leu Asp Asp Asp Asp Lys Arg Ala Ser Leu 1055 1060 1065 Leu Pro Leu Ile Asp Gly Phe Arg Ala Pro Glu Asp Pro Val Arg 1070 1075 1080 Gly Ser Arg Ile Asp Ser Thr Asp Leu His Gly Ala Leu Ala Gln 1085 1090 1095 Ala Gly Leu Ala Asp Arg Leu Gln Pro Leu Ser Gly Ser Ser Asp 1100 1105 1110 Ile Arg Trp Gly Ser Trp Gly Glu Ser Ala Gly Gly Glu Glu His 1115 1120 1125 Ala Glu Pro Val Val Val Pro Val Ala Val Ala Ala Gly Glu Ala 1130 1135 1140 Ala Val Glu Leu Asp Asp Pro Val His Gly Leu Gly Ala Thr Val 1145 1150 1155 Arg <210> 199 <211> 1174 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium noviomagense <400> 199 Met Ser Thr Asp Gly Arg Ala Glu Trp Leu Ala Arg Arg Val Glu Glu 1 5 10 15 Leu Ser Ala Thr Asp Pro Gln Phe Ala Ala Ala Gln Pro Ser Ser Ser 20 25 30 Val Ala Thr Ala Leu Glu Gln Ala Gly Leu Arg Leu Pro Gln Val Ile 35 40 45 Arg Thr Val Leu Gln Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 50 55 60 Val Val Gln Phe Val Glu Asp Ser Lys Thr Gly Arg Thr Val Leu Glu 65 70 75 80 Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Arg Val Leu Gly Glu Arg 85 90 95 Val Asp Ala Leu Ala Arg Ala Leu Thr Glu Asp Leu Val Gln Val Gly 100 105 110 Asp Arg Val Cys Val Leu Gly Phe Thr Ser Val Asp Tyr Thr Thr Ile 115 120 125 Asp Val Ala Leu Gly Leu Ile Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Pro Ile Thr Gln Leu Gln Ser Ile Val Ala Glu Thr Glu Pro 145 150 155 160 Ser Val Ile Ala Ala Ser Val Glu Tyr Leu Pro Asp Ala Ala Glu Leu 165 170 175 Ala Cys Ser Gly Pro Ala Pro Ala Lys Leu Val Val Phe Asp Tyr Arg 180 185 190 Pro Glu Val Asp Asp Gln Cys Glu Thr Val Glu Ala Val Arg Glu Arg 195 200 205 Leu Ala Asn Thr Ala Val Leu Val Glu Thr Leu Ala Asp Val Leu Lys 210 215 220 Arg Gly Lys Ala Leu Pro Ala Lys Pro Gly Gly Ala Pro Asn Ser Ser 225 230 235 240 Asp Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly 245 250 255 Glu Pro Lys Gly Ala Met Tyr Pro Gln Ser His Val Ala Lys Met Trp 260 265 270 Arg Arg Arg Thr Ser Ser Thr Asn Trp Phe Gly Phe Arg Ala Gly Ala 275 280 285 Ala Ser Ile Thr Leu Asn Phe Leu Pro Met Ser His Ala Leu Gly Arg 290 295 300 Gly Thr Leu Tyr Gly Thr Leu Gly Asn Gly Gly Thr Ala Tyr Phe Ala 305 310 315 320 Ala Arg Ser Asp Leu Ser Thr Leu Leu Glu Asp Leu Arg Leu Val Arg 325 330 335 Pro Thr Glu Leu Thr Phe Val Pro Arg Ile Trp Glu Met Leu Tyr Gly 340 345 350 Glu Tyr Val Ser Glu Val Asp Arg Arg Val Ala Glu Gly Ala Asp Arg 355 360 365 Glu Thr Val Glu Ala Gln Val Leu Arg Glu Val Arg Gln Glu Val Leu 370 375 380 Gly Gly Arg Tyr Val Phe Ala Met Thr Gly Ser Ala Pro Ile Ser Lys 385 390 395 400 Glu Leu Lys Ala Trp Val Glu Ser Leu Leu Glu Thr Pro Leu Thr Asp 405 410 415 Gly Tyr Ala Ser Thr Glu Ser Gly Met Ile Leu Arg Asp Gly Gln Val 420 425 430 Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu Leu 435 440 445 Gly Tyr Phe Ser Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val 450 455 460 Lys Thr Glu Asn Met Phe Pro Gly Tyr Tyr Lys Arg Pro Asp Ile Thr 465 470 475 480 Ala Ser Val Phe Asp Ala Asp Gly Tyr Tyr Arg Thr Gly Asp Val Phe 485 490 495 Ala Gln Val Gly Arg Asp Arg Leu Val Tyr Val Asp Arg Arg Asn Asn 500 505 510 Val Ile Lys Leu Ala Gln Gly Glu Phe Val Thr Leu Ala Lys Leu Glu 515 520 525 Ala Val Phe Asp Thr Ser Pro Leu Val His Gln Ile Tyr Val Tyr Gly 530 535 540 Asn Ser Ala His Arg Tyr Leu Leu Ala Val Val Val Pro Thr Arg Asp 545 550 555 560 Ala Leu Ala Arg Phe Asp Asp Pro Ser Thr Leu Arg Ala Arg Ile Ala 565 570 575 Asp Ser Leu Gln Glu Val Ala Lys Thr Ala Gly Leu Gln Ser Tyr Glu 580 585 590 Val Pro Arg Asp Phe Leu Ile Glu Thr Thr Pro Phe Ser Val Glu Asn 595 600 605 Gly Leu Leu Thr Gly Ile Gly Lys Leu Ala Trp Pro Lys Leu Lys Glu 610 615 620 Arg Tyr Gly Glu Arg Leu Glu Gln Leu Tyr Ala Glu Leu Asp Gln Gly 625 630 635 640 Gln Ala Asn Glu Leu Ala Glu Leu Arg Arg Ser Gly Ala Asp Arg Pro 645 650 655 Val Leu Gln Thr Ile Ser Arg Ala Ala Ala Ala Leu Leu Gly Thr Ala 660 665 670 Arg Val Glu Val Ser Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp 675 680 685 Ser Leu Ala Ala Leu Thr Phe Ala Asn Leu Leu Arg Glu Ile Phe Gly 690 695 700 Val Asp Val Pro Val Gly Val Ile Val Ser Pro Ala Thr Asp Leu Gln 705 710 715 720 Ala Ile Ala Asp Tyr Ile Gln Ala Glu Arg Gln Gly Val Lys Arg Pro 725 730 735 Thr Phe Val Ala Val His Gly Arg Ser Ala Thr Lys Val His Ala Gly 740 745 750 Asp Leu Thr Leu Asp Thr Phe Leu Asp Gly Ala Thr Leu Ser Ala Ala 755 760 765 Thr Asn Leu Pro Lys Pro Thr Thr Glu Val Arg Thr Val Leu Leu Thr 770 775 780 Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu 785 790 795 800 Arg Met Asp Leu Val Asp Gly Thr Val Thr Ala Leu Val Arg Ala Lys 805 810 815 Ser Asp Glu Glu Ala Arg Ala Arg Leu Asp Lys Thr Phe Asp Ser Gly 820 825 830 Asp Pro Arg Leu Leu Ala Arg Tyr Gln Glu Leu Ala Ala Glu His Leu 835 840 845 Glu Val Ile Ala Gly Asp Lys Gly Glu Pro Asn Val Gly Leu Asp Arg 850 855 860 Gln Thr Trp Gln Arg Leu Ala Asp Thr Val Asp Val Ile Ala Asp Pro 865 870 875 880 Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro 885 890 895 Asn Thr Leu Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Thr Lys 900 905 910 Leu Lys Pro Tyr Thr Tyr Val Ser Thr Ile Gly Val Gly Asp Gln Val 915 920 925 Glu Pro Ala Lys Phe Thr Glu Asp Ala Asp Ile Arg Lys Ile Ser Pro 930 935 940 Thr Arg Glu Ile Asn Asp Ser Tyr Ala Asn Gly Tyr Gly Ile Ser Lys 945 950 955 960 Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu 965 970 975 Pro Val Thr Val Phe Arg Cys Ser Met Ile Met Ala Asp Thr Thr Tyr 980 985 990 Lys Gly Gln Leu Asn Leu Pro Asp Met Phe Thr Arg Leu Met Leu Ser 995 1000 1005 Leu Ala Ala Thr Gly Ile Ala Pro Phe Ser Phe Tyr Glu Leu Asp 1010 1015 1020 Ala Asp Gly Asn Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val 1025 1030 1035 Glu Phe Ile Ala Glu Ala Ile Ala Thr Leu Gly Ala Gln Asn Val 1040 1045 1050 Glu Thr Phe Gln Thr Tyr His Val Met Asn Pro His Asp Asp Gly 1055 1060 1065 Ile Gly Leu Asp Glu Phe Val Asp Trp Leu Ile Asp Ala Gly Tyr 1070 1075 1080 Pro Leu Gln Arg Ile Gly Asp Tyr Ala Glu Trp Leu His Arg Phe 1085 1090 1095 Glu Thr Val Leu Arg Gly Leu Pro Asp Arg Gln Arg Gln Tyr Ser 1100 1105 1110 Leu Leu Pro Leu Leu His Asn Tyr Gln Lys Pro Gln Thr Pro Leu 1115 1120 1125 Arg Gly Ser Met Ala Pro Thr Asp Arg Phe Arg Ala Ala Val Gln 1130 1135 1140 Glu Ala Lys Ile Gly Pro Ala Lys Asp Ile Pro His Ile Ser Pro 1145 1150 1155 Ala Ile Ile Val Lys Tyr Val Thr Asp Leu Gln Leu Leu Gly Leu 1160 1165 1170 Leu <210> 200 <211> 1118 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium peregrinum <400> 200 Met Tyr Ala Ala Asp Arg Gln Phe Arg Ser Cys Val Pro Leu Pro Glu 1 5 10 15 Val Ser Ala Ala Val Arg Glu Asp Gly Leu Gly Leu Ala Gly Ile Ile 20 25 30 Ala Ala Val Met Thr Gly Tyr Ala Asp Arg Pro Ala Leu Gly Arg Cys 35 40 45 Ala Gly Ser Ala Pro His Thr Ile Ser Tyr Arg Asp Leu Trp Gln Arg 50 55 60 Ile Asn Ala Ile Ala Thr Asp Trp Leu Ala His Gln Thr Phe Pro Ile 65 70 75 80 Ser Ser Gly Glu Phe Val Cys Thr Leu Gly Phe Ala Ser Ala Asp Tyr 85 90 95 Ile Thr Val Asp Leu Ala Cys Ala Leu Thr Gly Ala Val Thr Val Pro 100 105 110 Val Gln Tyr Gly Ala Gln Thr Gly Gln Leu Thr Arg Val Leu Ala Glu 115 120 125 Thr Arg Ala Ser Ala Leu Ala Val Ser Ser Asp Gln Leu Pro Thr Ala 130 135 140 Val Glu Ala Ala Leu Ser Ala Pro Arg Leu Arg Arg Leu Ile Val Phe 145 150 155 160 Asp His Arg Ala Asp Ile Asp Asp Phe Gly Asp Thr Phe Glu Gln Ala 165 170 175 Gln Leu Arg Leu Thr Lys Ser Arg His Pro Ile Leu Phe Glu Thr Leu 180 185 190 Asp Glu Val Ile Arg Arg Gly Leu Arg Arg Pro Pro Ala Ala Ser Pro 195 200 205 Arg Pro Pro Leu Pro Pro Ala Asp Pro Asp Arg Leu Val Gly Leu Ser 210 215 220 Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Ala Ala Met Tyr Thr Glu 225 230 235 240 Arg Met Val Ala Gly Thr Trp Arg Asn Ser Val Ala Ile Pro Val Ile 245 250 255 Ser Tyr Asn Tyr Met Pro Met Ser His Tyr Gly Gly Lys Ala Leu Val 260 265 270 Leu Thr Thr Leu Ala Ser Gly Gly Thr Ala Tyr Phe Ala Ala Ala Pro 275 280 285 Asp Met Ser Ser Leu Phe Asp Asp Ile Ala Ala Val Arg Pro Thr Val 290 295 300 Leu Pro Leu Ile Pro Arg Val Cys Glu Met Ile Tyr Ser Arg Tyr Gln 305 310 315 320 Ser Glu Cys Ser Gln Arg Ser Ala Pro Thr Ser Asp Pro Ala Thr Val 325 330 335 Arg Ala Gln Val Met Thr His Leu Arg Glu Asn Val Leu Gly Gly Arg 340 345 350 Met Leu Leu Ala Ala Ser Gly Ser Ala Pro Leu Ser Ala Glu Leu Thr 355 360 365 Thr Phe Ile Glu Thr Cys Leu Arg Ile His Leu Ala Ile Gly Tyr Gly 370 375 380 Thr Thr Glu Thr Gly Asn Val Leu Asn Asp Gly Arg Val Val Arg Pro 385 390 395 400 Pro Val Ile Asp Tyr Lys Leu Val Asp Ile Pro Glu Leu Gly Tyr Phe 405 410 415 Gly Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Glu 420 425 430 Val Leu Thr Pro Gly Tyr Tyr His Arg Pro Asp Ala Thr Asp Thr Ala 435 440 445 Phe Asp Asp Glu Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu Ile 450 455 460 Gly Pro Asp His Leu Ala Phe Val Asp Arg Arg Ser Asn Val Val Lys 465 470 475 480 Leu Ser Gln Gly Glu Phe Val Ala Leu Ser His Leu Glu Ser Val Phe 485 490 495 Val Thr Ser Pro Tyr Ile Arg Gln Ile Phe Val Tyr Gly Ser Ser Arg 500 505 510 Arg Ala Phe Val Leu Ala Val Val Val Pro Glu Thr Pro Pro Gly Leu 515 520 525 Pro Ala Ala Thr Lys Ala Thr Ile Leu Ala Ser Leu Arg Thr Ile Ala 530 535 540 Arg Asp Asn Ala Leu Arg Pro Tyr Glu Val Pro Arg Asp Ile Leu Ile 545 550 555 560 Asp Pro Arg Pro Phe Ser Val Asp Asn Gly Leu Leu Thr Ala Thr Ala 565 570 575 Lys Pro Ala Arg Pro Ala Leu Thr Ile His Tyr Arg Glu Gln Leu Glu 580 585 590 Gln Thr Tyr Ala Asp Ile Ala Asp Arg Gln Ala Val Glu Leu Ala Thr 595 600 605 Leu Arg Gln Gly Ala Ala Asp Arg Pro Val Leu Glu Thr Val Arg Leu 610 615 620 Ala Ala Ala Ala Thr Leu Gly Ile Thr Thr Val Asp Val Asp Thr Val 625 630 635 640 Leu Ser Asp Ile Gly Ile Asp Ser Leu Thr Ala Leu Thr Leu Ala Thr 645 650 655 Leu Leu Thr Glu Ile Phe Gly Ala Arg Val Pro Ala Thr Ala Val Ile 660 665 670 Asp Pro Thr Arg Asn Leu Ser Gly Ile Ala Ser Leu Ile Glu Ala Gln 675 680 685 Arg Arg Ala Ile Pro Arg Arg Ala Cys Pro Gly Val His Gly Gln Cys 690 695 700 Thr Asp Arg Val Tyr Ala Arg Asp Leu Thr Leu Asp Arg Phe Ile Glu 705 710 715 720 Ala Arg Thr Ile Asp Arg Asp Arg Pro Val Ala Pro Asn Pro Gly Pro 725 730 735 Pro Arg Thr Val Leu Leu Thr Gly Ala Asn Gly Phe Leu Gly Gln Leu 740 745 750 Leu Cys Ala Glu Trp Leu Arg Arg Leu Ala Pro Ile Gly Gly Thr Val 755 760 765 Ile Cys Leu Val Arg Gly Ala Asp Asn Ala Asp Ala His Arg Arg Leu 770 775 780 Lys Ala Glu Phe Gly Pro Pro Ala Glu Ser Arg Leu Glu Val Leu Ala 785 790 795 800 Gly Asp Leu Thr Asp Glu His Leu Gly Leu Asp Gly Ala Thr Trp Ser 805 810 815 Arg Leu Ala Ala Thr Val Asp Leu Ile Gly His Ser Gly Ala Leu Val 820 825 830 Asn His Leu Leu Pro Tyr Pro Glu Leu Phe Gly Pro Asn Val Val Gly 835 840 845 Thr Ala Gly Leu Ile Arg Leu Ala Ile Thr Gly Lys Ser Lys Arg Phe 850 855 860 Ala Phe Val Ser Thr Ala Ala Ala Gly Thr Thr Asp Asp Gly Arg Pro 865 870 875 880 Leu Pro Glu Asp Ala Asp Val Arg Val Gly Cys Pro Ala Arg Thr Arg 885 890 895 Asn Thr Ala Pro Ala Asn Gly Tyr Val Ile Ser Lys Trp Ala Ala Glu 900 905 910 Val Leu Leu Arg Arg Ala His Asp Ala His Gly Leu Ser Val Thr Val 915 920 925 Phe Arg Pro Gly Met Ile Leu Ala His Ser Arg Phe Ser Asp His Leu 930 935 940 Asn Val Gly Asp Val Phe Thr Arg Leu Val Leu Ser Leu Ala Ala Thr 945 950 955 960 Gly Ile Ala Pro Pro Ser Phe Tyr Arg Gln Pro Ala Asn Arg Pro His 965 970 975 Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Ala Ala Ile Val Glu Leu 980 985 990 Ala Ala Gly Pro Gly Pro Phe Gly Gly Phe Ala Thr Tyr Asn Val Val 995 1000 1005 Asn Asp His Asp Asp Ala Ile Ser Leu Asp Glu Ile Val Asp Trp 1010 1015 1020 Leu Val Glu Ala Gly His Pro Ile Thr Arg Leu Gln Ser His Arg 1025 1030 1035 Glu Trp Ala Ala Arg Phe Glu Thr Ala Met Arg Ala Leu Pro Val 1040 1045 1050 Arg Gln Arg Arg His Cys Leu Leu Pro Leu Met Ala Ala Phe Ala 1055 1060 1065 Glu Pro Ala Glu Ala Val Ala Gly Ser Ala Phe Pro Thr Gln Arg 1070 1075 1080 Phe Arg Glu Cys Leu Arg Ser Ser Gly Ala Pro Arg Pro Val Pro 1085 1090 1095 His Leu Thr Pro Asp Leu Ile His Gly Tyr Leu Thr Ala Leu Arg 1100 1105 1110 His Arg Gly Leu Leu 1115 <210> 201 <211> 1174 <212> PRT <213> Artificial Sequence <220> <223> Pseudonocardia sp. SCN 73-27 <400> 201 Met Thr Leu Asp Pro Arg Ala Leu Pro Ala Tyr Ala Arg Arg Val Leu 1 5 10 15 Asp Leu Ala Glu Thr Asp Pro Gln Leu Arg Glu Leu Met Pro Asp Gly 20 25 30 Ala Val Glu Glu Ala Leu Gly Arg Pro Asp Leu Ser Phe Glu Gln Ala 35 40 45 Leu Ala Thr Val Leu Asp Thr Tyr Ala Glu Arg Pro Ala Leu Gly Glu 50 55 60 Arg Gly Tyr Asp Ile Ala Leu Gly Asp Ser Gly Arg His Val Arg Ala 65 70 75 80 Trp Asn Pro Trp Phe Arg Thr Ile Thr Tyr Gly Glu Leu His Gly Gln 85 90 95 Ile Thr Gly Leu Ala Ser Ser Trp Arg His Gln Pro Arg His Arg Val 100 105 110 Asp Pro Gly Asp Phe Val Cys Val Leu Gly Thr Thr Ser Ile Asp Phe 115 120 125 Val Thr Ile Asp Leu Ala Cys Ala Phe Ala His Ala Val Ser Val Pro 130 135 140 Leu Gln Gly Thr Met Gly Ala Ala Asn Leu Asp Arg Ile Leu His Asp 145 150 155 160 Thr Thr Pro Thr Thr Val Ala Ala Thr Val Ala Glu Leu Ser Leu Ala 165 170 175 Ala Glu Leu Val Ala Ala His Pro Ser Val Arg Ser Leu Val Val Ile 180 185 190 Asp Ser Asp Glu Arg Val Asp Asp Glu Arg Glu Ala Ile Glu Ala Ala 195 200 205 Ala Glu Thr Leu Gly Arg Ser Arg Ser Ser Ala Ala Leu Val Met Leu 210 215 220 Ala Glu Leu Val Ala Arg Gly Ala Ala Glu Pro Trp Thr Pro Leu Pro 225 230 235 240 Pro Ala Pro Glu Gly Asn Asp Arg Leu Ala Leu Leu Val His Ser Ser 245 250 255 Gly Ser Thr Gly Thr Pro Lys Gly Ala Val Leu Thr Glu Arg Leu Ala 260 265 270 Arg Ala Pro Phe Ser Arg Ala Pro Val Pro Val Pro Val Val Arg Leu 275 280 285 Cys Phe Ala Pro Met Ala His Thr Ala Gly Arg Gly Ser Pro Tyr Gly 290 295 300 Ala Leu Ala His Gly Gly Thr Ala Phe Phe Thr Ala Arg Pro Asp Leu 305 310 315 320 Ser Met Leu Phe Glu Asp Met Arg Leu Val Arg Pro Thr Glu Ser Phe 325 330 335 Ala Phe Pro Arg Ile Leu Glu Met Val His Arg Ala Phe Gln Gly Asp 340 345 350 Val Thr Arg Arg Val Asn Ser Gly Ile Asp Pro Ala Lys Ala Ser Ala 355 360 365 Asp Val Met Ala Glu Met Arg Asp Thr Phe Leu Gly Asp Arg Ile Ser 370 375 380 Leu Leu Thr Val Gly Gly Ala Pro Thr Pro Pro Ala Leu Ala Arg Phe 385 390 395 400 Thr Ala Glu Cys Leu Pro Val Glu Ile Ser Asp Arg Tyr Gly Ser Thr 405 410 415 Glu Val Gly Gln Val Thr Glu Asn Gly Arg Ile Met Arg Pro Pro Ile 420 425 430 Ile Asp Tyr Arg Leu Arg Asp Val Pro Glu Leu Gly Tyr His Thr Thr 435 440 445 Asp Glu Pro Tyr Pro Arg Gly Glu Leu Cys Leu Arg Thr Ala Thr Ala 450 455 460 Ile Ser Gly Tyr Phe Asn Arg Pro Asp Ala Thr Ala Ala Leu Phe Asp 465 470 475 480 Glu Asp Gly Tyr Leu Leu Thr Gly Asp Ile Met Glu Glu Arg Gly Pro 485 490 495 Asp His Leu Val Tyr Val Asp Arg Arg His Asp Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Ala Ala Gly Ala Leu Arg Thr Ala Phe Glu Asp 515 520 525 Gly Ser Asp Val Ile His Gln Ile Tyr Leu Tyr Gly Thr Ser Val Arg 530 535 540 Ser Tyr Leu Val Ala Val Val Val Pro Asp Ala Glu Ala Val Arg Arg 545 550 555 560 Val Leu Gly Glu Arg Pro Arg Asp Gly Ala Leu Lys Glu Leu Ile Arg 565 570 575 Ala Glu Leu Asn Glu Val Gly Ala Thr Ala Gly Leu Lys Ala Phe Glu 580 585 590 Ile Pro Arg Asp Phe Leu Val Glu Pro Glu Pro Phe Thr His Glu Asn 595 600 605 Asp Leu Leu Thr Ser Leu His Lys Pro Arg Arg Pro Asn Leu Glu Arg 610 615 620 Lys Tyr Gly Gly Arg Leu Glu Ala Leu Tyr Asp Glu Leu Glu Arg Arg 625 630 635 640 Gln Arg Asp Glu Leu Asp Ala Leu Arg Gly Gly Gly Asp Ser Leu Asp 645 650 655 Val Leu Glu Lys Ile Gly Arg Ala Leu Glu Ala Ser Leu Gly Leu Glu 660 665 670 His Val Asp Val His Arg Pro Tyr Gly Phe Thr Glu Leu Gly Gly Asp 675 680 685 Ser Leu Gly Ala Val Ala Phe Ser Glu Leu Leu Glu Asp Leu Phe Gly 690 695 700 Val Glu Val Pro Val Thr Thr Ile Leu Ser Pro Ala Gly Asn Pro Val 705 710 715 720 Arg Trp Ala Arg Ala Val Glu Ala Ala Leu Arg His Glu Gly Ser Pro 725 730 735 Ala Thr Phe Ser Ala Val His Gly Arg Gly Thr Arg Glu Leu Arg Ala 740 745 750 Ala Asp Leu Gly Leu Asp Ala Phe Leu Asp Ala Asp Ala Leu Arg Asp 755 760 765 Thr Pro Gly Ser Glu Pro Pro Thr Ala Pro Arg Thr Val Leu Leu Thr 770 775 780 Gly Ala Thr Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Glu 785 790 795 800 Glu Leu Ala Ala Thr Gly Gly Thr Leu Val Ala Leu Val Arg Ala Ala 805 810 815 Asp Glu Pro Ala Ala Arg Ser Arg Leu Asp Ala Ala Phe Ala Ser Asp 820 825 830 Pro Ala Leu Leu Glu Arg Phe Arg Ala Leu Ala Arg Asp Arg Leu Arg 835 840 845 Ile Leu Pro Gly Asp Val Ala Glu Pro Arg Leu Gly Leu Thr Ala Arg 850 855 860 Asp His Asp Arg Leu Ala Asp Glu Val Asp Arg Ile Val His Pro Ala 865 870 875 880 Ala Leu Val Asn His Val Leu Gly Tyr Glu Ser Leu Phe Gly Pro Asn 885 890 895 Val Ala Gly Thr Ala Gln Leu Ile Gly Leu Ala Leu His Arg Arg Gln 900 905 910 Lys Arg Ile Asp Phe Val Ser Ser Ala Ala Val Arg Pro Phe Leu Asp 915 920 925 Arg Ser Ala Gly Pro Gln Asp Glu Trp Pro Leu Ser Pro Gln Ile Val 930 935 940 Leu Thr Gly Arg Tyr Gly Ser Gly Tyr Gly Ala Ser Lys Trp Ala Ala 945 950 955 960 Glu Leu Leu Leu His Asp Ala His Arg Arg Phe Gly Leu Pro Val Asp 965 970 975 Ile His Arg Gly Ser Met Met Leu Pro His Arg His Tyr Arg Gly Gln 980 985 990 Ile Asn Pro Asp Asp Val Phe Thr Arg Leu Leu His Ser Val Ile Thr 995 1000 1005 Thr Gly Leu Ala Pro Arg Ser Phe Tyr Phe Pro Gly Pro Asp Gly 1010 1015 1020 Ser Arg Ala Arg Ala His Tyr Asp Gly Leu Pro Val Asp Phe Val 1025 1030 1035 Ala Ala Ala Ile Val Arg Leu Gly Ala Gln Ala His Arg Asp Val 1040 1045 1050 Arg Thr Leu His Val Ser Asn Phe His Val Asp Asp Gly Tyr Ser 1055 1060 1065 Leu Asp Met Phe Val Asp Trp Ile Glu Gln Ala Gly Tyr Pro Ile 1070 1075 1080 Arg Arg Ile Asp Asp His Gly Glu Trp Leu Arg Leu Phe Glu Glu 1085 1090 1095 Arg Leu Arg Ala Leu Pro Glu Asp Glu Arg Asn Arg Ser Ser Leu 1100 1105 1110 Ala Val Leu Asp Ser Leu Arg Arg Pro Asp Asp Pro Ser Gly Arg 1115 1120 1125 Ala Ala Arg Gly Thr Arg Phe Arg Glu Ala Leu Asp Ala Val Pro 1130 1135 1140 Gly Gly Gly Leu Ala Pro Pro His Leu Thr Arg Glu Phe Leu Gly 1145 1150 1155 Lys Cys Leu Asp Asp Met Arg Arg Leu Gly Leu Leu Pro Ala Pro 1160 1165 1170 Ala <210> 202 <211> 1186 <212> PRT <213> Artificial Sequence <220> <223> Chloroflexi bacterium HGW-Chloroflexi-5 <400> 202 Met Thr Asp Ser Asn Thr Asn Pro Ser Pro Lys Lys Arg Tyr Phe Leu 1 5 10 15 Arg Met Gln Glu Leu Ala Gln Arg Asp Pro Gln Ile Lys Gln Leu Met 20 25 30 Pro Ser Glu Ser Val Arg Asp Ala Ile Phe Gln Pro Gly Leu Ser Tyr 35 40 45 Asp Arg Leu Ile Gln Thr Val Leu Glu Gly Tyr Ala Glu His Pro Ala 50 55 60 Leu Gly Glu Arg Asp Tyr Ala Ile Ala Arg Asp Glu Ala Thr Gly Gln 65 70 75 80 Asn Leu Arg Lys Leu Leu Pro Ser Phe Ser Thr Ile Thr Tyr Ala Glu 85 90 95 Leu His Asn Arg Val Gln Gly Leu Ala Asn Ala Trp Arg Cys Asn Pro 100 105 110 Gln Asn Arg Val Ala Pro Gly Asp Phe Val Cys Ile Phe Gly Ser Thr 115 120 125 Ser Ile Asp Tyr Val Ala Val Asp Leu Ala Cys Val Tyr Ala His Ala 130 135 140 Val Ser Val Pro Leu Gln Thr Thr Leu Ala Glu Ala Asp Leu Met Arg 145 150 155 160 Ile Leu Ala Tyr Ser Asn Pro Ala Ala Leu Val Ala Gly Pro Gly Asp 165 170 175 Leu Ser Ile Val Ala Arg Leu Ala Val Glu His Gly Ser Ile Pro Ala 180 185 190 Leu Val Val Met Glu Tyr Asp Glu Arg Asp Asp Arg Glu Arg Ala Gln 195 200 205 Phe Glu Ala Ala Lys Ala Lys Leu Asp Ser Ala Gly Val Leu Thr Gln 210 215 220 Ile Val Thr Ile Lys Ala Leu Ile Glu Asp Gly Gln Ser Thr Thr Trp 225 230 235 240 Glu Phe Leu Leu Pro Gly Pro Glu Gly Ala Glu Arg Thr Val Met Leu 245 250 255 Leu His Ser Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Ile Tyr Pro 260 265 270 Glu Arg Ala Ala Lys Ala Leu Trp Leu Thr Thr Arg Asn Gln Leu Pro 275 280 285 Met Val Gly Val Ser Tyr Ala Pro Leu Asn His Leu Val Gly Arg Thr 290 295 300 Thr Ile Ser Asn Val Leu Ser Ala Gly Gly Thr Ala Tyr Val Thr Ala 305 310 315 320 Lys Ala Asp Leu Ser Thr Leu Phe Glu Asp Ile Arg Leu Val Arg Pro 325 330 335 Thr Tyr Leu Asn Leu Ile Pro Arg Ile Cys Asp Leu Val Tyr Gln His 340 345 350 Tyr Gln Asn Glu Val Leu Arg Arg Thr Lys Ala Gly Glu Gly Asp Lys 355 360 365 Glu Ser Val Gly Gln Arg Val Lys Ala Gln Met Arg Ser Thr Phe Leu 370 375 380 Gly Asp Arg Phe Leu Gly Ala Val Ile Ser Ser Ala Pro Thr Ser Pro 385 390 395 400 Ala Val Lys Glu Phe Met Arg Asp Cys Phe Asp Ile Leu Phe Gln Asp 405 410 415 Phe Tyr Gly Thr Thr Glu Ser Val Ala Gly Leu Phe Leu Asp Gly Arg 420 425 430 Val Leu Arg Pro Arg Val Lys Asp Tyr Arg Leu Arg Asp Val Pro Glu 435 440 445 Leu Gly Tyr Ser Val Gln Asp Lys Pro Tyr Pro Arg Gly Glu Phe Cys 450 455 460 Phe Lys Ser Asp Tyr Cys Ile Lys Gly Tyr Tyr Gln Met Pro Glu Ala 465 470 475 480 Ser Ala Ala Leu Phe Asp Glu Asp Gly Tyr Gln Cys Thr Gly Asp Ile 485 490 495 Val Glu Glu Arg Ala Phe Asp His Val Val Ile Ile Asp Arg Arg Asn 500 505 510 Asp Val Gln Lys Leu Ser His Gly Glu Tyr Val Ala Val Gly Pro Leu 515 520 525 Gly Thr Val Phe Glu Ser Gly Ser Ala Val Ile Lys Gln Ile Tyr Leu 530 535 540 Tyr Gly Asn Ser Leu Arg Ala Tyr Leu Leu Ala Val Val Val Pro Asn 545 550 555 560 Arg Glu Val Val Thr Ser Leu Leu Gly Asp Asn Pro Gly Glu Ala Gln 565 570 575 Leu Arg Ala Leu Ile Arg Arg Glu Leu Gln Thr Val Gly His Asn Ala 580 585 590 Lys Leu Arg Gly Phe Glu Val Pro Arg Asp Phe Ile Ile Asp Trp Glu 595 600 605 Pro Phe Ser Ile Glu Asn Gly Leu Leu Ser Ser Val Leu Lys Arg Lys 610 615 620 Arg Pro Asn Leu Lys Arg Lys Tyr Gly Glu Gln Leu Glu Ala Leu Tyr 625 630 635 640 Glu Lys Leu Glu Gln Lys Gln Lys Gln Asp Leu Glu Ala Leu Lys Asp 645 650 655 Pro Thr Ser Ser Leu Thr Val Leu Glu Lys Ile Cys Ala Leu Leu Ala 660 665 670 Ala Asn Leu Gly Leu Gln Glu Thr Asp Ile Asp Pro Arg Arg Thr Tyr 675 680 685 Lys Glu Leu Gly Gly Asp Ser Leu Gly Ala Val Thr Phe Ser Ile Met 690 695 700 Met Glu Glu Ile Phe Asp Val Leu Ile Pro Ala Asp Ala Ile Leu Ser 705 710 715 720 Pro Ile Gly Ser Pro Ala Ala Trp Ala Glu Ala Ile Thr Ser Ala Gln 725 730 735 Asn Pro Ala Gly Val Arg Ser Pro Gly Phe Ala Asp Ile His Gly Lys 740 745 750 Gly Ala Lys Lys Ile Ser Gly Lys Asp Leu Thr Leu Glu Arg Phe Leu 755 760 765 Gly Gln Ser Ala Leu Arg Asn Ala Ala Thr Glu Ser Ala Gly Ala Val 770 775 780 Lys Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Ser Arg Phe Leu 785 790 795 800 Thr Leu Glu Tyr Leu Gln Lys Leu Ala Asn Lys Gly Gly Lys Leu Ile 805 810 815 Cys Leu Val Trp Ala Arg Asp Asn Asp Asp Ala Lys Arg Gln Leu Asp 820 825 830 Ala Val Phe Ala Gly Ala Asp Pro Glu Met Glu Ala Arg Tyr Arg Asn 835 840 845 Leu Ala Glu Lys His Leu Asp Val Leu Ala Gly Asp Ile Ser Ala Pro 850 855 860 Leu Cys Gly Leu Lys Gln Glu Ala Phe Glu Gln Leu Ala Ser Arg Val 865 870 875 880 Asp Arg Ile Val His Ala Ala Ala Leu Val Asn His Ala Leu Ala Tyr 885 890 895 Glu His Phe Phe Gly Ser Asn Val Val Gly Thr Ala Glu Met Ile Arg 900 905 910 Leu Ala Val Ser Lys Arg Lys Lys Pro Ile Asp Phe Phe Ser Thr Val 915 920 925 Ala Val Arg Pro Phe Leu Lys Leu Thr Lys Gly Gln Cys Asp Thr Glu 930 935 940 Gln Ser Pro Ile Lys Asp Ser Ile Val Leu Ala Pro Gly Tyr Ala Ala 945 950 955 960 Gly Tyr Gly Ala Ser Lys Trp Ala Gly Glu His Leu Leu Gly Asp Ala 965 970 975 His Arg Arg Phe Gly Leu Pro Val Asn Ile Phe Arg Cys Asp Met Met 980 985 990 Leu Ala His Gln Lys Tyr Val Gly Gln Ile Asn Lys Thr Asp Met Phe 995 1000 1005 Thr Arg Leu Val Tyr Ser Leu Ile Val Thr Gly Ile Ala Pro Gly 1010 1015 1020 Ser Phe Tyr Leu Pro Gln Ser Asp Gly Ser Arg Ser Lys Ala His 1025 1030 1035 Tyr Asp Gly Val Pro Val Asp Val Val Ala Ser Val Val Ala Gly 1040 1045 1050 Val Ser Asp Asp Thr Ala Ser Ala Leu Lys Val Phe Asn Val Arg 1055 1060 1065 Asn Tyr His Asp Ser Asp Gly Val Ser Leu Asp Ser Phe Ala Asp 1070 1075 1080 Trp Ile Arg Ser Ala Gly Tyr Pro Leu Glu Gln Val His Asn Tyr 1085 1090 1095 Lys Asp Trp Val Thr Arg Phe Glu Gln Met Leu Lys Asn Leu Pro 1100 1105 1110 Asp Asp Gln Arg Gln Asn Ser Phe Leu Asp Leu Met Gly Ala Val 1115 1120 1125 Arg Asp Pro Trp Pro Pro Lys Met Leu Val Gln Asp Ser Ser Gln 1130 1135 1140 Phe Gln Glu Leu Val Gln Arg Leu Pro Ile Gly Asp Met Pro His 1145 1150 1155 Leu Ser Glu Val Tyr Val His Lys Cys Leu Asp Asp Met Arg Arg 1160 1165 1170 Leu Gly Leu Ile Pro Ala Pro Val His Ala Ser Leu Leu 1175 1180 1185 <210> 203 <211> 1164 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium tusciae <400> 203 Met Ser Thr Asp Thr Arg Glu Glu Arg Leu Ala Arg Arg Ile Ala Asp 1 5 10 15 Leu Thr Ala Ala Asp Pro Gln Phe Ala Ala Ala Lys Pro Asp Pro Ala 20 25 30 Val Ser Gln Ala Ile Glu Asn Pro Glu Leu Ser Leu Asp Ala Val Val 35 40 45 Arg Thr Val Leu Thr Ala Tyr Ala Asp Arg Pro Ala Leu Gly Glu Arg 50 55 60 Ala Val Asp Tyr Val Glu Asp Arg Arg Gly Arg Thr Ser Ala Lys Leu 65 70 75 80 Leu Pro His Tyr Asn Thr Ile Thr Tyr His Glu Leu Asp Asp Arg Ile 85 90 95 Ser Ser Leu Thr Arg Ala Leu Thr Asp Val His Pro Gly Asp Arg Val 100 105 110 Ala Ile Leu Gly Phe Gly Ser Ile Asp Tyr Thr Val Ile Asp Val Ala 115 120 125 Thr Ile Pro Leu Gly Ala Ile Ala Val Pro Leu Gln Thr Ser Ala Pro 130 135 140 Leu Thr Ala Leu Arg Pro Ile Val Ile Glu Thr Glu Pro Ala Val Ile 145 150 155 160 Ala Ser Ser Ile Asp Tyr Val Asp Asp Ala Ala Glu Leu Val Leu Thr 165 170 175 Gly Tyr Ala Pro Ser Ser Leu Val Val Phe Asp Tyr Asp Pro Glu Ile 180 185 190 Thr Asp His Arg Asp Ala Tyr Asp Ala Leu Arg Ala Arg Leu Ala Asp 195 200 205 Ala Glu Ser Thr Val Val Val Glu Thr Leu Gln Asp Ala Leu Glu Arg 210 215 220 Gly Lys Thr Leu Pro Ala Lys Pro Ala Ala His Arg Glu Ala Asp Asp 225 230 235 240 Met Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly 245 250 255 Ala Ile Tyr Thr Arg Asn Met Thr Gly Lys Leu Trp Arg Pro Ala Ser 260 265 270 Trp Gly Trp Ala Asp Ser Val Glu Pro Ser Ile Val Leu Ser Phe Met 275 280 285 Pro Met Ser His Val Met Gly Arg Ser Gly Leu Phe Gly Ala Leu Ser 290 295 300 His Gly Gly Thr Ala Tyr Phe Ala Ala Lys Ser Asp Leu Ser Thr Phe 305 310 315 320 Leu Asp Asp Leu Ala Leu Val Arg Pro Thr Gln Leu Ser Phe Val Pro 325 330 335 Arg Val Trp Asp Met Leu Ser Ala Glu Val His Ser Arg Leu Asp Arg 340 345 350 His Ala Phe Glu Gly Thr Asp Thr Lys Ser Asp Ala Glu Phe Leu Ala 355 360 365 Asp Val Arg Ala Ala Val Ile Gly Asn Arg Tyr Leu Thr Ala Val Thr 370 375 380 Gly Ser Ala Pro Thr Ser Ser Asp Leu Lys Ala Trp Val Glu Ser Phe 385 390 395 400 Leu Asp Leu Asp Leu Leu Asp Gly Tyr Gly Ser Thr Glu Ala Gly Gly 405 410 415 Val Leu Leu Asn Gly Gln Ile Lys Arg Pro Pro Val Ile Glu Tyr Lys 420 425 430 Leu Ala Asp Val Pro Asp Leu Gly Tyr Phe Ser Thr Asp Arg Pro His 435 440 445 Pro Arg Gly Glu Leu Leu Leu Lys Thr Val Asn Met Phe Pro Gly Tyr 450 455 460 Tyr Lys Arg Pro Glu Val Thr Ala Glu Val Phe Asp Glu Glu Gly Phe 465 470 475 480 Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Gly Pro Asp Arg Leu Gln 485 490 495 Tyr Val Asp Arg Arg Asn Phe Val Leu Lys Leu Ser Gln Gly Glu Phe 500 505 510 Val Thr Ala Ser Lys Leu Glu Ala Val Phe Glu Thr Ser Pro Leu Val 515 520 525 Arg Gln Ile Tyr Ile Tyr Gly Asn Ser Ala Arg Ser Tyr Leu Leu Ala 530 535 540 Val Ile Val Pro Thr Pro Glu Ala Leu Ser Gln His Asp Thr Ser Glu 545 550 555 560 Leu Arg Ala Leu Ile Ser Glu Ser Leu Ala Asp Val Ala Lys Gly Ala 565 570 575 Asp Leu Gln Ser Phe Glu Val Pro Arg Asp Phe Ile Leu Glu Thr Thr 580 585 590 Ala Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala 595 600 605 Arg Pro Lys Leu Lys Glu Ile Tyr Gly Pro Gln Leu Glu Glu Leu Tyr 610 615 620 Glu Asp Leu Ala Gln Gly Gln Ala Ala Glu Leu Arg Glu Leu Arg Gln 625 630 635 640 Asp Gly Ala Thr Cys Pro Val Ile Glu Thr Val Thr Arg Ala Ala Ala 645 650 655 Ala Leu Leu Gly Ser Ala Ala Ala Asp Leu Ser Pro Asp Ala His Phe 660 665 670 Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ala Asn Leu 675 680 685 Leu Arg Glu Ile Phe Phe Val Glu Val Pro Val Gly Val Ile Val Ser 690 695 700 Pro Ala Thr Asp Leu Ala Ala Leu Ala Glu Tyr Ile Glu Thr Glu Arg 705 710 715 720 Ser Gly Ser Thr Arg Pro Thr Phe Ala Ser Val His Gly Arg Gly Ala 725 730 735 Thr Glu Ile His Ala Arg Asp Leu Met Leu Gly Lys Phe Leu Asp Ala 740 745 750 His Thr Leu Ala Asn Ala Pro Ala Leu Pro Tyr Pro Ser Gln Glu Val 755 760 765 Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu 770 775 780 Ala Leu Asp Trp Leu Glu Arg Met Ser Leu Val Gly Gly Arg Val Ile 785 790 795 800 Thr Leu Val Arg Ala Lys Asp Asp Ala Thr Ala Arg Gln Arg Leu Asp 805 810 815 Glu Thr Phe Asp Ser Gly Asp Pro Ala Leu Leu Asp His Tyr Arg Arg 820 825 830 Leu Ala Ala Gly His Leu Glu Val Leu Ala Gly Asp Lys Gly Glu Pro 835 840 845 Gly Leu Gly Leu Asp Glu Thr Thr Trp Gln Arg Leu Ala Asp Ser Val 850 855 860 Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Asp Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Leu Val Arg 885 890 895 Leu Ala Leu Thr Thr Lys Leu Lys Pro Phe Val Tyr Leu Ser Thr Val 900 905 910 Gly Val Gly Asp Gln Ile Glu Pro Ser Ala Phe Val Glu Asp Ala Asp 915 920 925 Val Arg Gln Ile Ser Ala Thr Arg Val Val Asn Asp Ser Tyr Ala Asn 930 935 940 Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala 945 950 955 960 His Asp Leu Ser Gly Leu Pro Val Glu Val Phe Arg Cys Asp Met Ile 965 970 975 Leu Ala Glu Pro Glu Tyr Ala Gly Gln Leu Asn Val Pro Asp Met Phe 980 985 990 Thr Arg Leu Met Leu Ser Leu Val Ala Thr Gly Ile Ala Pro Gly Ser 995 1000 1005 Phe Tyr Glu Leu Asp Ala Ala Gly His Arg Gln Arg Ala His Tyr 1010 1015 1020 Asp Gly Leu Pro Val Asp Phe Ile Ala Asp Ala Ile Ser Thr Leu 1025 1030 1035 Gly Ala His His Ser Tyr Gly Phe Glu Thr Phe His Val Met Asn 1040 1045 1050 Pro His Asp Asp Gly Val Gly Leu Asp Glu Phe Val Asp Trp Leu 1055 1060 1065 Val Asp Ala Gly Tyr Pro Ile Asp Arg Val Ala Asp Tyr Gly Glu 1070 1075 1080 Trp Leu Gln Arg Phe Glu Met Ser Met Arg Gly Leu Pro Asp Arg 1085 1090 1095 Gln Arg Gln Ala Ser Leu Leu Pro Leu Leu His Ser Tyr Ala Gln 1100 1105 1110 Pro Ala Lys Pro Leu Leu Gly Ser Val Ala Thr Thr Asp Arg Phe 1115 1120 1125 Arg Ala Ala Val Gln Asp Ala Lys Ile Gly Pro Asp Lys Asp Ile 1130 1135 1140 Pro His Ile Thr Ala Glu Ile Ile Val Lys Tyr Ile Thr Asp Leu 1145 1150 1155 Gln Leu Leu Gly Leu Leu 1160 <210> 204 <211> 1181 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium goodii <400> 204 Met Gln Asp Arg Leu Asn Arg Arg Ile Ala His Leu Tyr Ala Thr Asp 1 5 10 15 Pro Gln Phe Ala Ala Ala Leu Pro Asp Ala Asp Thr Val Ala Thr Ile 20 25 30 Arg Thr Arg Glu Leu Arg Leu Asn Glu Phe Phe Glu Thr Val Val Ala 35 40 45 Ala Tyr Gly Asp Arg Pro Ala Leu Gly Thr Arg Ala Arg Ala Ser Asp 50 55 60 Pro Glu Asn Asp Ile Gly Thr Cys Leu Ala Pro Arg Phe Arg Thr Leu 65 70 75 80 Ser Phe Arg Glu Thr Trp Ala Arg Val Ser Ala Val Ala Thr Ala Leu 85 90 95 Arg Arg Gly Asp Glu Pro Pro Leu Gln Pro Gly Asp Val Val Val Ile 100 105 110 Ile Gly Phe Ser Ser Ala Asp His Leu Val Val Glu Leu Ala Cys Ala 115 120 125 Tyr Leu Gly Leu Val Ala Val Pro Leu Ala His Asn Ala Thr Ala Ala 130 135 140 Gln Leu Arg Pro Ile Ile Asp Glu Val Glu Pro Arg Val Val Ala Val 145 150 155 160 Gly Ala Gly His Ile Arg Leu Ala Val Asp Ala Thr Ile Asp Ala Pro 165 170 175 Ser Val Arg Gln Val Val Val Phe Asp Gly Gly Asp Asp Asp Ala Gly 180 185 190 Gln Glu Val Ala Ala Leu Gly Tyr Gly His Arg Thr Val Arg Phe His 195 200 205 Thr Leu Asp Gly Leu Ala Glu Thr Gly Arg Arg Val Pro Ala Glu Leu 210 215 220 Pro Tyr Met Gly Gly Ser Pro Gln Arg Leu Ala Met Ile Leu Tyr Thr 225 230 235 240 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr Thr Glu Ala Met 245 250 255 Val Thr Lys Leu Trp Cys Ser Gly Leu Val Pro Val Glu Val Pro Val 260 265 270 Phe Asn Leu Asn Phe Gln Pro Leu Asn His Gly Ala Gly Arg Leu Pro 275 280 285 Leu Ile Ala Ala Phe Gln Ala Gly Gly Thr Ser Tyr Phe Val Ala Glu 290 295 300 Pro Asp Leu Ser Thr Leu Phe Glu Asp Trp Ala Ser Val Arg Pro Thr 305 310 315 320 Gln Leu Pro Leu Val Pro Arg Val Val Asp Met Leu Tyr Gln Arg Tyr 325 330 335 Arg Ala Ser Val Asp Arg Ala Ser Thr Cys Gly Ser Ser Leu Cys Ala 340 345 350 Ala Glu Ala Ala Ala Ala Ala Glu Leu Arg Asp Asp Val Leu Gly Gly 355 360 365 Arg Val Leu Asn Ala Phe Val Gly Thr Ala Pro Leu Gly Glu Pro Met 370 375 380 Lys Arg Phe Leu Asp Thr Val Leu Asp Ile His Val Ile Asp Ala Tyr 385 390 395 400 Gly Thr Ser Glu Ala Gly Val Ile Ala Lys Asp Gly Val Ile Met Arg 405 410 415 Pro Pro Val Leu Asp Tyr Lys Ile Ile Asp Val Pro Glu Leu Gly Tyr 420 425 430 Arg Arg Ser Asp Lys Pro Phe Pro Arg Gly Glu Leu Ala Val Arg Thr 435 440 445 Val Ser Ala Thr Pro Gly Tyr Phe Lys Arg Pro Asp Leu Thr Ser Met 450 455 460 Ile Phe Asp Ser Glu Gly Tyr Cys Arg Thr Gly Asp Val Val Ala Glu 465 470 475 480 Ile Ala Pro Asp His Ile Ser Ile Ile Asp Arg Arg Asn Asn Val Ile 485 490 495 Lys Leu Ser Gln Gly Glu Phe Val Ala Ile Glu Arg Leu Glu Thr Leu 500 505 510 Tyr Ala Thr Ala Pro Leu Val Arg Gln Ile Phe Leu His Gly Asn Gly 515 520 525 Asp Arg Pro Arg Leu Leu Ala Val Val Val Pro Thr Gly Glu Ala Ile 530 535 540 Ala Ala Ala Arg Asp Pro Gly Gly Leu Lys Arg Val Leu Leu Glu Ser 545 550 555 560 Leu Gln Arg Thr Ala Glu Glu His Gly Leu Arg Ser Phe Glu Ile Pro 565 570 575 Val Asp Ile Ile Val Glu Asn Thr Pro Phe Ser Ala Asp Asp Gly Leu 580 585 590 Leu Ser Ser Gly Gly Lys Leu Leu Arg Pro Arg Leu Ile Glu Arg Phe 595 600 605 Gly Glu Arg Leu Glu Gln Met Phe Asp Asp Leu Ala Val Ala Gln Val 610 615 620 Thr Ala Ile Arg Gln Leu Arg Thr Val Ala Ala Ala Gly Arg Thr Val 625 630 635 640 Glu Ala Val Val His Ala Ala Arg Val Val Leu Gly Ala Asp Gln Val 645 650 655 Asp Ser His Val Pro Phe Val Ala Leu Gly Gly Asp Ser Leu Ser Ala 660 665 670 Leu Thr Phe Ser Asp Val Leu Arg Gln Met Tyr Gly Phe Glu Val Pro 675 680 685 Val Ser Met Ile Ile Ser Pro Ala Gly Asp Leu Ser Gln Leu Ala Asp 690 695 700 Phe Ile Asp Gly Arg Arg Gly Ser Gly Ala Arg Val Ser Thr Gly Ala 705 710 715 720 Val His Gly Glu Asp Val Thr Glu Leu Arg Ala Ala Asp Leu Lys Leu 725 730 735 Asp Lys Phe Ile Asp Arg Gln Ala Leu Val Asp Ala Val Ser Leu Pro 740 745 750 Arg Pro Thr Gly Val Pro Asn Thr Val Leu Val Thr Gly Ala Asn Gly 755 760 765 Trp Leu Gly Arg Phe Leu Thr Leu Glu Leu Leu Arg Arg Ala Ala Arg 770 775 780 Arg Gly Gly Thr Val Ile Ala Met Ala Arg Ala Arg Thr Ala Asp Ala 785 790 795 800 Ala Arg Ala Arg Leu Ile Gln Ala Phe Asp Arg Gly Asp Asp Asp Leu 805 810 815 Met Arg Glu Phe Thr Thr Leu Ala Ala Asp His Leu Gly Val Val Ala 820 825 830 Gly Asp Leu Thr Ala Pro Leu Leu Gly Leu His Pro Val Val Trp Ser 835 840 845 Arg Leu Thr Arg Thr Val Asp Ser Ile Val His Thr Ala Ala Leu Val 850 855 860 Asn His Leu Leu Pro Tyr Gly Glu Leu Phe Gly Pro Asn Val Ala Gly 865 870 875 880 Thr Ala Glu Val Ile Arg Met Ala Ile Thr Asn Lys Leu Lys Ser Val 885 890 895 Ser Tyr Val Ser Ser Met Ala Ile Ile Gly Glu Gly Glu Pro Ser Met 900 905 910 Leu Asn Glu Ala Gly Asp Ile Arg Ser Leu Asn Pro Val Arg Ile Asn 915 920 925 Thr Ala Asp Gly Pro Gly Thr Tyr Ala Leu Gly Tyr Ala Asn Ser Lys 930 935 940 Trp Ala Gly Glu Ile Leu Leu Arg Glu Ala His Asp Leu Cys Lys Leu 945 950 955 960 Pro Val Ala Val Phe Arg Ser Asp Met Val Met Ala His Arg Arg Phe 965 970 975 Ser Gly Gln Ile Asn Arg Asp Asp Leu Val Thr Arg Leu Ile Leu Ser 980 985 990 Leu Val Val Thr Gly Ile Ala Pro Arg Ser Phe Tyr Asp Lys Thr Cys 995 1000 1005 Val Asn Ala Arg Phe Asp Gly Leu Pro Val Asp Phe Val Ala Arg 1010 1015 1020 Ala Ile Ala Ala Ile Ser Gln Asp Gly Ala Ala Gly Phe Arg Thr 1025 1030 1035 Phe Asn Val Ser Ser Pro His Asp Asp Gly Val Ser Leu Asp Val 1040 1045 1050 Phe Ile Asp Trp Leu Glu Ala Ala Gly His Ala Ile Thr Arg Val 1055 1060 1065 Asp Asp His Asp Glu Trp Leu Arg Arg Phe Glu Asp Thr Leu Lys 1070 1075 1080 Ala Leu Pro Thr Asp Leu Arg Asn Arg Ser Val Leu Pro Leu Ile 1085 1090 1095 Asp Ala Tyr Arg Arg Pro Ile Arg Ser Thr Arg Gly Ile Ala Arg 1100 1105 1110 Ala Phe Gln Gln Ala Ala Arg Glu His Gly Val Gly Glu Ile Pro 1115 1120 1125 Arg Leu Ser Ser Thr Leu Ile Asp Lys Tyr Val Ala Asp Leu Ser 1130 1135 1140 Val Ala Val Gly Val Lys Val Arg Ser Ala Ser Leu Cys Pro Ala 1145 1150 1155 Gln Ser Ser Ser Ser Asp Ser Thr Ser Ser Gly Val Thr Ser Arg 1160 1165 1170 Val Ala Ile Pro Pro Ser Arg Pro 1175 1180 <210> 205 <211> 1171 <212> PRT <213> Artificial Sequence <220> <223> Frankia sp. EUN1h <400> 205 Met Ser Val Thr Asp Val Arg Arg Pro Ala Asp Arg Leu Ala Glu Leu 1 5 10 15 Val Glu Thr Asp Asp Glu Leu Arg Ala Leu Thr Pro Asp Pro Lys Val 20 25 30 Thr Ala Ala Ala Arg Arg Pro Gly Leu Ser Tyr Arg Gln Ile Val Glu 35 40 45 Thr Val Leu Asp Gly Tyr Ala Glu Arg Ala Ala Leu Gly Gln Arg Arg 50 55 60 Tyr Glu Ile Val Gln Asp Gly Ala Gly Arg Ala Arg Arg Val Asp Gln 65 70 75 80 Pro Gly Phe Asp Thr Ile Thr Tyr Gly Glu Leu His Arg Arg Ile Arg 85 90 95 Cys Leu Ala Ala Val Trp Lys His Asp Pro Leu Tyr Arg Val Glu Pro 100 105 110 Gly Asp Leu Val Cys Ile Leu Gly Phe Ala Ser Thr Asp Tyr Val Thr 115 120 125 Val Asp Leu Ala Ala Ala Tyr Gln Leu Ala Val Ser Val Pro Leu Gln 130 135 140 Ala Thr Leu Ala Ala Thr Asp Leu Arg Gly Thr Ile Ala Asp Thr Ala 145 150 155 160 Pro Thr Ala Val Ala Ala Glu Met Val Asp Leu His Leu Ala Ala Thr 165 170 175 Leu Ala Gly Thr Gln Glu Ser Ile Arg Thr Ile Ile Ala Leu Ser Tyr 180 185 190 Asp Ala Arg Val Asp Glu Asp Arg Glu Arg Leu Ala Ala Ala Arg Asp 195 200 205 Glu Leu Ala Arg Asn Arg Ser Arg Ala Arg Leu Val Thr Leu Asp Glu 210 215 220 Leu Leu Val Ala Gly Ala Gly Leu Pro Ala Trp Glu Pro Pro Pro Ala 225 230 235 240 Ser Ala Ala Gly Thr Arg Arg Met Thr Leu Leu Ile His Ser Ser Gly 245 250 255 Ser Thr Gly Thr Pro Lys Gly Val Ile Val Thr Glu Gly Thr Val Ala 260 265 270 Ala Gln Trp Asp Pro Gly Glu Arg Pro Gly Pro Val Val Arg Val Ala 275 280 285 Leu Ala Pro Leu Asn His Met Ala Gly Arg His Met Ile Tyr Ser Ala 290 295 300 Leu Ala Arg Gly Gly Arg Ala Asn Ile Thr Ala Arg Ser Asp Leu Ser 305 310 315 320 Thr Val Phe Glu Asp Ile Arg Leu Thr Arg Pro Thr Glu Met Ser Ala 325 330 335 Phe Pro Arg Ile Leu Asp Leu Ile His Gln His Phe Leu Ser Glu Val 340 345 350 Val Arg Arg Thr Ser Ala Gly Ala Asp Ala Ala Thr Ala Arg Ala Glu 355 360 365 Ala Met Arg Leu Val Arg Thr Glu Phe Leu Gly Asp Arg Val Cys Met 370 375 380 Ile Gly Gly Ala Gly Ala Pro Val Thr Pro Gln Val Gln Ser Phe Ile 385 390 395 400 Glu Glu Cys Phe Gln Val Arg Leu Gly Gly Gly Tyr Gly Ser Thr Glu 405 410 415 Ala Gly Thr Met Ala Val Met Gly Arg Val Leu Arg Pro Pro Val Ile 420 425 430 Asp Tyr Arg Leu Arg Asp Val Pro Asp Leu Gly Tyr Phe Leu Thr Asp 435 440 445 Lys Pro Tyr Pro Arg Gly Glu Phe Cys Val Lys Ser Glu Arg Ala Thr 450 455 460 Pro Gly Tyr Phe Lys Arg Pro Glu Ala Thr Ala Ala Leu Phe Asp Ala 465 470 475 480 Asp Gly Phe Leu Arg Thr Gly Asp Ile Val Glu Glu Arg Gly Pro Asp 485 490 495 Gln Ile Glu Trp Ile Gly Arg Arg Asn Asp Val Leu Lys Leu Ala Gln 500 505 510 Ser Glu Phe Val Ala Val Gly Gly Leu Ala Thr Thr Phe Glu Asn Gly 515 520 525 Ser Glu Leu Ile Asp Gln Ile Phe Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Val Leu Ala Val Val Val Pro Asn Pro Asp Val Val Arg Asp Arg 545 550 555 560 Leu Gly Asp Arg Pro Thr Glu Thr Ser Val Arg Ser Leu Ile Arg Ser 565 570 575 Ala Leu Arg Asp Val Ala Ala Arg Glu Asp Leu Arg Ser Phe Glu Val 580 585 590 Pro Arg Asp Phe Ile Val Glu His Glu Pro Phe Thr His Glu Asn Gly 595 600 605 Leu Leu Ser Ser Val His Lys Arg Met Arg Pro Ala Leu Glu Ala Arg 610 615 620 Tyr Arg Asp Arg Leu Glu Gln Leu Tyr Thr Asp Leu Glu Leu Arg Arg 625 630 635 640 Thr Glu Asn Leu Thr Ala Leu Arg Glu Leu Asp Gly Gly Ser Val Leu 645 650 655 Asp Lys Val Ala Arg Ala Leu Glu Val Ala Leu Gly Val Glu Asp Ile 660 665 670 Asp Arg Ser Ala Pro Leu Gly Phe Leu Asp Leu Gly Gly Asp Ser Leu 675 680 685 Gly Ala Ala Ala Phe Ser Thr Val Leu Ala Gly Ile Phe Gly Val Glu 690 695 700 Val Pro Val Asn Ala Ile Leu Ser Pro Thr Gly Asn Pro Arg Thr Trp 705 710 715 720 Thr Arg Leu Ile Glu Ser Ala Leu Asp Gln Ser Ser Glu Arg Leu Thr 725 730 735 Thr Phe Glu Arg Val His Gly Lys Gly Ala Arg Leu Leu Arg Ala Ala 740 745 750 Asp Leu Asp Ile Arg Ala Phe Leu Asp Ala Asp Val Leu Arg Gln Pro 755 760 765 Pro Ser Glu Pro Pro Pro Ala Val Ser Asn Cys Val Leu Leu Thr Gly 770 775 780 Ala Thr Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Glu Arg 785 790 795 800 Leu Glu Ala Thr Gly Gly Arg Leu Ile Cys Leu Val Arg Ala Thr Asp 805 810 815 Glu Ala Ala Ala Leu Arg Arg Leu Thr Ala Val Phe Asp Thr Asp Pro 820 825 830 Asp Leu Arg Gln Arg Phe Ala Ala Leu Ser Glu Gly Arg Leu Glu Val 835 840 845 Val Val Gly Asp Val Ala Glu Pro Gly Leu Gly Leu Ser Val Ala Asp 850 855 860 Phe Asp Arg Leu Ala Arg Gln Val Asp Arg Val Val His Pro Gly Ala 865 870 875 880 Leu Val Asn His Val Leu Pro Tyr Glu Asp Leu Phe Gly Pro Asn Val 885 890 895 Ala Gly Thr Ala Glu Leu Val Arg Leu Ala Leu Thr His Arg Gln Lys 900 905 910 Arg Phe Asp Phe Val Ser Ser Ala Ala Thr Thr His Leu Leu Asp Arg 915 920 925 Gly Ala Pro Arg His Glu Asp Ser Pro Leu Leu Ala Glu Ile Asp Leu 930 935 940 Asp Ser His Arg Met Gly Tyr Gly Ala Ser Lys Trp Ala Ala Glu Gln 945 950 955 960 Val Leu Leu Ser Ala His Arg Ala Thr Gly Leu Pro Val Asn Val Phe 965 970 975 Arg Gly Asp Met Met Leu Ala His Arg Thr Tyr His Gly Gln Ile Asn 980 985 990 Val Pro Asp Val Phe Thr Arg Leu Leu Thr Ser Ile Val Leu Ala Gly 995 1000 1005 Val Ala Pro Ala Ser Phe Tyr Pro Pro Thr Glu Thr Gly Ala Pro 1010 1015 1020 Ala Arg Ala His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Ala 1025 1030 1035 Thr Ile Val Gly Ile Ser Thr Gln Pro His Asp Gly Ala Arg Asn 1040 1045 1050 Tyr His Val Leu Asn His His Ala Asp Asp Gly Ile Ser Leu Asp 1055 1060 1065 Thr Phe Val Gly Trp Ile Ala Glu Ala Gly Tyr Pro Ile Glu Arg 1070 1075 1080 Val Pro Asp Tyr Ala Thr Trp Phe Ala Arg Phe Glu Thr Lys Leu 1085 1090 1095 Lys Ala Leu Pro Glu Ala Lys Arg Gln His Ser Ser Leu Thr Val 1100 1105 1110 Leu Gly Thr Met Ser Arg Pro Arg Pro Val Glu Pro Met Val Asp 1115 1120 1125 Thr Thr Arg Phe Gln Ala Ala Val Arg Asp Leu Pro Val Gly Pro 1130 1135 1140 Arg Ile Pro His Leu Thr Arg Glu Phe Ile His Lys Cys Leu Asp 1145 1150 1155 Asp Met Ile Arg Met Gly Leu Val Pro Pro Pro Pro Ala 1160 1165 1170 <210> 206 <211> 1168 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. JS623 <400> 206 Met Ser Thr Val Ser Arg Glu Glu Arg Leu Ala Arg Arg Ile Ser Asp 1 5 10 15 Leu Tyr Ala Thr Asp Gln Gln Phe Ala Asp Ala Arg Pro Ser Glu Ala 20 25 30 Val Ala His Ala Ile Glu Ser Pro Ala Leu Arg Leu Pro Gln Ile Ile 35 40 45 Gln Thr Val Ile Asp Gly Tyr Ala Glu Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Val Glu Phe Val Thr Asp Pro Thr Thr Gly Arg Thr Ser Ala Ala 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Arg Glu Leu Ser Glu Arg 85 90 95 Val Asp Ala Val Ala Thr Ala Leu Thr Gln Asn Pro Val Arg Pro Gly 100 105 110 Asp Arg Val Ala Ile Leu Gly Phe Thr Ser Ile Asp Tyr Thr Thr Val 115 120 125 Asp Met Ala Leu Leu Arg Ala Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Pro Val Ala Gln Leu Arg Pro Ile Ala Ala Glu Thr Glu Pro 145 150 155 160 Val Ala Ile Leu Ser Ser Val Asp Phe Leu Asp Asp Ala Val Glu Leu 165 170 175 Met Leu Thr Gly His Leu Pro Glu Arg Leu Val Val Phe Asp Tyr His 180 185 190 Ala Glu Val Asp Asp His Arg Glu Ala Leu Ala Ser Ala Thr Ala Arg 195 200 205 Leu Ala Glu Thr Pro Val Val Val Glu Thr Leu Ala Glu Val Leu Ala 210 215 220 Arg Gly Asn Ala Leu Pro Ala His Pro Ala Phe Asp Ala Gly Asp Asp 225 230 235 240 Asn Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys 245 250 255 Gly Ala Met Tyr Leu Ala Lys Ala Val Ala Asn Ser Trp Arg Arg Ser 260 265 270 Ser Met Ala Met Trp Gly Asn Glu Gly Ala Thr Pro Ser Ile Thr Leu 275 280 285 Asn Phe Met Pro Met Ser His Met Met Gly Arg Gly Ile Leu Tyr Ala 290 295 300 Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Val Ala Arg Ser Asp Leu 305 310 315 320 Ser Thr Phe Phe Asp Asp Leu Ser Leu Val Arg Pro Thr Gln Leu Ser 325 330 335 Phe Val Pro Arg Ile Trp Asp Met Val Phe Ala Glu Tyr Gln Ser Glu 340 345 350 Val Asp Arg Arg Ser Ala Asp Gly Gly Asp Arg Trp Ala Val Glu Ala 355 360 365 Asp Val Leu Ala Asp Leu Arg Gln Asn Leu Leu Gly Gly Arg Phe Ile 370 375 380 Ser Ala Met Thr Gly Ser Ala Pro Ile Ser Ser Glu Met Arg Thr Phe 385 390 395 400 Val Glu Ser Leu Leu Asp Ile His Leu Thr Asp Gly Tyr Gly Ser Thr 405 410 415 Glu Ala Gly Ala Val Phe Val Asp Gly Gln Val Gln Arg Pro Pro Val 420 425 430 Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe Ser Thr 435 440 445 Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Glu Thr Met 450 455 460 Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Ile Thr Ala Asp Val Phe Asp 465 470 475 480 Ala Asp Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Gly Pro 485 490 495 Asp Gln Leu Gln Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Thr Val Ala Lys Leu Glu Ala Val Phe Val Asp 515 520 525 Ser Pro Leu Ile Arg Gln Ile Phe Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Leu Leu Ala Val Ile Val Pro Thr Glu Glu Ala Leu Ala Arg His 545 550 555 560 Asp Ala Ala Glu Leu Lys Gln Leu Ile Thr Glu Ser Leu Gln Asp Val 565 570 575 Ala Lys Ala Thr Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile 580 585 590 Ile Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile 595 600 605 Arg Lys Leu Ala Arg Pro Lys Leu Lys Glu Phe Tyr Gly Glu Arg Leu 610 615 620 Glu Gln Leu Tyr Thr Asp Leu Ala Asp Ser Gln Ala Asn Glu Leu Arg 625 630 635 640 Glu Leu Arg Gln His Gly Ala Asp Arg Pro Val Leu Glu Thr Ile Ser 645 650 655 Arg Ala Ala Gly Ala Leu Leu Gly Ala Ala Ala Ser Glu Leu Gln Pro 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Ala Asn Leu Leu His Glu Ile Phe Glu Ile Asp Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Leu Ala Ala Tyr Ile 705 710 715 720 Glu Ala Glu Arg Gln Pro Gly Ser Lys Arg Pro Thr Phe Ala Ser Val 725 730 735 His Gly Arg Asp Ala Thr Glu Val Tyr Ala Asn Asp Leu Thr Leu Asp 740 745 750 Lys Phe Ile Asp Ala Lys Thr Leu Ala Ala Ala Ser Ser Leu Pro Gly 755 760 765 Pro Ser Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Met Val 785 790 795 800 Asp Gly Lys Val Ile Ala Leu Val Arg Ala Lys Asp Asp Asp Ala Ala 805 810 815 Arg Glu Arg Leu Asp Lys Thr Phe Asp Ser Gly Asp Pro Glu Leu Leu 820 825 830 Arg His Tyr His Glu Leu Ala Ala Asp His Leu Glu Val Ile Ala Gly 835 840 845 Asp Lys Gly Glu Ala Asn Leu Gly Leu Asp Gln Gln Thr Trp Gln Arg 850 855 860 Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn 865 870 875 880 His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Ala Leu Gly Thr 885 890 895 Ala Glu Leu Ile Arg Ile Ala Leu Thr Thr Lys Gln Lys Pro Phe Val 900 905 910 Tyr Val Ser Thr Ile Gly Val Gly Ala Gly Ile Glu Pro Gly Gln Phe 915 920 925 Thr Glu Asp Gly Asp Val Arg Val Tyr Ser Ala Thr Arg Lys Val Asp 930 935 940 Asp Thr Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val 945 950 955 960 Leu Leu Arg Glu Ala His Asp Leu Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Asp Ser Phe Tyr Glu Val Asp Ala Asn Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala Glu Ala 1025 1030 1035 Ile Ser Thr Leu Gly Ala Gln Val Val Asp Gly Phe Glu Thr Tyr 1040 1045 1050 His Val Met Asn Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu Tyr 1055 1060 1065 Val Asp Trp Leu Ile Glu Ala Gly Phe Pro Val Glu Arg Val Gly 1070 1075 1080 Asp Tyr Thr Thr Trp Leu Gln Arg Phe Asp Thr Ala Val Arg Ala 1085 1090 1095 Leu Pro Glu Arg Gln Arg Gln Ala Ser Leu Leu Pro Leu Leu His 1100 1105 1110 Asn Tyr Gln Arg Pro Glu Thr Pro Ile Arg Gly Ser Ile Ala Pro 1115 1120 1125 Thr Asp Arg Phe Arg Ala Ala Val Gln Asp Ala Lys Ile Gly Pro 1130 1135 1140 Asp Lys Asp Ile Pro His Val Thr Arg Asp Val Ile Val Lys Tyr 1145 1150 1155 Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 <210> 207 <211> 1155 <212> PRT <213> Artificial Sequence <220> <223> Legionella moravica <400> 207 Met Glu Ile Ser Leu Ser Cys Ile Glu Leu Ile Glu Gln Tyr Cys Leu 1 5 10 15 Lys Tyr Gly Asp Lys Pro Ala Leu Gly Tyr Arg Lys Thr Glu Ile Thr 20 25 30 Asn Gln Asn Gln Asn Gln Thr Ile His Tyr Leu Pro Glu Phe Glu Thr 35 40 45 Leu Thr Phe Arg Gln Val Trp Asp Arg Ile Ser Tyr Ile Ala Lys Gly 50 55 60 Phe Asn Tyr Ser Asn Arg Val Ser Pro Asn Asp Phe Val Gly Ile Cys 65 70 75 80 Ala Phe Gly Ser Pro Glu Tyr Ile Leu Ala Glu Phe Ser Cys Leu Tyr 85 90 95 Leu Gly Ala Val Ser Val Pro Leu Gln Phe Asn Ile Lys Glu Pro Glu 100 105 110 Leu Ile Lys Ile Val Thr Asp Thr Lys Met Arg Cys Leu Ile Thr Gly 115 120 125 Leu Gln Gln Leu Lys Leu Ala Cys Asn Ala Val Pro His Cys Pro Ser 130 135 140 Ile Gln Ser Ile Ile Val Leu Asp Cys His Glu Glu Asp Lys Asp His 145 150 155 160 Ser Ile Gln Ile Arg Thr Leu Arg Ala Asp Phe Ala Asn Gln Asn Ile 165 170 175 Gln Cys Glu Leu Leu Thr Leu Ala Asp Leu Glu Arg Gly Gly Gln His 180 185 190 Thr Val Ile Val Lys Pro Phe Ile Pro Gln Asn Asn Ala Asn His Leu 195 200 205 Ala Thr Leu Val Tyr Thr Ser Gly Ser Thr Gly Leu Pro Lys Gly Ala 210 215 220 Met Ile Thr Glu Gln Ser Trp Arg Glu Leu Trp Thr Lys Thr Gly Phe 225 230 235 240 Tyr Lys His Thr Pro Asp Ile Pro Leu Ile Val Phe Asn Phe Met Pro 245 250 255 Leu Ser His Met Phe Gly Arg Met Ile Val Ile Asn Ser Leu Met Gln 260 265 270 Gly Gly Thr Thr Tyr Phe Ala Ser Lys Ser Asp Met Ser Thr Phe Phe 275 280 285 Glu Glu Ile Arg Leu Val Arg Pro Thr Val Leu Tyr Leu Val Pro Arg 290 295 300 Val Ser Glu Leu Ile Tyr Gln Asn Ile Gln Ile Ala Val Asn Asn Arg 305 310 315 320 Leu Gln Ala Ser Asn Pro Ser Pro Arg Thr Glu Ile Glu Asn Glu Ile 325 330 335 Leu Ser Glu Met Lys Asn Thr Ile Leu Gly Asp Arg Leu Ser Ile Ala 340 345 350 Ile Thr Ala Ser Ala Pro Thr Pro Pro Glu Ile Met Tyr Phe Leu Lys 355 360 365 Arg Leu Phe Asp Val Pro Val Ile Asp Val Tyr Gly Ser Thr Glu Leu 370 375 380 Gly Ile Ile Leu Ile Asn Asn Gln Thr Ser Pro Gln Asn Val Ile Ala 385 390 395 400 Tyr Lys Leu Val Ser Arg Pro Glu Leu Asp Phe Phe Thr Thr Asp Lys 405 410 415 Pro Tyr Pro Arg Gly Glu Leu Tyr Met Lys Thr His Arg Ala Val Ile 420 425 430 Gly Tyr Tyr Gln Asn Pro Asp Ala Thr Ala Asp Leu Phe Asp Ala Glu 435 440 445 Gly Tyr Leu Lys Thr Gly Asp Val Val Glu Glu Arg Ala Pro Asn Asn 450 455 460 Leu Phe Leu Ile Asp Arg Ile Asn Asn Ile Ile Lys Leu Gly Asn Gly 465 470 475 480 Glu Phe Val Ser Leu Leu Arg Leu Glu Gln Ile Phe Leu Gly Gly Ser 485 490 495 Arg Leu Ile Lys Gln Leu Phe Leu Tyr Gly Ser Ser Leu Arg Ser Tyr 500 505 510 Leu Leu Ala Val Leu Val Pro Asp Ile Ser Leu Leu Lys Glu Lys Leu 515 520 525 Ile Glu Leu Gly Leu Pro Glu Asn Pro Val Gln Met Lys Lys Ile Leu 530 535 540 Leu Gln Glu Ile His Ala Ile Ala Lys Leu Glu Gln Ile Arg Ser Tyr 545 550 555 560 Glu Val Pro Leu Asp Phe Ile Met Glu Leu Glu Pro Phe Ser Gln Glu 565 570 575 Asn Gln Leu Ile Thr Glu Ser Asn Lys Leu Ala Arg Asn Asn Leu Lys 580 585 590 Lys Lys Tyr Gly His Ser Leu Glu Glu Leu Tyr Glu His Ile Glu Lys 595 600 605 Asn Gln Leu Ala Asp Leu Ile Asn Leu Gly Asn Ser Asp Ser Ser Ile 610 615 620 Glu Asn Leu Val Cys Val Val Leu Gly Ser Gln Asn Ile Glu Trp Gly 625 630 635 640 Asn Ser Ser Phe Ile Asp Leu Gly Gly Asp Ser Leu Asp Ala Val Arg 645 650 655 Leu Met Asn Thr Ile Lys Asp Ile Tyr Ser Val Ser Val Pro Val Ser 660 665 670 Leu Ile Leu Asn Pro Ala Tyr Ser Ile Lys Asn Leu Ile Asn Asn Val 675 680 685 Asn Glu Lys Arg His Gly Lys Thr Glu Arg Cys Arg Thr His Ala Ile 690 695 700 Ile Phe Ser Asp Ile His Pro Ile Asn Ala Ser Lys Ser Glu Lys Met 705 710 715 720 Lys Leu Phe Ala Ser Asp Leu His Leu Ser Ala Phe Phe Ser Ser His 725 730 735 Glu Met Glu Gln Ala Lys Lys Leu Pro Lys Arg Asp Lys Ser Leu Pro 740 745 750 Val Ser Asn Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe 755 760 765 Leu Ala Leu Ala Leu Leu Glu Lys Leu Ser Leu Asn Gln Gly Lys Leu 770 775 780 Ile Cys Phe Val Arg Ala His Asn Asn Thr His Ala Arg Lys Arg Met 785 790 795 800 Phe Glu Ser Phe Gln His Ser Glu Phe Ala Leu Arg Glu Arg Phe Ile 805 810 815 Gln Leu Ala Gln Asn His Leu Val Val Tyr Ala Ala Asp Leu Thr Ala 820 825 830 Pro Asn Phe Gly Leu Ser Asp Asp Val Tyr Asp Thr Leu Ala Thr Glu 835 840 845 Val Asp Leu Val Leu His Asn Gly Ala Leu Val Asn His Ala Leu Ser 850 855 860 Tyr Glu Gln Leu Phe Glu Pro Asn Val Leu Gly Thr Val Glu Val Ile 865 870 875 880 Arg Phe Ala Leu Gln Asn Lys Leu Lys Pro Ile His Phe Val Ser Ser 885 890 895 Val Ala Val Thr Lys Gly Leu Tyr His Arg Ser Ile Ile Leu Glu Thr 900 905 910 Glu Asp Ile Arg Lys Gln Trp Pro Met Arg Tyr Asn Lys Thr Gly Tyr 915 920 925 Ala Glu Gly Tyr Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Lys 930 935 940 Asn Phe Ser Glu Ala Phe Asp Leu Pro Val His Val Phe Arg Cys Gly 945 950 955 960 Met Ile Leu Ala His Ser Thr Tyr Leu Gly Glu Ile Asn Ala Asp Asp 965 970 975 Phe Phe Thr Arg Leu Met Ala Gly Ile Ile Asn Thr Gly Ile Ala Pro 980 985 990 Lys Thr Phe Tyr Glu Val Thr His Glu Thr Asp Phe Lys Pro Cys Phe 995 1000 1005 Asp Gly Leu Pro Val Asp Phe Ile Ala Asp Thr Ile Ala Asp Asp 1010 1015 1020 Ala Leu Val Phe Gly Thr Asp Tyr Ala Thr Tyr Cys Val Ile Asn 1025 1030 1035 Pro Thr Gly Asn Arg Ser Ile Asn Leu Asp Val Ile Ile Asn Trp 1040 1045 1050 Val Ile Glu Phe Gly Tyr Lys Ile Asp Gln Leu Glu Phe Tyr Glu 1055 1060 1065 Glu Trp Tyr Arg Glu Phe Leu Thr Arg Leu Lys Gln Leu Ser Gly 1070 1075 1080 Ile Gln Lys Arg His Ser Pro Leu Pro Ile Ile His Lys Trp Glu 1085 1090 1095 His Pro Ala Glu Ile Gly His Glu Ser Lys Leu Asp Asn Ser Gln 1100 1105 1110 Phe Tyr Lys Met Ile Lys Lys His Val Asp Ser Asn Val Pro Ile 1115 1120 1125 Ile Asn Gln Ala Phe Ile Tyr Lys Cys Leu Ile Asp Met Ala Met 1130 1135 1140 Leu Lys Ile Ile Gly Leu Pro Gln Ala Ile Gln Ser 1145 1150 1155 <210> 208 <211> 1153 <212> PRT <213> Artificial Sequence <220> <223> Pseudomonas sp. 43NM1 <400> 208 Met Ser Leu Ala Lys Ile Val Ala Asp Thr Met Ser Lys Tyr Ala Asp 1 5 10 15 Arg Pro Ala Ile Gly Glu Arg Asp Lys Ile Phe Ile Thr Asp Asp Ser 20 25 30 Ser Gln Glu Val Ser Leu Lys Leu Leu Pro Ser Tyr Gly Thr Ile Thr 35 40 45 Tyr Gly Glu Leu Trp Lys Arg Thr Gly Ala Leu Ala Ala Glu Leu His 50 55 60 His Ser Thr Asn Ala Pro Leu Thr Ala Gly Ser Ser Val Ala Phe Leu 65 70 75 80 Ala Phe Thr Ser Gly Asp Tyr Ala Ile Leu Asp Leu Ala Cys Ile Arg 85 90 95 Leu Gly Ala Ile Val Val Pro Leu Gln Thr Gly Ser Ser Gln Ala Gln 100 105 110 Ile Asp Ser Ile Leu Gln Glu Thr Glu Pro Leu Val Phe Ala Thr Ser 115 120 125 Ile Asp Tyr Leu Asp Ile Ala Val Glu Val Ala Ile Lys Thr Pro Ser 130 135 140 Ile Arg Arg Ile Leu Leu Leu Asp Tyr Tyr Ser Gln Ile Ser Glu His 145 150 155 160 Ser Lys Lys Leu Asn Ala Val Leu Ser Gln Leu Asp Ser Asn Ser Ser 165 170 175 Val Ile Ser Ile Glu Pro Leu Gln Asp Leu Ile Lys Arg Gly Thr Ala 180 185 190 Leu Ser Glu Pro Pro Met Tyr Ser Ser Ser Thr Ser Asp Glu Glu Leu 195 200 205 Ser Met Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 210 215 220 Met Tyr Thr Gln Lys Leu Ala Ser Gly Met Trp Gly Gly Ser Trp Ala 225 230 235 240 Thr Ile Phe Ser Glu Glu Arg Ala Ile Thr Phe His Tyr Met Pro Met 245 250 255 Ser His Val Ala Gly His Ser Ser Leu Lys Ser Thr Leu Ala Arg Gly 260 265 270 Gly Thr Cys Tyr Phe Thr Ala Lys Ser Asn Leu Ser Thr Leu Leu Glu 275 280 285 Asp Ile Ser Leu Ser Lys Pro Thr Glu Leu Ser Leu Val Pro Arg Ile 290 295 300 Cys Glu Met Ile Tyr Gln Lys Tyr Gln Thr Glu Leu Ala Arg Lys Arg 305 310 315 320 Ala Ser His Gly Asp Asp Thr Ser Leu Thr Ile Leu Glu Asp Ile Arg 325 330 335 Val Asn Ile Leu Gly Gly Gln Val Gly Trp Ala Ser Cys Ser Ser Ala 340 345 350 Pro Leu Ser Asn Glu Leu Lys Ile Phe Thr Glu Ser Leu Leu Asn Ile 355 360 365 Pro Leu His Asn Val Tyr Gly Ser Thr Glu Ala Gly Ala Ile Trp Ile 370 375 380 Asp Asn Glu Leu Leu Ser Pro Pro Val Glu Asp Tyr Arg Ile Ile Asp 385 390 395 400 Val Pro Glu Leu Gly Tyr Tyr Gly Thr Asp Ser Pro Phe Pro Arg Gly 405 410 415 Glu Leu Leu Leu Lys Thr Gln Ser Ile Ile Pro Gly Tyr Tyr Lys Arg 420 425 430 Pro Glu Leu Ala Ser Glu Leu Phe Asp Glu His Gly Tyr Tyr Lys Thr 435 440 445 Gly Asp Ile Val Ala Glu Thr Gly His Asn Arg Leu Val Tyr Val Asp 450 455 460 Arg Arg Lys Asn Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Thr 465 470 475 480 Ala Lys Leu Glu Thr Ile Phe Ser Ala Ile Pro Glu Ile Gln Ser Ile 485 490 495 Phe Val Tyr Gly Lys Ser Glu Trp Ser Tyr Leu Leu Ala Val Val Val 500 505 510 Pro Ser Lys His Leu Ala Gln Arg Phe Asp Gly Lys Ala Glu Leu Ile 515 520 525 Lys Gln Phe Ile Gly Asp Ala Ile Arg Lys Val Ala Lys Thr Ser Glu 530 535 540 Leu Arg Ser Tyr Glu Ile Pro Arg Asp Leu Leu Ile Asp Asn Glu Pro 545 550 555 560 Phe Thr Gln Thr Asn Gly Leu Leu Ser Asp His Gly Lys Pro Leu Trp 565 570 575 Pro Lys Leu Arg Glu Lys Tyr Ala Ser Gln Leu Glu Glu Leu Asn Ile 580 585 590 Gln Leu Val Ser Lys Glu Leu Asn Glu Leu His Asp Ile His Glu Arg 595 600 605 Ile Asn Gln Gln Thr Val Leu Glu Thr Leu Lys Gln Ala Val Arg Ser 610 615 620 Leu Val Gly Gly Ala Thr Glu Glu Ile Ser Ser His Ala Gln Phe Arg 625 630 635 640 Glu Leu Gly Gly Asp Ser Leu Ser Ala Val Ser Leu Ala Ser Ile Leu 645 650 655 Ser Asp Ala Tyr Gly Ile Thr Ile Pro Val Asp Met Leu Ile Ser Pro 660 665 670 Ala Tyr Asp Leu Gln His Val Ser Asp Tyr Ile Glu Lys Thr Leu His 675 680 685 Ser Gly Gln Ile Arg Pro Ser Ala Ala Ser Ile His Gly Ala Lys Pro 690 695 700 Asn Val Phe Asn Ala Lys Asp Leu Ser Leu Gln Lys Phe Ile Ser Pro 705 710 715 720 Asp Ile Leu Glu Lys Ala Gln Gly Leu Lys Pro Ser Ser Asn Ser Ala 725 730 735 Arg Thr Ile Leu Leu Thr Gly Ser Thr Gly Tyr Leu Gly Arg Phe Leu 740 745 750 Cys Leu Gln Leu Leu Glu Glu Phe Gly Glu Thr Gly Gly Lys Leu Ile 755 760 765 Cys Val Val Arg Gly Lys Asn Val Ala Leu Ala Thr Lys Arg Leu Tyr 770 775 780 Glu Ser Phe Gly Ser Ala Asn Ser Gln Val Ser Arg Lys Leu Arg Ser 785 790 795 800 Leu Ser Thr Leu His Leu Glu Val Leu Ala Gly Asp Ile Gly Glu Pro 805 810 815 Lys Leu Gly Leu Asp Pro Glu Thr Trp Asp Lys Leu Gly Lys Glu Val 820 825 830 Asp Thr Ile Val His Ala Gly Ala Leu Val Asn His Val Leu Pro Tyr 835 840 845 Ser Asn Leu Phe Asp Ala Asn Val Thr Gly Thr Ala Glu Ile Ile Ser 850 855 860 Leu Ala Leu Ser Asn His Leu Lys Pro Val Val Phe Leu Ser Ser Ile 865 870 875 880 Ala Val Ala Ser Leu Val Asn Thr Glu Thr Thr Leu Asp Glu Asp Ala 885 890 895 Asp Ile Arg Ile Ala Ala Ala Glu Ile Glu Ala Glu Asp Thr Tyr Ala 900 905 910 Ala Gly Tyr Ala Leu Ser Lys Trp Ala Ser Glu Val Leu Leu Arg Glu 915 920 925 Ala His Ser His Tyr Gly Leu Pro Val Thr Thr Phe Arg Ser Ser Met 930 935 940 Ile Leu Ala His Ser Gln Tyr Pro Gly Gln Leu Asn Val Pro Asp Met 945 950 955 960 Phe Thr Arg Leu Leu Leu Ser Val Ala Leu Thr Gly Ile Ala Pro Pro 965 970 975 Ser Phe Tyr Arg Ala Thr Asn Asn Val Gly Leu Pro His Tyr Asp Gly 980 985 990 Leu Pro Val Asp Phe Thr Ala Ser Ala Ile Leu Lys Ile Gly Val Lys 995 1000 1005 Gln His Thr Glu Ser Tyr Arg Ser Phe Asn Leu Val Asn Pro His 1010 1015 1020 Asp Asp Gly Ile Ser Leu Asp Thr Phe Val Gly Trp Met Thr Asp 1025 1030 1035 His Gly Val Asn Ile Arg Lys Ile Ala Asp Tyr Ala Asp Trp Tyr 1040 1045 1050 Asn Arg Leu Glu Thr Ala Leu Leu Gly Leu Pro Glu Arg Leu Lys 1055 1060 1065 Gln His Ser Ile Leu Pro Leu Met His Gly Phe Ser Glu Pro Ala 1070 1075 1080 Glu Val Ile Ser Gly Ser Thr Ile Pro Ser Asn Arg Phe Gln Glu 1085 1090 1095 Ala Val Glu Thr Phe Asp Ser Gly Ser Gly Ala Phe Ala Ile Pro 1100 1105 1110 His Ile Ser Glu Ser Leu Ile Arg Lys Tyr Val Thr Asp Leu Gln 1115 1120 1125 Ser Leu Gly Leu Leu Gly Asp Leu His Lys Arg Leu Asn Arg Thr 1130 1135 1140 Ser Ser Ala Ala Ile Pro Glu Leu Gln Leu 1145 1150 <210> 209 <211> 1162 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. EPG1 <400> 209 Met Ser Thr Asp Thr Gln Arg Phe Glu Arg Arg Ile Ala Asp Leu Leu 1 5 10 15 Ala His Asp Thr Gln Phe Ala Ala Ala Ala Pro Ser Pro Ala Val Thr 20 25 30 Ala Ala Ile Glu Ala Pro Gly Ile Arg Leu Pro Asp Val Ile Gln Thr 35 40 45 Val Leu Asp Gly Tyr Ala Asp Arg Pro Ala Leu Ala Gln Arg Ala Val 50 55 60 Arg Tyr Thr Thr Asp Pro His Asp Gly Arg Thr Thr Thr Glu Leu Leu 65 70 75 80 Pro Glu Phe Asp Thr Met Thr Tyr Gly Glu Leu Ser Arg Arg Val His 85 90 95 Ala Val Ala Asp Ala Leu Thr Glu Val Ser Pro Gly Asp Arg Val Ala 100 105 110 Val Leu Gly Phe Thr Ser Val Asp Tyr Ala Val Ile Asp Ile Ala Leu 115 120 125 Pro Val Arg Gly Ala Val Ala Val Pro Leu Gln Thr Ala Ala Pro Val 130 135 140 Ala Ser Leu Lys Pro Ile Ile Ala Glu Thr Glu Pro Val Val Ile Phe 145 150 155 160 Ser Ala Val Asp Tyr Leu Asp Asp Ala Val Glu Leu Ala Leu Gly Ala 165 170 175 Pro Trp Val Arg Arg Leu Val Val Phe Asp Leu Leu Ser Arg Val Asp 180 185 190 Ala His Arg Glu Arg Val Asp Ala Ala Lys Arg Arg Leu Gln Asp Ala 195 200 205 Gly Ser Pro Ile Ser Val Val Thr Leu Ala Glu Leu Ile Asp Ser Ala 210 215 220 Pro Ala Glu Pro Ala Gly Pro Pro His Val Ser Pro Gly Pro Asp Pro 225 230 235 240 Leu Ser Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly 245 250 255 Ala Met Tyr Thr Glu Arg Leu Val Ala Asn Ala Trp Arg Pro Ser Asn 260 265 270 Arg Met Asn Trp Gly Glu Arg Gly Ser His Pro Ser Ile Thr Leu Asn 275 280 285 Phe Met Pro Met Ser His Val Met Gly Arg Met Leu Leu Tyr Gly Thr 290 295 300 Leu Gly Ser Gly Gly Thr Ala Tyr Phe Ala Ala Arg Ser Asp Leu Ser 305 310 315 320 Thr Phe Leu Glu Asp Leu Ala Leu Val Arg Pro Thr Gln Leu Ser Phe 325 330 335 Val Pro Arg Ile Trp Asp Thr Ile Val Ala Glu Val Thr Lys Glu Leu 340 345 350 Asp Arg Arg Pro Gly Glu Arg Glu Ala Val Phe Ala Glu Leu Arg His 355 360 365 Arg Met Leu Gly Gly Arg Tyr Leu Leu Ala Met Thr Gly Ser Ala Pro 370 375 380 Leu Ser Pro Glu Leu Arg Ala Phe Val Glu Glu Phe Leu Asp Leu His 385 390 395 400 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Ala Val Phe Val Asp 405 410 415 Gly Gln Val Gln Arg Pro Pro Val Leu Asp Tyr Lys Leu Val Asp Val 420 425 430 Pro Asp Leu Gly Tyr Phe Arg Thr Asp Arg Pro His Pro Arg Gly Glu 435 440 445 Leu Leu Val Lys Ser Asp Thr Leu Phe Pro Gly Tyr Tyr Lys Arg Pro 450 455 460 Glu Ile Thr Ala Glu Met Phe Asp Glu Asp Gly Tyr Tyr Arg Thr Gly 465 470 475 480 Asp Val Val Ala Glu Leu Ala Pro Asp Gln Leu Ala Tyr Leu Asp Arg 485 490 495 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Thr Val Ser 500 505 510 Lys Leu Glu Ala Val Phe Gly Asp Ser Pro Val Ile Arg Gln Ile Tyr 515 520 525 Leu Tyr Gly Asn Ser Ala Arg Ser Tyr Leu Leu Ala Val Val Val Pro 530 535 540 Thr Glu Ala Ala Leu Ala Gly Glu Asp Val Lys Ser Val Val Ala Glu 545 550 555 560 Ser Leu Gln Glu Ile Ala Lys Ala Ala Asp Leu Gln Ser Tyr Glu Ile 565 570 575 Pro Arg Asp Phe Leu Ile Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly 580 585 590 Leu Leu Thr Gly Ile Arg Lys Leu Ala Arg Pro Arg Leu Lys Asp His 595 600 605 Tyr Gly Ala Arg Leu Glu Ala Leu Tyr Ser Glu Leu Ala Asp Gly Gln 610 615 620 Glu Asp Glu Leu Arg Ala Leu Arg Arg Asp Gly Ala Arg Arg Pro Thr 625 630 635 640 Leu Glu Thr Val Ser Arg Ala Ala Ala Ala Leu Leu Gly Thr Ala Ala 645 650 655 Gly Asp Leu Arg Ser Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser 660 665 670 Leu Ser Ala Leu Thr Tyr Ala Asn Leu Leu His Asp Ile Phe Asp Val 675 680 685 Asp Val Pro Val Gly Val Ile Val Ser Pro Ala Thr Asp Leu Ala Ala 690 695 700 Val Ala Ser Phe Ile Asp Thr Glu Arg Glu Asn Ser Ser Gly Arg Ala 705 710 715 720 Thr Phe Ala Ser Val His Gly Arg Asp Ala Ser Glu Val His Ala Arg 725 730 735 Asp Leu Thr Leu Asp Lys Phe Leu Asp Ala Thr Thr Leu Ala Gln Ala 740 745 750 Pro Gly Ile Pro Gly Pro Arg Pro Glu Val Arg Thr Val Leu Leu Thr 755 760 765 Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Gln 770 775 780 Arg Leu Ala Leu Val Gly Gly Thr Leu Ile Cys Leu Val Arg Ala Lys 785 790 795 800 Asp Asp Ala Ala Ala Arg Asp Arg Leu Asp Arg Thr Phe Asp Ser Gly 805 810 815 Asp Pro Ala Leu Thr Glu His Tyr Arg Arg Leu Ala Ala Asp His Leu 820 825 830 Gln Val Ile Ala Gly Asp Lys Gly Glu Pro Asp Leu Gly Leu Asp Arg 835 840 845 Asp Thr Trp Gln Arg Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro 850 855 860 Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro 865 870 875 880 Asn Ala Val Gly Thr Ala Glu Leu Ile Arg Val Ala Leu Thr Thr Arg 885 890 895 Gln Lys Pro Tyr Val Tyr Val Ser Thr Ile Gly Val Gly Ala Gly Val 900 905 910 Ala Pro Asp Arg Phe Thr Glu Asp Gly Asp Ile Arg Glu Ile Ser Pro 915 920 925 Thr Arg Gln Val Asp Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys 930 935 940 Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu 945 950 955 960 Pro Val Ala Val Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Ser Tyr 965 970 975 Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg Leu Ile Leu Ser 980 985 990 Leu Val Ala Thr Gly Val Ala Pro Asp Ser Phe Tyr Gln Leu Asp Pro 995 1000 1005 Ala Gly His Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Val Glu 1010 1015 1020 Phe Ile Ala Glu Ala Ile Ser Thr Leu Gly Ala Asp Val Ala Asp 1025 1030 1035 Asp Ser Pro Thr Gly Phe Glu Thr Tyr His Val Met Asn Pro Tyr 1040 1045 1050 Asp Asp Gly Ile Gly Leu Asp Glu Tyr Val Asp Trp Leu Ile Asp 1055 1060 1065 Ser Gly Tyr Pro Val His Arg Val Gly Asp Tyr Asp Thr Trp Leu 1070 1075 1080 Gln Arg Phe Thr Ala Ala Ile Asn Ala Leu Pro Glu Arg Gln Arg 1085 1090 1095 Gln Ala Ser Leu Leu Pro Leu Leu His Asn Tyr Gln His Pro Glu 1100 1105 1110 Thr Pro Leu Arg Gly Ser Leu Ala Pro Thr Glu His Phe Arg Lys 1115 1120 1125 Ala Val Gln Asp Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro His 1130 1135 1140 Val Thr Arg Gln Ile Ile Val Lys Tyr Val Thr Asp Leu Glu Leu 1145 1150 1155 Leu Gly Ile Leu 1160 <210> 210 <211> 1152 <212> PRT <213> Artificial Sequence <220> <223> Aphanothece cf. minutissima CCALA 015 <400> 210 Met Cys Ser Glu Thr Ser Ser Ser Ser Arg Leu Pro Thr Ser Cys Pro 1 5 10 15 Val Pro Phe Pro Val Thr Thr Ser Ala Gly Pro Ala Ser Thr Pro Ser 20 25 30 Ser Cys Pro Arg Thr Phe Arg Ser Ser Arg Ser Thr Arg His Arg Pro 35 40 45 Asp Ala Ile Val Val Val Ser Glu Ser Ser Ala Val Pro Pro Ser Ser 50 55 60 Leu Ala Tyr Gly Ala Leu Ile Asp Phe Phe Leu Ala Ala His Pro Glu 65 70 75 80 Arg Pro Ala Leu Ala Glu Arg Ala Tyr Thr Val Glu Ala Asp Pro Ala 85 90 95 Ser Gly Ala Thr His Arg Arg Thr Leu Ala Glu Phe Arg Pro Ile Thr 100 105 110 Tyr Arg Thr Leu Arg Asp Arg Val Arg Ser Leu Ala Ser Ala Trp His 115 120 125 Ala Asp Pro Ala Ala Ala Ile Arg Arg Gly Glu Arg Val Ala Ile Leu 130 135 140 Gly Phe Ala Ser Ile Glu Tyr Ala Val Ile Asp Leu Ala Leu Ala Tyr 145 150 155 160 Val Gly Ala Val Pro Met Pro Leu Ser Gly His His Ser Ala Pro Glu 165 170 175 Tyr Asp Ala Ile Leu Glu Arg Ala Thr Pro Ala Ala Leu Ala Val Ser 180 185 190 Ile Ala Gln Leu Pro Ala Met Val Asp Leu Val Arg Arg His Gly Cys 195 200 205 Leu Arg Gln Leu Ile Val Phe Asp Ala Asp Thr Arg Ile Thr Ala Glu 210 215 220 Arg Thr Leu Leu Glu Glu Ala Lys Ala Thr Leu Arg Ala Ala Gly Ser 225 230 235 240 Thr Val Pro Leu Leu Leu Leu Pro Asp Leu Leu Arg Arg Gly Glu Gly 245 250 255 Leu Asp Val Pro Pro Pro Ala Ala Val Asp Pro Glu Ala Met Ala Leu 260 265 270 Leu Ile His Thr Ser Gly Ser Thr Gly Leu Pro Lys Gly Ala Cys Ile 275 280 285 Ser Ala Ala Ala Leu Ser Asn Thr Trp Arg Gln Val Thr Gly Pro Asp 290 295 300 Pro Lys Val Ala Val Val Leu Ala Pro Phe His His Met Met Gly Arg 305 310 315 320 Asp Ser Met Val Thr Ala Leu Asn Cys Gly Gly Leu Ala Cys Phe Thr 325 330 335 Leu Lys Pro Asp Leu Ser Thr Val Phe Glu Asp Ile Arg Leu Ala Arg 340 345 350 Pro Thr Gly Leu Val Leu Phe Pro Arg Leu Cys Glu Trp Ile Asp Gln 355 360 365 His Val Arg Ser Thr Lys Ser Gly Asp Leu Arg Phe Phe Leu Gly Asp 370 375 380 Arg Leu Glu Ser Ile Val Val Ala Ser Ala Pro Ile Ala Pro Arg Ile 385 390 395 400 Arg Ala Leu Leu Glu Asp Thr Phe Gly Val Pro Val His Glu Gly Tyr 405 410 415 Ser Ser Thr Glu Thr Ala Ser Gly Gly Leu Ala Met Asn Gly Arg Leu 420 425 430 Asn Arg Ser Asn Val Leu Asp Tyr Arg Leu Arg Asp Val Pro Glu Ser 435 440 445 Gly Tyr Phe Arg Ser Asp Arg Pro Tyr Pro Arg Gly Glu Leu Cys Val 450 455 460 Lys Thr Arg Phe Gly Ile Arg Ala Tyr Phe Arg Asn Pro Glu Ala Thr 465 470 475 480 Ala Ala Leu Phe Asp Ala Asp Gly Phe Ser Cys Thr Gly Asp Val Val 485 490 495 Glu Glu Arg Gly Pro Gly Gln Ile Ala Ile Ile Asp Arg Arg Arg Asn 500 505 510 Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Val Gly Ala Leu Glu 515 520 525 Gln Leu Phe Ala Asp Gly Cys Ala Ser Val Ala Gln Ile His Val His 530 535 540 Gly Glu Ser Ser Arg Ser Tyr Leu Leu Ala Val Val Val Pro Asp Arg 545 550 555 560 Glu Ala Leu Ala Arg Arg Pro Arg Pro Pro Gly Ser Asp Ala Ala Leu 565 570 575 Val Ala Leu Val Arg Glu Glu Met Val Gln Leu Ala Gly Glu Gln Gly 580 585 590 Leu Lys Ser Phe Glu Ile Pro Arg Ala Val Leu Leu Ala Glu Glu Pro 595 600 605 Phe Ser His Ala Asn Gly Leu Leu Ser Ser Leu Gly Lys Pro Ile Arg 610 615 620 Pro Ala Ile Arg Gln Arg Tyr Gln Glu Ala Leu Ala Ala Leu Tyr Asp 625 630 635 640 Ser His Asp Arg Leu Gly Asp Ala Ala Leu Ala Thr Leu Arg Gln Pro 645 650 655 Gly Ala Gly Leu Ser Leu Glu Gln Arg Leu Arg Leu Leu Leu His Ser 660 665 670 Thr Leu Gly Val His Asp Asp Gly Ala Leu Glu Gly His Cys Phe Arg 675 680 685 Asp Leu Gly Gly Asp Ser Leu Gly Ala Val Gln Leu Ser Val Arg Ile 690 695 700 Glu Ala Glu Phe Gly Val Ala Ile Glu Ala Ser Gln Ile Leu Gly Pro 705 710 715 720 Asp Gly Thr Ile Ala Ala Trp Ala Arg Ile Leu Arg Ala Ser Gly Ser 725 730 735 Gly Pro Gly Gln Glu His Ala Ala Gly Asp Phe Ala Thr Ser Asp Arg 740 745 750 Val Ala Ser Asp Leu Ala Thr Ser Glu Leu Ala Ala Glu Asp Phe Arg 755 760 765 Val Glu Ala Phe Ile Asp Gly Ala Thr Leu Asp Ala Ala Ala Val Leu 770 775 780 Pro Ala Ala Pro Trp Pro Ala Arg Ser Val Leu Leu Thr Gly Ala Asn 785 790 795 800 Gly Phe Leu Gly Gly Arg Leu Ala Leu Ala Trp Leu Glu Arg Leu Ala 805 810 815 Arg Thr Gly Gly Arg Leu Val Cys Leu Val Arg Pro Ser His Thr Arg 820 825 830 Ser Ala Arg Glu Arg Leu Glu Ala Arg Phe Ala His Leu Asp Pro Thr 835 840 845 Thr Ala Ala Arg Trp Arg Thr Leu Ala Ala Asp His Leu Glu Val Val 850 855 860 Ala Gly Asp Ile Ser Ala Pro Arg Leu Gly Leu Asp Ala Ala Thr Tyr 865 870 875 880 Asp Arg Leu Ala His Gly Ile Glu Ala Ile Gly His Cys Ala Ala Leu 885 890 895 Val Asn His Arg Leu Glu Tyr Arg His Leu Arg Arg Pro Asn Val Ile 900 905 910 Gly Thr Ala Glu Ile Val Arg Leu Ala Leu Thr His Arg Arg Lys Pro 915 920 925 Ile Asp Leu Ile Ser Thr Ile Gly Val Ala Pro Leu Gly Glu Arg Leu 930 935 940 Arg Leu Asp Gly Ser Tyr Ala Asn Gly Tyr Phe Ala Ser Lys Trp Ala 945 950 955 960 Cys Glu Gln Leu Leu Arg Ser Thr His Ala Thr Thr Ala Leu Pro Ile 965 970 975 Arg Ile Leu Arg Ser Gly Leu Val Leu Pro Asp Arg Gln Leu Ala Gly 980 985 990 Glu Arg Asn Pro Asp Asp Ile Leu Ser Arg Leu Ile His Ser Leu Leu 995 1000 1005 Leu Thr Gly Leu Ala Pro Pro Gly Phe Ser Ser Asn Glu Ala Gly 1010 1015 1020 Gly Glu Ser Val Gly Phe His Ala Ser Gly Leu Pro Val Asp Gln 1025 1030 1035 Leu Ala Gln Ala Ile Val Ala Leu Gly Asp Val Ala Pro Glu Gly 1040 1045 1050 Phe His Leu Leu Thr Leu Gly Gly Pro Ala Asp Gly Trp Phe Pro 1055 1060 1065 Leu Glu Ala Leu Val Glu Arg Ile Glu Ala Ser Gly Phe Pro Leu 1070 1075 1080 Gln Arg Thr Ala Ser Tyr Ala Glu Trp Leu Glu Arg Ile Glu Pro 1085 1090 1095 Ala Leu Arg Arg Leu Pro Ala Glu Gln Arg Ala Leu Ser Leu Leu 1100 1105 1110 Asp Val Leu Glu Ala Tyr Arg Pro Val Arg Arg Pro Gly Ala Glu 1115 1120 1125 Thr Cys Ala Gly Phe Pro Val Ala Tyr Leu Asp Lys Val Cys Ser 1130 1135 1140 Glu Ala Val Ala Ala Ala Gly His Gly 1145 1150 <210> 211 <211> 1154 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. AG1013 <400> 211 Met Pro Asn Asp Pro Arg Ala Ile Leu Glu Gln Arg Ile Ala Ala Leu 1 5 10 15 Ala Ile Ala Asp Pro Gln Val Arg Ala Ala Met Pro Ser Gln Glu Val 20 25 30 Val Ser Ala Leu Gly Gln Pro Asp Leu Ser Pro Ala Gln Ile Ala Glu 35 40 45 Ile Val Leu Ala Ala Tyr Ala Asp Arg Pro Ala Leu Ala His Arg Val 50 55 60 Gly Glu Ile Thr Thr Asp Pro Arg Thr Gly Arg Arg Thr Arg Arg Leu 65 70 75 80 Leu Pro Gln Phe Val Ala Leu Ser Tyr Ala Glu Val Ala Ala Arg Val 85 90 95 Asp Ala Val Ala Ala Ala Cys Arg Ala Thr Ala Pro Leu Ala Val Ala 100 105 110 Pro Gly Asp Val Val Cys Ile Val Gly Ser Pro Gly Ile Asp Phe Thr 115 120 125 Thr Leu Asp Leu Ala Cys Ala Arg Val Gly Ala Thr Val Val Pro Leu 130 135 140 His Ser Asp Val Ser Ser Asp Leu Leu Ala Ala Ile Val Thr Glu Thr 145 150 155 160 Glu Pro Thr Met Leu Ala Val Ala Thr Asp Glu Leu Cys Val Ala Val 165 170 175 Glu Ser Leu Arg His Ser Pro Ala Pro Arg His Leu Ile Cys Phe Asp 180 185 190 Tyr His Ala Glu Asp Asp Asp His Arg Asp Ala Ile Asp Ala Ala Arg 195 200 205 Ser Thr Phe Ala Ala Cys Gly Ile Asn Val Val Ile Glu Thr Leu Pro 210 215 220 Glu Leu Leu Asp Arg Gly Ala Leu Leu Pro Pro Pro Pro Pro Val Ala 225 230 235 240 Val Ser Leu Asp Ala Thr Ala Ile Leu Leu Tyr Thr Ser Gly Ser Thr 245 250 255 Gly Ala Pro Lys Gly Val Ile Tyr Thr Ala Lys Thr Ala Ala Ala Met 260 265 270 Trp Ala Ala Lys Gly Glu Ile Pro Ser Leu Thr Val His Phe Met Pro 275 280 285 Leu Ser His Leu Ala Gly Arg Asn Ala Leu Phe Ser Thr Leu Ala Glu 290 295 300 Gly Gly Thr Val His Phe Thr Gly Gln Ser Asp Met Ser Thr Leu Leu 305 310 315 320 Glu Asp Ile Ala Leu Val Arg Pro Thr Arg Leu Arg Leu Val Pro Arg 325 330 335 Val Cys Glu Thr Leu His Gln Arg Tyr His Gly Asp Val Thr Arg Arg 340 345 350 Ile Ala Glu Gly Ser Lys Arg Ala Asp Ala Glu Ala Asn Ala Arg Val 355 360 365 Val Phe Arg Arg Glu Leu Leu Gly Gly Arg Val Val Trp Ala Leu Cys 370 375 380 Gly Thr Ala Pro Leu Pro Thr Glu Leu Arg Glu Phe Val Glu Ser Val 385 390 395 400 Leu Glu Leu Lys Leu His Asp Ala Tyr Gly Ser Thr Glu Ala Gly Ala 405 410 415 Ile Leu Ala Asp Gly Arg Leu Met Arg Pro Pro Ile Leu Asp Tyr Lys 420 425 430 Leu Ala Asp Val Pro Glu Leu Gly Tyr Phe Cys Thr Asp Gln Pro Tyr 435 440 445 Pro Arg Gly Glu Leu Leu Leu Arg Ser Gln Thr Leu Thr Thr Gly Tyr 450 455 460 Phe Arg Arg Pro Glu Ala Thr Ala Ala Ala Phe Asp Glu Glu Gly Tyr 465 470 475 480 Tyr Arg Thr Gly Asp Ile Val Ala Glu Ile Glu Thr Asp Arg Leu Gln 485 490 495 Leu Ile Asp Arg Arg Ser Ser Ile Leu Lys Leu Ala His Gly Glu Phe 500 505 510 Val Ala Val Ser Arg Leu Glu Ser Thr Phe Gly Ala Ala Pro Ala Ile 515 520 525 Arg Gln Ile Phe Ile Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala 530 535 540 Val Val Val Pro Thr Asp Pro Thr Arg Ser Lys Leu Asp Leu Leu Gln 545 550 555 560 Ser Ile Arg Glu Thr Ala Arg Ser Ala Gly Leu Asn Ala Tyr Glu Ile 565 570 575 Pro Arg Asp Ile Leu Ile Glu His Glu Pro Phe Ser Val Gly Asn Gly 580 585 590 Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Met Leu His Arg Thr 595 600 605 Tyr Ser Glu Arg Leu Glu Gln Leu Tyr Arg Glu Gln Thr Glu Arg Arg 610 615 620 Glu Gln Glu Leu Ser Ala Leu Arg Ala Gly Arg Asp Glu Ser Ala Leu 625 630 635 640 Gly Thr Val Tyr Gln Ala Val Ala Ala Val Leu Gly Cys Pro Thr Thr 645 650 655 Asp Leu Arg Pro Asp Val His Phe Ala Glu Leu Gly Gly Asp Ser Leu 660 665 670 Ala Ala Val Ser Phe Ala Gly Leu Leu Ala Glu Thr Phe Asp Ile Asp 675 680 685 Ile Gln Ala Ala Thr Val Thr Asn Pro Val His Thr Leu Trp Arg Leu 690 695 700 Ala Glu His Ile Glu Cys Leu Arg Ile Gly Thr Arg Arg Arg Pro Thr 705 710 715 720 Cys Ser Ser Val His Glu Asp Pro Thr Ala Lys Leu His Ala His Glu 725 730 735 Leu Thr Leu Glu Lys Phe Phe Asp Pro Met Ala Leu Pro Val Pro Asp 740 745 750 Arg Pro Arg Ile Ala Ala Ala Pro Thr Val Leu Leu Thr Gly Ala Asn 755 760 765 Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Arg Lys Leu Ala 770 775 780 Asp Ser Gly Gly Arg Leu Ile Cys Leu Val Arg Gly Val Asp Arg Ala 785 790 795 800 Asp Ala Arg Ala Arg Leu Glu Ala Pro Phe Gly Asn Val Asp Pro Arg 805 810 815 Leu Ala Arg Asp Phe Arg Ala Leu Ala Asp Arg Leu Glu Val Val Ala 820 825 830 Gly Asp Ile Ala Glu Pro Asn Leu Gly Leu Ser Glu Asp Asp Trp Gln 835 840 845 Lys Leu Ser Glu Asn Val Asp Val Ile Val His Ala Ala Ala Ala Val 850 855 860 Asn His Leu His Gly Tyr Gly Pro Leu Phe Gly Pro Asn Val Ala Gly 865 870 875 880 Thr Ala Glu Ile Ile Arg Leu Ala Leu Thr Thr Arg Leu Lys Pro Val 885 890 895 Asp Phe Ile Ser Ser Val Ala Val Ala Ala Gly Ser Asp Thr Pro Pro 900 905 910 Ile Thr Glu Asp Asp Asp Leu Arg Ser Val Leu Pro Thr Arg Met Val 915 920 925 Ser Gln Glu Tyr Ala Asn Gly Tyr Gly Ser Ser Lys Trp Ala Ala Glu 930 935 940 Val Leu Leu Arg Glu Ala His Asp Arg Tyr Gly Leu Pro Val Thr Val 945 950 955 960 Phe Arg Ser Gly Met Met Leu Ala His Arg His Tyr Thr Gly Gln Leu 965 970 975 Asn Asn Asp Asp Thr Phe Thr Arg Leu Leu Phe Ser Val Ile Ala Thr 980 985 990 Gly Val Ala Pro Lys Ser Phe Tyr Arg Ala Asn Glu Gln Gly Glu Arg 995 1000 1005 Gln Arg Ala His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Ser 1010 1015 1020 Ser Ile Thr Glu Leu Gly Ala Arg Gln Gln Cys Gly Tyr Arg Thr 1025 1030 1035 Phe His Val Val Asn Pro His Asp Asp Gly Val Ser Leu Asp Thr 1040 1045 1050 Leu Val Asp His Leu Ala Ala Ser Gly His Ala Val Arg Gln Val 1055 1060 1065 Asp Asp Tyr Asp Glu Trp Phe Thr Arg Phe Gly Ile Ala Leu Arg 1070 1075 1080 Ser Leu Pro Val Ala Gly Arg Gln Gln Ser Ile Leu Pro Leu Leu 1085 1090 1095 His Ser Leu His Gln Pro Ala Pro Ala Gln Cys Gly Ser Ala Val 1100 1105 1110 Ser Ala Asp Gln Phe Arg Thr Ala Val Arg Val Ala Ala Pro Gly 1115 1120 1125 Gly Ser Pro Asp Ile Pro His Leu Pro Glu Gly Leu Ile Asp Thr 1130 1135 1140 Tyr Leu Glu Asn Phe Arg Ser His Gly Ile Ile 1145 1150 <210> 212 <211> 1063 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. AG1013 <400> 212 Met Thr Ala Glu Thr Pro Val Asp Glu Arg Leu Val His Arg Val Glu 1 5 10 15 Asp Leu Ser Thr Thr Asp Pro Gln Phe Arg Ala Ala Ala Pro Asp Leu 20 25 30 Ala Val Thr Ala Ala Ala Arg Arg Gly Gly Leu Arg Leu Ser Glu Val 35 40 45 Val Ala Ala Tyr Leu Asp Gly Tyr Ala Asp Arg Pro Ala Leu Gly Arg 50 55 60 Arg Ala His Thr Leu Thr Thr Asp Pro Asp Ser Gly Arg Thr Thr Val 65 70 75 80 Ala Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Arg Ala Leu Arg Glu 85 90 95 Arg Ala Ala Ala Leu Ala Arg Ser Trp Gln Ala Glu Leu Pro Gly Gly 100 105 110 Val Arg Ala Gly Asp Phe Val Ala Val Leu Gly Phe Thr Ser Ile Asp 115 120 125 Tyr Ala Val Ile Asp Leu Thr Cys Ile Arg Leu Gly Ala Val Ser Val 130 135 140 Pro Leu Gln Ser Ser Ser Thr Ala Arg Gln Leu Ala Pro Ile Val Ala 145 150 155 160 Glu Thr Ala Pro Arg Val Leu Ala Glu Glu Leu Asp Arg Gly Ala Ala 165 170 175 Leu Pro Ala Val Pro Ala Phe Val Pro Ala Gln Asp Asp Asp Pro Leu 180 185 190 Ala Met Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala 195 200 205 Met Tyr Thr Thr Asp Met Val Thr Arg Met Trp Gln Arg Ser Arg Gly 210 215 220 Pro Asp Ala Asp Val Asp Gly Arg Val Pro Ala Ile His Val Gln Tyr 225 230 235 240 Met Pro Leu Ser His Val Phe Gly Leu Gly Trp Leu Val Thr Thr Leu 245 250 255 Ser Ser Gly Gly Thr Gly Tyr Phe Ala Ala Arg Asn Ala Met Ser Ser 260 265 270 Leu Phe Asp Asp Ile Ala Leu Ala Arg Pro Thr Ala Leu Asn Leu Val 275 280 285 Pro Arg Val Cys Glu Met Ile Phe Gln Arg Tyr Arg Arg Glu Leu Asp 290 295 300 Arg Arg Pro Pro Gly Ala Ser Pro Asp Ala Val Lys Ser Asp Leu Arg 305 310 315 320 Arg Asn Val Leu Gly Gly Arg Val Leu Thr Ala Leu Cys Gly Ser Ala 325 330 335 Pro Leu Ser Glu Ala Met His Ser Phe Val Glu Ser Thr Leu Asp Val 340 345 350 Thr Val Asn Asp Gly Tyr Gly Ser Thr Glu Thr Gly Gly Gly Val Leu 355 360 365 Arg Asn Gly Arg Ile Leu Arg Pro Pro Val Thr Asp Tyr Lys Leu Val 370 375 380 Asp Val Pro Glu Leu Gly Tyr Leu Thr Gly Asp Glu Pro Tyr Pro Arg 385 390 395 400 Gly Glu Leu Cys Val Lys Ser Thr Asn Leu Ile Pro Gly Tyr Tyr Lys 405 410 415 His Pro Glu Leu Ser Ala Ser Ile Phe Asp Arg Asp Gly Phe Tyr Lys 420 425 430 Thr Gly Asp Ile Met Ala Glu Thr Ala Pro Asp Arg Leu Val Tyr Leu 435 440 445 Asp Arg Arg Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala 450 455 460 Ile Ser Lys Leu Glu Ser Val Tyr Ser Thr Ser Pro Tyr Leu Arg Gln 465 470 475 480 Ile Phe Ile Tyr Gly Ser Ser Glu Gln Ser Phe Leu Leu Ala Val Ile 485 490 495 Val Pro Asn Pro Asp Thr Val Gly Asp Gly Asp Ala His Thr Leu Ile 500 505 510 Ala Ala Ser Leu Gln Gln Ile Ala Asp Asp Ile Asp Leu Asp Ser Tyr 515 520 525 Glu Ile Pro Arg Asp Phe Leu Leu Glu Ser Glu Pro Phe Thr Arg Asp 530 535 540 Asn Gly Leu Leu Ser Gly Ile Gly Lys Leu Leu Arg Pro Ala Leu Ala 545 550 555 560 Asp Leu Tyr Gly Pro Arg Leu Glu Ala Met Tyr Asp Glu Ile Ala Ala 565 570 575 Gly Gln Asp Thr Arg Leu Ala Glu Leu Arg Ala Ala Ala Ala Asp Leu 580 585 590 Pro Thr Leu Glu Ala Val Arg Arg Ala Ala Ala Val Thr Leu Gly Val 595 600 605 Pro Asp Ala Asp Ile Pro Asp Gly Asp Asp Ala Gly Phe Ala Asp Leu 610 615 620 Gly Gly Asp Ser Leu Ala Ala Phe Thr Phe Ala Thr Thr Leu Glu Gln 625 630 635 640 Leu Phe Asp Val Asp Val Pro Val Gln Thr Ile Val Ser Pro Ile Ala 645 650 655 Thr Leu Gly Thr Ile Thr Lys Tyr Leu Asp Gly Glu Arg Ser Ser Ala 660 665 670 Ala Thr Arg Pro Thr Phe Ala Ser Val His Gly Arg Gly Ala Thr Ile 675 680 685 Ala Arg Ala Glu Gly Leu Arg Leu Asp Ala Phe Ile Asp Ala Ala Thr 690 695 700 Leu Ala Ala Ala Pro Ser Leu Pro Ala Pro Thr Gly Thr Val Asp Thr 705 710 715 720 Val Leu Met Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu 725 730 735 Ala Trp Leu Glu Arg Leu Ala Arg Thr Gly Gly Thr Leu Ile Cys Ile 740 745 750 Thr Arg Gly Ala Asp Pro Ala Glu Ala Arg Gln Arg Ile Val Ala Ala 755 760 765 Ile Asp Ser Gly Asp Glu Asp Leu Ser Val Arg Phe Arg Ala Leu Ala 770 775 780 Asp Asp His Leu Glu Val Leu Ala Gly Asp Val Gly Asp Pro Tyr Leu 785 790 795 800 Gly Leu Asp Gln Pro Thr Trp Ser Arg Leu Ala Asp Ser Val Asp Leu 805 810 815 Ile Val His Ser Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln 820 825 830 Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Val Arg Leu Ala 835 840 845 Ile Thr Ala Arg Leu Lys Pro Val Asp Tyr Ile Ser Thr Val Ala Val 850 855 860 Thr Ala Leu Pro Gly Gly Gly Phe Ile Gly Glu Asp Val Asp Val Arg 865 870 875 880 Ala Ala Ser Pro Ser Arg Ala Leu Asp Ala Ser Tyr Ala Asn Gly Tyr 885 890 895 Ala Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 900 905 910 Leu Cys Gly Leu Pro Val Thr Val Phe Arg Ser Asp Met Ile Leu Ala 915 920 925 His Ser Arg Tyr Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg 930 935 940 Leu Met Leu Ser Leu Val Ala Thr Gly Ile Ala Pro Arg Ser Phe Tyr 945 950 955 960 Arg Leu Asp Ala Ala Gly His Arg Gln Arg Ala His Tyr Asp Asp Trp 965 970 975 Leu Ala Arg Phe Glu Ala Ala Ile Glu Ser Leu Pro Asp Asn Gln Arg 980 985 990 Gln His Ser Val Arg Pro Leu Leu Ser Ala Tyr Ala His Pro Ala Pro 995 1000 1005 Ala Arg Pro Glu Ala Gln Pro Pro Ser Glu Gln Phe Arg Ala Ala 1010 1015 1020 Val Gln Ser Ala Gly Ile Asp Gly Phe Ala Asp Val Pro His Leu 1025 1030 1035 Thr Glu Ser Leu Ile Asp Lys Tyr Ile Ala Asp Leu Arg Arg Leu 1040 1045 1050 Gly Leu Leu Ala Ala Ser Pro Ser Asp Gly 1055 1060 <210> 213 <211> 1116 <212> PRT <213> Artificial Sequence <220> <223> Microbacterium sp. AG157 <400> 213 Met Glu Gln Gln His Asp Asp Met Ser Val Glu Ala Val Phe Ala Gln 1 5 10 15 His Ala Asp Arg Pro Ala Leu Arg Glu Arg Phe Gly Ala Asp Val Glu 20 25 30 Asp Thr Ser Phe His Glu Leu Trp Asp Arg Ala Ser Ala Val Ala Ala 35 40 45 Ala Leu Gly Glu Thr Val Ser Pro Gly Asp Arg Ile Ala Met Leu Gly 50 55 60 Ala Ala Thr Val Asp Phe Val Thr Leu Asp Leu Ala Ser Trp Ile Leu 65 70 75 80 Gly Ala Val Ser Val Pro Leu Gln Ala Ser Ala Ser Phe Glu Ala Leu 85 90 95 Arg Ala Ile Val Asp Glu Thr Glu Pro Val Trp Leu Ala Ala Ser Ala 100 105 110 Glu Gln Ser Ala Ile Ala Gln Ala Ile Ala Glu Ala Ser Ala Gly Asp 115 120 125 Val Arg Thr Met Leu Leu Asp Thr Ala Val Asp Thr Asp Thr Ser Gly 130 135 140 Pro Thr Leu Ala Glu Leu Val Thr Arg Gly Glu Leu Leu Pro Arg Pro 145 150 155 160 Thr Pro Trp His Pro Ala Ala Gly Glu Asp Pro Leu Ala Leu Leu Ile 165 170 175 Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Ser Arg 180 185 190 Ser Met Val Glu Arg Leu Trp His Ala Arg Arg Pro Gly Val Asp Asp 195 200 205 Gly Thr Thr Asp Asp Ile Val Gly Tyr Ala Tyr Leu Pro Met Ser His 210 215 220 Leu Thr Gly Arg Ala Ala Val Phe Ala Thr Leu Gly Arg Gly Gly Thr 225 230 235 240 Leu Ala Leu Ala Thr Ser Thr Asp Leu Ser Ala Leu Phe Asp Asp Leu 245 250 255 Arg Thr Phe Ala Pro Thr Glu Phe Val Phe Val Pro Arg Val Ala Glu 260 265 270 Met Val Arg Gln Glu Gly Asp Arg Asp Glu Gln Arg Arg Leu Ala Ala 275 280 285 Gly Asp Thr Asp Gln Asp Ala Val Arg Ala Ala Val His Ala Asp Leu 290 295 300 Arg Val Arg Ala Phe Gly Gly Arg Ile Arg Arg Ala Ile Cys Ala Ser 305 310 315 320 Ala Pro Leu Thr Pro Glu Leu Arg Ser Tyr Ile Glu Glu Cys Leu Gly 325 330 335 Thr Ala Leu His Asp Val Tyr Gly Ser Thr Glu Ala Gly Ser Ile Leu 340 345 350 His Asp Gly Val Val Gln Gln Pro Pro Val Thr Ala His Lys Leu Ile 355 360 365 Asp Val Pro Glu Leu Gly Tyr Arg Val Thr Asp Arg Pro His Pro Arg 370 375 380 Gly Glu Leu Leu Val Lys Ser Thr Ser Thr Ile Thr Gly Tyr Phe Arg 385 390 395 400 Arg Pro Asp Val Thr Ala Ala Val Phe Asp Gln Asp Gly Phe Tyr Arg 405 410 415 Thr Gly Asp Ile Met Ala Gln Thr Gly Pro Gly Ser Tyr Glu Tyr Leu 420 425 430 Asp Arg Arg Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala 435 440 445 Val Ala Ala Leu Glu Ala Thr Tyr Gly Gly Thr Pro Glu Val Arg Gln 450 455 460 Ile Ala Leu His Gly Asp Ser Arg His Ala Phe Leu Val Ala Val Val 465 470 475 480 Val Pro Ala Asp Ala Gly Ser Ser Glu Arg Asp Val Leu Ala Ala Leu 485 490 495 Gln Arg Thr Ala Arg Glu His Gly Leu Ala Pro Tyr Glu Val Pro Arg 500 505 510 Gly Val Ile Val Glu Pro Glu Pro Phe Thr Val Glu Asn Gly Met Leu 515 520 525 Ser Asp Ala Arg Lys Leu Leu Arg Pro Arg Ile Thr Ala Arg Tyr Gly 530 535 540 Glu Arg Leu Ala Ser Leu Tyr Ala Asp Leu Ala Glu Glu Arg Ser Gly 545 550 555 560 Ala Leu Val Ala Ala Leu Arg Glu Arg Val Gly Leu Glu Pro Thr Leu 565 570 575 Asp Thr Val Val Arg Ala Ala Cys Glu Phe Leu Gly Ala Glu Val Ser 580 585 590 Ser Ala Thr Ala Ala Ala Ala Arg Tyr Ser Asp Leu Gly Gly Asp Ser 595 600 605 Leu Ser Ala Leu Thr Phe Ser Gly Met Leu Glu Asp Val Phe Gly Thr 610 615 620 Glu Val Pro Val Gly Val Ile Thr Asp Pro Thr Asn Asp Leu Thr Ala 625 630 635 640 Ile Ala Ala Phe Ile Asp Arg Ser Ala Ala Asp Asp Arg Pro Thr Val 645 650 655 Ala Arg Val His Gly Thr Asp Pro Ser Thr Leu Arg Ala Ser Asp Leu 660 665 670 Arg Leu Asp Arg Val Leu Gly Gly Ile Pro Glu Pro Val Leu Arg Thr 675 680 685 Ser Arg Thr Pro Ala Ala Ser Glu Pro Ala Gly Thr Ala Arg Gly Arg 690 695 700 Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Ala 705 710 715 720 Leu Asp Trp Leu Glu Arg Leu Ala Pro Val Gly Gly Thr Leu Val Cys 725 730 735 Ile Val Arg Gly Ser Asp Asp Ala Asp Ala Arg Arg Arg Leu Asp Thr 740 745 750 Ala Phe Ala Ala Asp Pro Ala Phe Ala Glu Arg Phe Thr Asp Leu Gly 755 760 765 Ala Ser Leu Glu Val Arg Ala Gly Asp Val Ser Glu Arg Leu Phe Gly 770 775 780 Leu Asp Glu Pro Arg Trp Arg Asp Leu Ala Ala Arg Val Asp Leu Ile 785 790 795 800 Ala His Ala Ala Ala Leu Val Asn His Val Leu Pro Tyr Thr Ala Leu 805 810 815 Phe Gly Pro Asn Val Val Gly Thr Ser Glu Ile Ile Arg Leu Ser Ile 820 825 830 Ala Ala Gly Ser Val Pro Val Thr Phe Val Ser Ser Val Ala Val Ala 835 840 845 Gly Gly Ala Arg Pro Thr Val Glu Ala Ala Ala Asp Pro Ala Ala Pro 850 855 860 Ala Ala Leu Asp Glu Arg Ala Asp Ile Arg Asp Thr Ile Pro Ala Trp 865 870 875 880 Ser Ile Gly Asp Glu Tyr Ala Asn Gly Tyr Gly Ala Ser Lys Trp Ala 885 890 895 Ser Glu Val Leu Leu Arg Glu Ala His Glu Gln His Gly Val Pro Val 900 905 910 Ala Val Phe Arg Ser Asp Met Val Leu Ala His Pro Arg Trp Arg Gly 915 920 925 Gln Val Asn Leu Pro Asp Val Phe Thr Arg Leu Val Trp Ser Val Leu 930 935 940 Ala Thr Gly Leu Ala Pro Glu Ser Phe Val Arg Arg Gly Ala Asp Gly 945 950 955 960 Glu Arg Leu Ser Ser His Tyr Asp Gly Leu Pro Ala Asp Phe Thr Ser 965 970 975 Ala Ala Met Thr Ala Ile Gly Ala Ser Thr Asn Ala Gly Tyr Arg Thr 980 985 990 Tyr Asn Val Val Asn Pro Asn Asp Asp Gly Val Ser Leu Asp Thr Val 995 1000 1005 Val Asp Trp Leu Gln Asp Asp Gly Tyr Ala Ile Glu Arg Ile Ala 1010 1015 1020 Asp His Ala Glu Trp Val Asp Arg Phe Arg Thr Ala Leu Glu Ala 1025 1030 1035 Leu Pro Asp Glu Asp Arg Ala Arg Ser Val Leu Pro Leu Met His 1040 1045 1050 Ala Phe Ala Thr Pro Glu Glu Pro His Ala Gly Ser Thr Ile Pro 1055 1060 1065 Ala Asp Ala Phe Val Glu Ala Ile Arg Thr Ile His Pro Leu Gly 1070 1075 1080 Ser Pro Asp Ile Pro Ser Ile Asp His Ala Leu Ile Thr Lys Val 1085 1090 1095 Ala Asp Asp Leu Ser Phe Leu Lys Leu Leu Glu Pro Ser Arg Arg 1100 1105 1110 Ala Val Ala 1115 <210> 214 <211> 1146 <212> PRT <213> Artificial Sequence <220> <223> Nocardia sp. YIM PH 21724 <400> 214 Met Tyr Ala Glu Asp Glu Gln Val Arg Ala Ala Ala Pro Asp Ala Ala 1 5 10 15 Ile Ala Ala Arg Val Arg Glu Pro Gly Ile Gly Leu Pro Arg Ile Val 20 25 30 Thr Thr Ile Leu Gln Gly Tyr Ala Asp Arg Pro Ala Ile Gly Gln Arg 35 40 45 Ala Thr Glu Ile Thr Val Glu Asp Thr Gly Arg Lys Thr Val Arg Arg 50 55 60 Leu Pro Arg Phe Asp Thr Val Thr Tyr Gly Glu Leu Ala Glu Arg Val 65 70 75 80 Ala Ala Val Ala Ala Ala Trp Ala Gly Glu Glu Asp Asn Pro Leu Arg 85 90 95 Gln Gly Asp Phe Val Ala Thr Leu Gly Phe Ile Ser Gly Asp Tyr Ala 100 105 110 Ala Ile Asp Leu Ala Cys Leu Arg Thr Gly Ala Val Ala Val Pro Leu 115 120 125 Gln Ala Gly Ala Thr Arg Ala Gln Gln Gly Ala Ile Leu Ala Glu Thr 130 135 140 Glu Pro Leu Leu Phe Ala Ser Ser Ala Glu Leu Leu Asp Thr Ala Val 145 150 155 160 Glu Leu Val Leu Ala Ala Pro Val Thr Pro His His Leu Val Val Phe 165 170 175 Asp Tyr His Pro Gly Asp Asp Lys His Arg Ala Ala Leu Glu Ser Ala 180 185 190 Arg Glu Arg Leu Ala Gly Arg Val Val Val Glu Pro Leu Thr Glu Val 195 200 205 Leu Asp Arg Gly Arg Thr Leu Pro Pro Ala Pro Glu Leu Ser Gly Asp 210 215 220 Asp Asp Ala Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala 225 230 235 240 Pro Lys Gly Ala Met Tyr Thr Gln Arg His Val Ala Arg Ile Trp Leu 245 250 255 Gly Met Arg Gln Leu Pro Val Ile Asn Phe Asn Phe Met Pro Leu Gly 260 265 270 His Val Ala Gly Arg Ile Ser Leu Tyr Ala Thr Leu Ala Arg Gly Gly 275 280 285 Thr Ala Tyr Phe Ala Ala Glu Ser Asp Met Ser Thr Leu Phe Glu Asp 290 295 300 Leu Ala Leu Ile His Pro Thr Glu Leu Phe Phe Val Pro Arg Val Cys 305 310 315 320 Asp Met Val Phe Gln Arg Tyr Gln Ser Glu Val Asp Arg Arg Thr Thr 325 330 335 Ala Gly Ala Asp Pro Ala Val Leu Asp Arg Glu Val Lys Asp Glu Leu 340 345 350 Arg His Glu Ile Leu Gly Asp Arg Leu Ile Tyr Ala Leu Val Gly Ser 355 360 365 Ala Pro Leu Ala Pro Glu Met Arg Ala Phe Thr Arg Ser Leu Leu Gly 370 375 380 Ile Pro Leu His Asp Gly Tyr Gly Ser Thr Glu Ala Gly Gly Gly Val 385 390 395 400 Leu Leu Asp Asn Arg Ile Gln Arg Asp Ser Val Leu Asp Tyr Lys Leu 405 410 415 Ile Asp Val Pro Glu Leu Gly Tyr Phe Ala Thr Asp Lys Pro Tyr Pro 420 425 430 Arg Gly Glu Leu Leu Leu Lys Thr Asn Thr Met Ile Pro Gly Tyr Tyr 435 440 445 Arg Arg Pro Glu Val Thr Ala Glu Ile Phe Asp Ala Asp Gly Phe Tyr 450 455 460 Lys Thr Gly Asp Ile Met Ala Glu Thr Gly Pro Asp Glu Leu Ile Tyr 465 470 475 480 Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val 485 490 495 Ala Val Ala His Leu Glu Ser Val Tyr Ala Ser Ser Pro Leu Val Arg 500 505 510 Gln Ile Phe Leu Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val 515 520 525 Ile Val Pro Thr Ala Asp Ala Leu Ala Ala His Gly Asp Ser Ile Lys 530 535 540 Ser Ala Leu Gly Asp Ser Leu Gln Arg Ile Gly Lys Asp Ala Gln Leu 545 550 555 560 Gln Ser Tyr Glu Ile Pro Arg Asp Phe Leu Ile Glu Thr Glu Pro Phe 565 570 575 Ser Glu Glu Asn Gly Leu Leu Ser Gly Ile Gly Lys Ile Leu Arg Pro 580 585 590 Lys Leu Arg Asp His Tyr Gly Pro Arg Leu Gln Gln Leu Tyr Ala Asp 595 600 605 Leu Ala Ala Glu Gln Thr Asn Glu Leu Leu Glu Leu Arg Arg Thr Ala 610 615 620 Ala Gly Leu Pro Val Leu Glu Val Val Gly Arg Ala Ala Gly Ala Leu 625 630 635 640 Leu Gly Cys Ala Gly Ala Asp Leu Arg Pro Asp Ala His Phe Thr Asp 645 650 655 Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Tyr Ser Thr Leu Leu Arg 660 665 670 Asp Ile Leu Gly Val Glu Val Pro Val Gly Val Ile Val Ser Pro Ala 675 680 685 Asn Asp Leu Thr Ser Leu Ala Lys Tyr Ile Glu Ala Glu Arg Asp Ser 690 695 700 Ser Ala Gly Arg Pro Thr Ala Ala Ser Val His Ala Ser Ala Thr Glu 705 710 715 720 Ile Arg Ala Ala Glu Leu Thr Leu Asp Lys Phe Leu Asp Glu Arg Thr 725 730 735 Leu Ala Ala Ala Ser Thr Leu Pro Ala Ala Thr Gly Thr Pro Arg Thr 740 745 750 Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu 755 760 765 Glu Trp Leu Gln Arg Leu Ala Pro Val Gly Gly Lys Leu Val Cys Val 770 775 780 Ile Arg Gly Ser Asp Pro Ala Ala Ala Arg Ala Arg Leu Asp Ala Ala 785 790 795 800 Phe Asp Ser Gly Asp Pro Glu Leu Leu Arg His Tyr Thr Glu Leu Ala 805 810 815 Arg Asp Thr Leu Glu Val Leu Pro Gly Asp Ile Gly Asp Pro Asp Leu 820 825 830 Gly Leu Asp Gln Ala Asn Trp Arg Arg Leu Ala Glu Thr Val Asp Leu 835 840 845 Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Gly Gln 850 855 860 Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Arg Leu Ala 865 870 875 880 Ile Thr Ala Arg Arg Lys Pro Val Thr Tyr Leu Ser Thr Val Gly Val 885 890 895 Ala Ser Gly Met Ala Pro Gly Glu Phe Asp Glu Asp Gly Asp Ile Arg 900 905 910 Arg Thr Ser Pro Gln Arg Arg Ile Asp Asp Gly Tyr Ala Asn Gly Tyr 915 920 925 Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 930 935 940 Arg Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala 945 950 955 960 His Ser Arg Tyr Ala Gly Gln Leu Asn Leu Pro Asp Met Phe Thr Arg 965 970 975 Leu Ile Leu Ser Leu Leu Thr Thr Gly Val Ala Pro Tyr Ser Phe Tyr 980 985 990 Arg Thr Asp Ala Ala Gly Glu Arg Glu Arg Gly His Tyr Asp Gly Leu 995 1000 1005 Pro Ala Asp Phe Thr Ala Ala Ala Ile Thr Glu Leu Gly Val Arg 1010 1015 1020 Val Thr Asp Gly Tyr Arg Thr Tyr Asp Val Phe Asn Pro His Asp 1025 1030 1035 Asp Gly Val Ser Leu Asp Leu Phe Val Asp Trp Leu Ile Glu Ala 1040 1045 1050 Gly His Pro Ile Arg Arg Leu Asp Asp Tyr Gly Gln Trp Phe Ala 1055 1060 1065 Arg Phe Glu Thr Ser Leu Arg Ala Leu Pro Asp Lys Gln Arg Gln 1070 1075 1080 Ala Ser Val Leu Pro Leu Leu His Ala Tyr Arg Glu Pro Glu Pro 1085 1090 1095 Ala Val Arg Gly Ser Ala Phe Pro Thr Glu Arg Phe His Glu Ala 1100 1105 1110 Val Arg Glu Ala Lys Ile Gly Pro Asp His Asp Ile Pro His Leu 1115 1120 1125 Ser Arg Ala Leu Ile Asp Lys Tyr Val Ser Asp Leu Arg Leu Arg 1130 1135 1140 Gly Leu Leu 1145 <210> 215 <211> 1126 <212> PRT <213> Artificial Sequence <220> <223> Myceligenerans xiligouense <400> 215 Met Ala Leu Ala Ser Thr Met Thr Ala Val Phe Glu Arg Tyr Thr Asp 1 5 10 15 Arg Pro Ala Leu Ala Glu Arg Thr Pro Val Pro Arg Ser Asp Glu Asp 20 25 30 Leu Thr Thr Phe Thr Ala Arg Ala Glu Asp Ser Tyr Asp Leu Leu Thr 35 40 45 Tyr Gly Glu Leu Ala Gln Arg Val Ser Ser Val Ala Ala Gln Leu Thr 50 55 60 Asp Asp Arg Arg Gly Ala Gly Arg Leu Thr Glu Gly Asp Met Thr Ala 65 70 75 80 Phe Leu Gly Phe Ala Gly Ala Asp Tyr Val Thr Ala Asp Leu Ala Cys 85 90 95 Asn Leu Ala Gly Ile Thr Thr Val Pro Leu Gln Thr Ser Ala Ser Leu 100 105 110 Asp Gln Gln Ala Ser Ile Leu Ala Thr Thr Ala Pro Arg Ala Leu Ala 115 120 125 Val Ser Val Ser Leu Leu Gly Arg Ala Val Glu Leu Leu Ala Ala Gln 130 135 140 Pro Thr Ile Thr Arg Leu Leu Val Leu Asp Tyr Arg Gly Gly Asp Pro 145 150 155 160 Asp His Val Arg Glu Leu Glu Ser Leu Asp Gly Thr Gly Val Pro Arg 165 170 175 Pro Glu Leu Leu Asp Leu Ser Gly Ala Gly Ala Ala Val Val Ala Pro 180 185 190 Trp Thr Glu Ser Arg Pro Val Met Leu Leu His Thr Ser Gly Ser Thr 195 200 205 Gly Thr Pro Lys Gly Ala Ile Tyr Pro Glu Arg Leu Val Thr Ala Met 210 215 220 Trp Gly Gly Asp Gly Trp Ser Glu Phe Phe Ala Ala Glu Pro Asp Val 225 230 235 240 Ser Thr Phe His Tyr Met Pro Met Ser His Val Ala Gly His Ser Ser 245 250 255 Val Arg Ser Thr Leu Ala Arg Gly Gly Leu Thr Tyr Phe Ala Ser Ser 260 265 270 Thr Asn Leu Ser Ser Leu Phe Asp Asp Leu Ala Leu Ala Arg Pro Thr 275 280 285 Glu Leu Ser Leu Val Pro Arg Val Cys Glu Leu Met Arg Gln Glu Phe 290 295 300 Arg Arg Arg Leu Gln Ala Ala Arg Ser His Thr Pro Asp Gly Asp Asp 305 310 315 320 Asp Val Leu Ala Ala Ser Val Arg Asp Glu Met Arg Thr Gln Val Leu 325 330 335 Gly Gly Asn Val Arg Trp Ala Ser Cys Thr Ser Ala Pro Ile Ser Ala 340 345 350 Glu Leu Lys Ala Phe Val Glu Asp Leu Leu Gln Ile Asp Val His Glu 355 360 365 Leu Tyr Gly Thr Thr Glu Ile Gly Gly Val Leu Ser Asn Gly Arg Phe 370 375 380 Leu Arg Pro Pro Val Leu Asp His Arg Leu Glu Asp Val Pro Glu Leu 385 390 395 400 Gly Tyr Tyr Ser Ser Asp Arg Pro Arg Ser Arg Gly Glu Leu Leu Ile 405 410 415 Arg Ser Thr Ser Thr Ile Pro Gly Tyr Tyr Gly Arg Pro Asp Leu Asp 420 425 430 Glu Gln Ile Phe Thr Asp Asp Gly Phe Tyr Arg Thr Gly Asp Ile Ala 435 440 445 Ser Val Asp Asp Thr Gly Thr Val Arg Ile Ile Asp Arg Lys Asn Ala 450 455 460 Ile Val Lys Leu Ser Gln Gly Glu Phe Val Ala Leu Pro Ser Leu Glu 465 470 475 480 Gly Thr Tyr Val Ser Arg Ser Glu Val Leu Arg Gln Val Tyr Leu His 485 490 495 Gly Asp Gly Gly Glu Ser Ser Ile Leu Ala Val Ala Val Pro Thr Asp 500 505 510 Glu Leu Val Asp Arg Leu Gly Gly Asp Val Pro Ala Ile Arg Glu His 515 520 525 Leu Leu Gln Glu Phe Arg Ala Ile Gly Ala Ala Glu Ala Leu Asn Ser 530 535 540 Tyr Glu Val Pro Arg Gly Val Leu Val Glu Leu Glu Pro Phe Ser Glu 545 550 555 560 Ser Asn Gly Leu Leu Ser Asp His Arg Lys Leu Val Arg Pro Glu Leu 565 570 575 Ala Arg Arg Tyr Gly Pro Val Leu Thr Ala Phe Tyr Glu Ser Leu Arg 580 585 590 Ser Ser Ser Asp Ala Leu Leu Glu Ser Leu Arg Asp Asn Ala Gly Asp 595 600 605 Ala Pro Thr Val Ala Thr Val Arg Asp Ala Ala Ala Ile Ala Ile Gly 610 615 620 Thr Ser Pro Ala Asp Ile Gly Ala Glu Asp Arg Phe Arg Asp Leu Gly 625 630 635 640 Gly Asp Ser Leu Thr Ala Val His Leu Ser Asn Leu Leu Glu Gln Ile 645 650 655 Phe Gly Val Arg Val Pro Val Asn Thr Ile Ala Gly Glu Ala Thr Thr 660 665 670 Ile Gly Arg Leu Ala Asp Leu Leu Asp Ala Arg Arg Asn Gly Asp Ala 675 680 685 Ala Val Val Ser Phe Glu Ser Val His Gly Asp Ala Pro Glu Leu Leu 690 695 700 Arg Ala Glu Asp Leu Arg Leu Ala Arg Phe Leu Gly Asp Gly Phe Thr 705 710 715 720 Pro Ala Pro Val Glu Ser Pro Thr Gly Asp Ala Pro Thr Val Leu Ile 725 730 735 Thr Gly Ala Asn Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu 740 745 750 His Glu Val Ala Ala Thr Gly Gly Arg Val Ile Cys Ile Val Arg Ala 755 760 765 Ala Asp Asp Asp Glu Ala Tyr Glu Arg Leu Arg Arg Ala Phe Thr Ser 770 775 780 Asp Glu Arg Leu Leu Lys Thr Phe Asp Arg Phe Gly His Ala Leu Glu 785 790 795 800 Val Leu Ala Gly Asp Leu Ser Glu Pro Ala Leu Gly Leu Asp Ala Asp 805 810 815 Thr Trp Asp Arg Leu Ala Arg Asp Val His Arg Val Val His Ala Gly 820 825 830 Ala Met Val Asn His Ala Leu Pro Tyr Gln Glu Leu Phe Asp Ala Asn 835 840 845 Val Ala Gly Thr Ala Glu Val Val Arg Leu Ala Ala Ser Val Arg Leu 850 855 860 Lys Pro Val Ser Phe Val Ser Ser Ile Ala Thr Ala Leu Leu Ala Gly 865 870 875 880 Thr Glu Ser Pro Leu Asp Glu His Ala Asp Ile Arg Arg Ala Leu Pro 885 890 895 Ser Val Gly Thr Gly Thr Lys Asn Asn Val Glu Gly Tyr Ala Ala Thr 900 905 910 Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Ser Phe His 915 920 925 Leu Pro Val Thr Thr Phe Arg Ala Ser Met Ile Leu Ala His Ser Glu 930 935 940 Tyr Val Gly Gln Ile Asn Val Pro Asp Thr Phe Ser Arg Leu Val Tyr 945 950 955 960 Ser Leu Val Arg Thr Gly Val Val Pro Ser Ser Phe Tyr Ala Pro Gly 965 970 975 Gly Gly Arg Pro His Tyr Asp Gly Leu Pro Val Asp Val Val Ala Ser 980 985 990 Cys Ile Val Ala Leu Asp Ala Ala Gly Arg Gly Gly Tyr Ser Thr His 995 1000 1005 His Val Val Asn Pro Leu Asp Asp Gly Val Ser Leu Asp Thr Met 1010 1015 1020 Val Asp Trp Leu Thr Gly Leu Gly Val Glu Leu Thr Lys Val Asp 1025 1030 1035 Asp His Ala Asp Trp His Arg Arg Leu Gly Ala Gly Leu Arg Ala 1040 1045 1050 Leu Pro Glu Ser Glu Arg Arg Ala Ser Ile Leu Pro Leu Leu Asp 1055 1060 1065 Ser Phe Ser Ala Pro Glu Gln Pro Val Ala Gly Ser Ser Ile Ala 1070 1075 1080 Ser Pro Gly Phe Leu Ala Arg Val Arg Asp Leu Gly Leu Asp Thr 1085 1090 1095 Arg Ile Arg Ser Leu Asp Ala Arg Phe Val Glu Lys Ser Leu Ser 1100 1105 1110 Asp Leu Glu His Val His Gly Arg Pro Leu Arg Thr Ala 1115 1120 1125 <210> 216 <211> 1182 <212> PRT <213> Artificial Sequence <220> <223> Pseudonocardiales bacterium <400> 216 Met Thr Thr Ala Thr Ile Asp Thr Pro Val Lys Gly Ala Leu Phe Thr 1 5 10 15 Gly Gly Ala Thr Thr Asp Trp Gly Lys Ala Arg Phe Glu Leu Leu Val 20 25 30 Val Glu Asp Ala Gln Phe Arg Asp Ala Leu Pro Arg Ala Ala Val Thr 35 40 45 Asp Ala Lys Arg Gln Pro Gly Leu Arg Leu Ala Gln Val Val Gln Thr 50 55 60 Val Met Glu Gly Tyr Ala Asp Arg Pro Ala Ile Gly Gln Arg Ala Arg 65 70 75 80 Glu Phe Val Thr Asp Ala Ser Ser Gly Arg Thr Ser Ala Arg Ile Leu 85 90 95 Gly His Phe Glu Thr Cys Thr Phe Gly Glu Leu Trp Ser Arg Val Lys 100 105 110 Ala Thr Ala Thr Asp Trp His His His Ala Gly His Pro Val Lys Pro 115 120 125 Gly Asp Phe Val Ala Ile Leu Gly Phe Ala Ser Ala Asp Tyr Ala Thr 130 135 140 Leu Ala Leu Ala Asn Ile His Leu Gly Ala Val Asn Val Pro Leu Gln 145 150 155 160 Ala Thr Ala Pro Ala Ser Gln His Ala Asp Ile Ile Ala Glu Thr Glu 165 170 175 Pro Ser Val Leu Ala Thr Gly Ile Glu Tyr Ile Asp Ser Ala Val Glu 180 185 190 Ala Val Leu Ser Gly Thr Val Pro Pro Arg Leu Ile Val Phe Asp Tyr 195 200 205 Glu Pro Arg Asp Asp Thr Gln Arg Glu Arg Phe Glu Ala Ala Arg Glu 210 215 220 Arg Leu Lys Ala Ala Ala Cys Pro Ile Ala Val Asp Thr Leu Gln Asp 225 230 235 240 Val Ile Ala Arg Gly Arg Ser Leu Pro Glu Val Pro Leu His Val Ser 245 250 255 Glu Gln Asp Asp Pro Leu Thr Trp Leu Phe Tyr Thr Ser Gly Thr Thr 260 265 270 Gly Thr Pro Lys Gly Ala Met Ile Ala Glu Gln Thr Ile Arg Asn Thr 275 280 285 Trp Leu Tyr Ala Ala Glu Lys Pro Ser Ile Thr Leu Ser Phe Met Pro 290 295 300 Met Ser His Met Val Gly Tyr Gly Tyr Leu Phe Leu Ala Leu Ala Asn 305 310 315 320 Gly Gly Thr Ser Phe Cys Ser Pro Lys Ser Asp Leu Ser Thr Leu Phe 325 330 335 Glu Asp Leu Ala Met Ala Arg Pro Thr Met Ala Ser Leu Val Pro Arg 340 345 350 Val Cys Glu Met Leu Tyr Gln His Tyr Leu Gly Glu Val Asp Arg Arg 355 360 365 Ile Ala Lys Gly Ala Asp Glu Ala Ala Ala Gln Gln Glu Val Lys Leu 370 375 380 Glu Met Arg Glu Lys Leu Leu Gly Gly Arg Leu Leu Ser Val Gly Cys 385 390 395 400 Gly Ser Ala Val Leu Ser Pro Glu Val His Gln Phe Met Leu Ser Met 405 410 415 Leu Gly Ile His Met Ala Ile Gly Tyr Ser Ser Thr Glu Met Ala Thr 420 425 430 Ala Thr Val Leu Val Asp Gly Arg Ile Gln Arg Pro Pro Val Ile Asp 435 440 445 Tyr Lys Leu Ala Asp Val Pro Glu Leu Gly Tyr Phe Thr Thr Asp Lys 450 455 460 Pro Tyr Pro Arg Gly Glu Phe Leu Val Lys Ile Ala Lys Phe Met Asp 465 470 475 480 Gly Tyr Tyr Lys Arg Pro Asp Leu Thr Ala Glu Lys Phe Thr Glu Asp 485 490 495 Gly Phe Tyr Arg Ser Gly Asp Val Met Ala Leu Thr Gly Pro Asp Gln 500 505 510 Leu Ile Tyr Leu Asp Arg Val Asn Asn Val Gln Lys Leu Ser Gln Gly 515 520 525 Glu Phe Val Ala Ile Ala Arg Leu Glu Ala Leu Tyr Thr Gln Ser Pro 530 535 540 Pro Ile Arg Gln Ile Tyr Val Tyr Gly Ser Ser Asp Arg Ala Phe Leu 545 550 555 560 Leu Ala Val Ala Val Pro Ser Ala Glu Leu Met Thr Gln Tyr Val Gln 565 570 575 Gly Gly Glu Ala Ala Asp Arg Val Lys Ala Ala Ile Arg Arg Ala Leu 580 585 590 Gln Glu Val Ala Glu Glu His Gly Leu Ala Ser Tyr Glu Val Pro Arg 595 600 605 Asp Phe Leu Ile Glu Thr Glu Pro Phe Ser Ser Glu Asn Gly Leu Leu 610 615 620 Thr Gly Ile Gly Lys Phe Ser Arg Pro Lys Phe Lys Asp Arg Tyr Gly 625 630 635 640 Ala Arg Leu Glu Ala Val Tyr Ala Gln Ile Ala Gln Asp Gln Val Ser 645 650 655 Glu Leu Arg Ala Leu Arg Asn Gly Ser Thr Asp Arg Pro Val Ile Glu 660 665 670 Thr Val Ala Arg Ala Val Lys Ala Thr Leu Gly Val Ala Glu Thr Asp 675 680 685 Val Thr Pro Gln Ser Arg Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser 690 695 700 Ala Leu Ser Phe Ser Met Leu Leu Glu Glu Ile Phe Gly Val Glu Val 705 710 715 720 Pro Val Gly Val Ile Ile Asn Pro Ala Gly Asp Leu Arg Leu Ile Ala 725 730 735 Asp Tyr Val Glu Ala Leu Arg Ser Gly Ser Thr Arg Pro Ser Phe Ser 740 745 750 Thr Val His Ala Ala Asp Gly Thr Thr Ile His Ala Ala Asp Phe Lys 755 760 765 Leu Glu Lys Phe Ile Pro Ala Glu Met Leu Ala Ala Ala Pro Arg Leu 770 775 780 Pro Ala Pro Ala Glu Thr Val Arg Thr Val Leu Leu Thr Gly Ser Thr 785 790 795 800 Gly Phe Leu Gly Arg Phe Gln Ala Ile Ser Trp Leu Glu Arg Met Ala 805 810 815 Lys Thr Gly Gly Arg Leu Ile Leu Val Ala Arg Gly Ala Asn His Ala 820 825 830 Gln Ala Leu Gln Arg Val Glu Glu Ala Leu Asp Ser Asp Pro Ala Leu 835 840 845 Leu Arg His Phe Arg Ala Leu Ala Lys Asp His Leu Glu Val Leu Pro 850 855 860 Gly Asp Leu Gly Leu Pro Gly Leu Gly Leu Asp Glu Ala Thr Trp Asn 865 870 875 880 Arg Leu Ala Glu Thr Val Asp Leu Ile Ala His Thr Ala Ala His Val 885 890 895 Asn His Val Leu Pro Tyr Asn Gln Leu Phe Thr Ala Asn Val Gly Gly 900 905 910 Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr His Arg Leu Lys His Phe 915 920 925 Asp Tyr Val Ser Thr Leu Gly Val Met Ala Leu Ala Gly Arg Pro Val 930 935 940 Gly Glu Asp Gly Asp Ile Arg Glu Ala Ile Pro Thr Ala Glu Leu Ser 945 950 955 960 Asp Asp Tyr Ala Asn Gly Tyr Asn Ile Ser Lys Trp Ala Gly Glu Val 965 970 975 Leu Leu Arg Glu Ala His Asp Leu Cys Ser Leu Pro Val Ser Val Phe 980 985 990 Arg Pro Gly Met Ile Leu Ala His Ser Arg Tyr Val Gly Gln Leu Asn 995 1000 1005 Val Pro Asp Met Phe Thr Arg Leu Leu Tyr Ser Leu Ala Ile Thr 1010 1015 1020 Gly Val Ala Pro Ala Thr Phe Tyr Ala Glu Asn Leu Ser Gly Gly 1025 1030 1035 Arg Pro Val Ala Arg Tyr Glu Gly Ile Ala Val Asp Leu Leu Ala 1040 1045 1050 Asp Ala Ile Thr Ala Ile Gly Leu Ala Asn Arg Lys Gly Phe His 1055 1060 1065 Ala Tyr Asn Leu Ala Asn Pro His Asp Asp Gly Val Ser Leu Asp 1070 1075 1080 Thr Phe Val Asp Trp Met Ile Glu Ala Gly Cys Glu Ile Glu Arg 1085 1090 1095 Ile Asp Ser Tyr Ala Asp Trp Leu Ser Arg Phe Glu Thr Ala Met 1100 1105 1110 Asn Ala Leu Pro Glu Glu Ala Arg His Gln Ser Leu Leu Ala Ile 1115 1120 1125 Met Glu Pro Tyr Arg Arg Pro Gln Ala Ala Val Ala Lys Ser Phe 1130 1135 1140 Val Pro Val Glu Arg Phe Gln Ser Ala Ser Glu Ala Ala Gly His 1145 1150 1155 Ala Ile Pro Gly Ile Ser Ala Gly Leu Ile His Lys Tyr Val Asp 1160 1165 1170 Asp Leu Lys Gln Ile Gly Phe Leu Lys 1175 1180 <210> 217 <211> 1179 <212> PRT <213> Artificial Sequence <220> <223> Streptomyces scabrisporus <400> 217 Met Pro Glu Pro Gln Pro Asp His Asp Leu Ala Ala Arg Val Thr Ala 1 5 10 15 Leu Arg Ala His Asp Pro Glu Phe Ala Arg Ala Ile Pro Ser Ser Arg 20 25 30 Val Ala Asp Ala Ile Ala Gly Arg Asp Gly Ser Leu Val Gly Thr Ile 35 40 45 Val Ala Ala Met Arg Gly Tyr Ala Asp Arg Pro Ala Leu Ala Arg Arg 50 55 60 Ala Glu Arg Val Val Arg Asp Pro Asp Thr Gly Arg Val Thr Leu Glu 65 70 75 80 Leu Leu Pro Glu Phe Glu Met Phe Gly Tyr Ala Glu Val Trp Arg Arg 85 90 95 Val Val Ala Leu Ala Gly Ala Trp Ala Glu Cys Val Glu Gly Gly Leu 100 105 110 Arg Met Gly Asp Phe Val Ala Val Val Gly Phe Thr Gly Val Asp His 115 120 125 Ala Thr Ile Asp Leu Ala Cys Met Tyr Leu Gly Ala Val Ala Val Pro 130 135 140 Leu Pro Thr Gly Ser Pro Ala Ala Arg Leu Ala Pro Ile Val Ala Glu 145 150 155 160 Thr Ala Pro Arg Ile Leu Ala Ala Asp Leu Asp Ala Ile Asp Val Ala 165 170 175 Val Glu Thr Val Leu Arg Ser Ala Ser Val Glu Arg Leu Val Val Phe 180 185 190 Asp His Asp Ala Arg Val Asp Ala His Arg Glu Val Leu Arg Ala Ala 195 200 205 Ala Asp Lys Leu Ala Gly Arg Ala Glu Val Val Ser Leu Ala Asp Glu 210 215 220 Leu Arg Arg Gly Glu Glu Leu Pro Thr Val Leu Ala Arg Asp Asp Gly 225 230 235 240 Asp Pro Asp Arg Leu Val Gly Leu Ile Tyr Thr Ser Gly Ser Thr Gly 245 250 255 Thr Pro Lys Gly Ala Ile Tyr Thr Ala Ser Met Ile Thr Arg Met Trp 260 265 270 Gln Asn Gly Arg Gly Gly Met Thr Asn Ala Gly Ala Ser Pro Asp Thr 275 280 285 Pro Leu Pro Thr Ile Val Leu His Tyr Met Pro Met Ser His Val Asn 290 295 300 Gly Arg Ala Trp Leu Ile Ser Gly Leu Ser Ser Gly Gly Ile Gly Phe 305 310 315 320 Phe Ala Ala Arg Gly Asp Met Ser Thr Leu Phe Asp Asp Ile Arg Leu 325 330 335 Ser Arg Pro Thr Val Leu Ser Leu Val Pro Arg Ile Cys Asp Met Val 340 345 350 Arg Gln Arg Tyr Leu Leu Glu Val Asp Arg Val Thr Arg Ala Ala Thr 355 360 365 Glu Thr Pro Ala Asp Thr Asp Ala Ser Thr Ala Glu Thr Thr Ala Arg 370 375 380 Asp Arg Ile Arg Asp Gly Met Leu Gly Gly Arg Ile Val Ser Ala Leu 385 390 395 400 Cys Gly Ser Ala Pro Leu Ser Ala Ala Met His Thr Phe Met Ala Glu 405 410 415 Val Leu Gly Thr Arg Ile Val Asp Cys Tyr Gly Ser Thr Glu Thr Thr 420 425 430 Arg Ala Val Val Val Asp Gly Arg Val Arg Arg Pro Pro Val Leu Asp 435 440 445 Tyr Arg Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Gly Thr Asp Lys 450 455 460 Pro His Pro Arg Gly Glu Leu Arg Leu Lys Ser Val Gly Leu Val Pro 465 470 475 480 Gly Tyr Tyr Arg Gln Pro Glu Val Asp Ala Arg Ala Phe Asp Ala Asp 485 490 495 Gly Tyr Tyr Arg Thr Gly Asp Val Phe Ala Glu Leu Ala Pro Asp His 500 505 510 Leu Val Tyr Val Asp Arg Thr Asn Asn Val Val Lys Leu Ser Gln Gly 515 520 525 Glu Phe Val Ala Val Ser Arg Leu Glu Ala Leu Tyr Ala Thr Ser Pro 530 535 540 His Ile Ala Gln Ile His Val His Gly Ser Pro Glu Gln Ala Phe Leu 545 550 555 560 Leu Ala Val Val Val Pro Ala Arg Ser Gly Ala Ala Pro Ala Asp Asp 565 570 575 Asp Thr Met Arg Thr Arg Ile Leu Asp Ala Met Arg Glu Leu Ala Arg 580 585 590 Asp Ala Gly Leu Ala Ala Tyr Glu Ile Pro Tyr Asp Val Ile Leu Glu 595 600 605 Pro Glu Pro Phe Thr Val Ala Asn Gly Leu Leu Ser Gly Ile Gly Lys 610 615 620 Pro Leu Arg Pro Ala Leu Val Ala Arg Tyr Gly Ala Arg Leu Glu Gly 625 630 635 640 Leu Tyr Ala Asp Ile Ala Ala Gly Arg Ala Gly Arg Phe Ala Ala Leu 645 650 655 Arg Ala Ala Gly Pro His Ala Ala Pro Leu Asp Ala Val Leu Ala Ala 660 665 670 Val Gln Val Thr Leu Gly His Pro Ala Ser Ala Leu Arg Pro Asp Val 675 680 685 Gly Phe Ala Glu Leu Gly Gly Asp Ser Leu Ser Ala His Thr Phe Ala 690 695 700 Thr Val Leu Glu Gln Ile Phe Asp Val Glu Val Pro Val Gln Leu Val 705 710 715 720 Leu Gly Pro Thr Gly Thr Pro Ala Arg Ile Ala Glu His Leu Gly Ala 725 730 735 Ala Arg Glu Pro His Pro Ala Arg Pro Thr Phe Ala Ser Ile His Gly 740 745 750 Arg Asp Ala Val Glu Val Arg Ala Asp Glu Leu Thr Pro Asp Arg Phe 755 760 765 Met Asp Ala Gly Leu Leu Arg Arg Pro Ala Ser Pro Pro Ser Gly Ala 770 775 780 Pro Ala Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Tyr Leu Gly Ala 785 790 795 800 Phe Leu Ala Val Glu Trp Leu Arg Arg Val Ala Asp Thr Gly Gly Arg 805 810 815 Leu Ile Cys Pro Ala Arg Ala Asp Asp Asp Ala Ala Ala Arg Glu Arg 820 825 830 Val Val Arg Cys Leu Arg Ala Ala Ser Ala Asp Arg Pro Gly Trp Phe 835 840 845 Asp Thr Val Ala Ala Arg His Leu Glu Val Pro Ala Ala Asp Val Ser 850 855 860 Ala Pro Arg Leu Gly Leu Asp Ala Ser Thr Trp Arg Arg Leu Ala Ala 865 870 875 880 Glu Thr Asp Arg Ile Val His Ala Ala Ala Leu Val Asn His Val Leu 885 890 895 Pro Tyr Gly Arg Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Leu 900 905 910 Ile Glu Leu Ala Leu Thr Gly Pro Ala Lys Pro Phe Thr Phe Val Ser 915 920 925 Thr Ile Ala Ala Ala Leu Glu Pro Asp Gly Ser Val Leu Asp Glu Thr 930 935 940 Val Asp Val Arg Thr Ala Ala Pro Val Arg Arg Leu Asp Asp Ser Asp 945 950 955 960 Ala Asn Gly Tyr Ala Ala Gly Lys Trp Ala Ser Glu Val Leu Leu Arg 965 970 975 Ala Ala His Glu Arg Thr Gly Leu Pro Val Thr Val Phe Arg Pro Asp 980 985 990 Met Ile Leu Ala His Arg Arg Leu Pro Gly Val Val Asn Leu Pro Asp 995 1000 1005 Arg Phe Thr Arg Leu Ile Leu Ser Val Val Ala Thr Gly Met Ala 1010 1015 1020 Pro Leu Ser Phe His His Leu Asp Ala Asp Gly Arg Arg Arg Arg 1025 1030 1035 Ala His Tyr Ser Gly Leu Pro Val Asp Phe Thr Ala Ala Ala Ile 1040 1045 1050 Ala Ala Leu Gly Ala Asp Ala Ser Asp Gly Tyr Arg Thr Tyr His 1055 1060 1065 Ala Val Asn Ala Asn Asp Asp Gly Val Ser Leu Asp Glu Met Val 1070 1075 1080 Asp Trp Leu Ile Ala Ala Gly His Pro Ile Thr Arg Phe Ala Asp 1085 1090 1095 Tyr Glu Gln Trp Arg Met Arg Phe Glu Ala Ala Leu Arg Gly Leu 1100 1105 1110 Pro Glu Gln Arg Arg Arg Gly Ser Leu Leu Pro Leu Leu Pro Ala 1115 1120 1125 Tyr Ala Arg Pro Ser Glu Pro Arg Pro Ala Gly Ala Val Pro Asn 1130 1135 1140 Ala Arg Phe Thr Ala Ala Leu Ala Ala Val Gly Gly Glu Pro Val 1145 1150 1155 Pro Ser Ile Thr Pro Asp Tyr Leu Ala Lys Cys Val Ala Asp Leu 1160 1165 1170 Arg Gly Leu Asp Leu Leu 1175 <210> 218 <211> 1183 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium [tuberculosis] TKK-01-0051 <400> 218 Met Asp Ser Thr Ser Arg Thr Ala Ser Arg Leu Pro Ala Asp Pro Gly 1 5 10 15 Arg Tyr Ala Gly Ala Glu Ala Arg Val Ala Glu Leu Cys Ser Ser Asp 20 25 30 Ser Gln Val Arg Ala Ala Arg Pro Asp Pro Asp Thr Thr Ala Ala Leu 35 40 45 Gly Ile Arg Asp Leu Pro Leu Leu Asp Leu Val Arg Thr Val Met Ser 50 55 60 Arg Tyr Ala Asp Arg Pro Ala Leu Gly Glu Arg Val Arg Gln Pro Phe 65 70 75 80 Thr His Pro Gly Ser Gly Asn Thr Glu Leu Arg Leu Leu Pro Glu Phe 85 90 95 Ala Thr Ile Thr Tyr Arg Glu Val Trp Thr Arg Ala Glu Ala Ile Ala 100 105 110 Thr Ala Trp His His Met Arg Pro His Gly Leu Glu Ala Gly Asp Phe 115 120 125 Val Ala Ile Cys Gly Phe Thr Ser Ile Asp Tyr Thr Thr Val Asp Leu 130 135 140 Ala Cys Leu Arg Phe Gly Ala Val Ala Val Pro Met Gln Ser Ser Ala 145 150 155 160 Thr Val Glu Glu Leu Val Ala Leu Thr Ala Gln Val Gly Pro Lys Val 165 170 175 Val Ala Cys Ser Val Glu Thr Leu Pro Arg Val Val Glu Cys Val Arg 180 185 190 Arg Thr Pro Ser Val Gln Arg Val Ile Val Phe Asp Tyr His Pro Ala 195 200 205 Ala Asp Gln Gln Arg Asp Thr Val Asp Ala Ala Gly Ala Ala Leu Ala 210 215 220 Pro Gln Ala Val Asp Val Val Ser Leu Ala Asp Val Ile Ser Phe Gly 225 230 235 240 Arg Asp Leu Pro Ala Pro Pro Pro Ile Ala Asp Ala Ala Ala Ala Glu 245 250 255 Arg Leu Ser Val Leu Leu Phe Thr Ser Gly Ser Thr Gly Thr Pro Lys 260 265 270 Gly Ala Ile Tyr Thr Glu Arg Met Ala Ala Gly Phe Trp Arg Gly Ile 275 280 285 Pro Gln Thr Val Cys Thr His Pro Ala Ile Thr Leu Thr Tyr Leu Pro 290 295 300 Met Gly His Ala Ser Gly Arg Leu Val Leu Tyr Gly Val Leu Gly Ser 305 310 315 320 Gly Gly Thr Val Tyr Phe Thr Ala Gly Ser Asp Leu Ser Thr Met Phe 325 330 335 Glu Asp Val Thr Leu Val Arg Pro Thr Glu Ile Leu Phe Val Pro Arg 340 345 350 Phe Cys Glu Ala Val Leu Gln Arg Cys Arg Ala Glu Trp Gly Ala Gly 355 360 365 Gly Asp Thr Asp Arg Ala Cys Ala Asp Leu Gly Ala Leu Ser Gly Ala 370 375 380 Leu Thr Lys Ala Asp Ala Trp Pro Ser Leu Arg Glu Arg Leu Leu Gly 385 390 395 400 Gly Arg Leu Leu Ser Ala Trp Thr Gly Ser Ala Pro Leu Ser Thr Ala 405 410 415 Met Thr Asn Phe Met Glu Leu Leu Val Gly Leu Pro Leu Leu Gly Val 420 425 430 Phe Gly Ser Thr Glu Thr Gly Thr Ile Met Leu Asp Gly Val Val Ser 435 440 445 Arg Pro Pro Val Leu Asp Tyr Lys Leu Gln Asp Val Pro Glu Leu Gly 450 455 460 Tyr His Gly Thr Asp Glu Pro Phe Pro Arg Gly Glu Leu Leu Leu Lys 465 470 475 480 Ser Asp Ser Leu Phe Pro Gly Tyr Tyr Leu His Pro Glu Ala Thr Ala 485 490 495 Ser Ala Phe Asp Arg Asp Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala 500 505 510 Glu Ile Gly Pro Asp Arg Leu Ala Tyr Val Asp Arg Arg Asn Asn Val 515 520 525 Leu Lys Leu Ser Gln Gly Glu Phe Val Val Val Ser Arg Leu Glu Ala 530 535 540 Leu Phe Ala Thr Cys Pro Leu Leu Gln Gln Val Phe Leu Tyr Gly Asn 545 550 555 560 Ser Glu Arg Pro Tyr Leu Leu Ala Val Val Val Pro Thr Glu Asp Ala 565 570 575 Leu Gly Gly Ile Thr Pro Glu Glu Leu Arg Leu Arg Ile Ile Glu Ser 580 585 590 Met Arg Arg Thr Ala Lys Gly Ala Gly Leu Asn Ser Tyr Glu Ile Pro 595 600 605 Arg Asp Val Leu Ile Glu Pro Thr Pro Phe Ser Thr Ser Asn Gly Leu 610 615 620 Leu Thr Val Thr Arg Lys Leu Ala Arg Gln Arg Leu Val Asn His Tyr 625 630 635 640 Arg Arg Arg Leu Glu Arg Arg Tyr Ala Glu Leu Ala Glu Arg Glu Leu 645 650 655 Gln Gly Ser Arg Ala Pro Ser Thr Ser His Pro Pro Ser Ala Ala Leu 660 665 670 Asp Gly Val Val Gln Ala Ala Asn Leu Val Leu Gly Leu Cys Asp Ser 675 680 685 Ala Pro Ala Asp Ser Arg Phe Val Asp Ile Gly Gly Asp Ser Leu Ser 690 695 700 Ala Leu Leu Phe Ala Asn Arg Leu Thr Gln Ala Phe Gly Val Glu Val 705 710 715 720 Pro Val Ser Met Val Ile Gly Pro Asn Gly Ser Phe Arg Arg Leu Ala 725 730 735 Ala Tyr Ile Asp Asp Ala Arg Gly Thr Arg Ser Arg Arg Ala Thr Ala 740 745 750 Ala Thr Val His Gly Val Asp Ala Thr Ser Val Arg Ala Cys Asp Leu 755 760 765 Lys Leu Glu Lys Leu Leu Pro Ala Arg Thr Phe Glu Ala Ala Arg Glu 770 775 780 Leu Gln Phe Gln Pro Thr Glu Ile Lys Thr Val Leu Leu Thr Gly Ala 785 790 795 800 Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Gly Trp Leu Arg Arg Val 805 810 815 Ala Ala Asn Gly Gly Arg Leu Ile Cys Leu Val Arg Gly Glu Asn Ala 820 825 830 Glu Glu Ala Leu Arg Arg Leu Glu Ser Val Phe Glu Thr Asp Pro Asp 835 840 845 Leu Ala Thr Leu Phe Ala Glu His Ala Glu Gln His Leu Glu Ile Leu 850 855 860 Ser Gly Asp Ile Ser Glu His Gln Leu Gly Leu Ala Asp His Thr Trp 865 870 875 880 Gln Arg Leu Ser Glu Ser Val Asp Leu Ile Val His Ser Ala Ala Leu 885 890 895 Val Asn His Ala Leu Pro Tyr Ala Ala Leu Phe Gly Pro Asn Val Ala 900 905 910 Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Ser Ser Arg Ile Lys Pro 915 920 925 Ile Ser His Val Ser Thr Ala Ala Val Leu Pro Gly Leu Asp Ala Ser 930 935 940 Ala Glu Asp Thr Asp Ile Arg Ala Val Lys Ser Ser Cys Pro Leu Asp 945 950 955 960 Gly Gly Tyr Ala Asn Gly Tyr Val Thr Ser Lys Trp Ala Gly Glu Val 965 970 975 Leu Leu Arg Glu Ala His Glu Ala Phe Gln Leu Pro Val Ala Val Phe 980 985 990 Arg Pro Gly Met Val Leu Ala His Ser Gln Tyr Thr Gly Gln Leu Asn 995 1000 1005 Val Asp Asp Val Phe Thr Arg Leu Val Leu Ser Leu Leu Val Thr 1010 1015 1020 Gly Leu Ala Pro Arg Ser Phe His Pro Ala Thr Ser Arg Leu Phe 1025 1030 1035 Ala Ser Cys Asn Ala Leu Pro Ala Glu Val Val Ala Asp Ala Ile 1040 1045 1050 Thr Thr Ile Gly Glu Thr Ala Thr Gln Gly His Gln Ala Ile Asn 1055 1060 1065 Leu His Pro Pro His Ser Asp Thr Val Ser Leu Asp Val Ile Val 1070 1075 1080 Asp Trp Leu Ser Glu Thr Gly His Leu Ile Gln Arg Val Glu Asp 1085 1090 1095 Phe Asp Gln Trp Leu Ile Gln Phe Thr Ala Ala Leu His Ala Leu 1100 1105 1110 Pro Asp Gln Leu Arg Arg Arg Ser Ile Leu Pro Val Leu His Thr 1115 1120 1125 Leu Thr Asp Pro Ala Thr Pro Val Pro Pro Cys Ser His Ser Ala 1130 1135 1140 Arg Thr Arg Arg Ser Gln Pro Ala Asp Asn Pro Ser Gly Ala Glu 1145 1150 1155 Ser Gly Glu Val Ala Gly Val Ser Arg Ala Leu Val His Lys Tyr 1160 1165 1170 Ala Gln Asp Leu Arg Glu Leu His Leu Met 1175 1180 <210> 219 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium llatzerense <400> 219 Met Ser Asn Glu Glu Thr Ala Leu Thr Asp Glu Leu Thr Gln His Ile 1 5 10 15 Ala Asp Leu Cys Ala Thr Asp Pro Gln Leu Ala Ala Ala Arg Pro Leu 20 25 30 Ala Ala Val Gly Ala Ala Leu Asp Glu Pro Gly Ile Arg Leu Pro Asp 35 40 45 Met Ile Ser Ala Val Met Ala Ala Tyr Ala Asp Arg Pro Ala Leu Gly 50 55 60 Gln Arg Ala Val Glu Tyr Val Thr Asp Asp Ala Gly Arg Thr Val Ser 65 70 75 80 Arg Leu Leu Pro Arg Tyr Asp Thr Ile Thr Tyr Gly Glu Ala Trp Arg 85 90 95 Gln Ile Lys Ala Ile Gly Asn Ala Leu Leu Ala Gly Pro Asp Ala Val 100 105 110 Ala Ala Gly Asp Arg Val Ala Met Leu Gly Phe Thr Ser Ala Glu Phe 115 120 125 Thr Ile Ile Asp Thr Ala Leu Ala Arg Val Gly Val Val Ala Val Pro 130 135 140 Leu Gln Thr Ser Ala Pro Ala Glu Gln Leu Arg Pro Ile Leu Asp Glu 145 150 155 160 Thr Glu Pro Val Gly Leu Phe Ala Asp Val Lys Phe Leu Asp Glu Ala 165 170 175 Val Glu Leu Val Ser Gly Ser Gly Ala Ala Val Lys Arg Val Val Val 180 185 190 Phe Asp His His Ala Gln Val Asp Asp Asp Arg Ala Ala Val Glu Arg 195 200 205 Ala Ala Thr Gln Leu Ala Glu Arg Gly Val Val Val Glu Thr Leu Ala 210 215 220 Asp Leu Val Thr Arg Gly Thr Ala Leu Pro Thr Val Glu Pro Val Val 225 230 235 240 Ser Ala Asp Pro Asp Pro Leu Leu Val Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Thr Pro Lys Gly Ala Met Tyr Pro Glu Arg Leu Val Ala Asn 260 265 270 Ala Trp Arg Thr Gly Leu Thr His Gln Gln Pro Ala Leu Pro Ser Ile 275 280 285 Val Leu Ser Phe Leu Pro Met Ser His Met Met Gly Arg Gly Thr Val 290 295 300 Tyr Arg Thr Leu Ala His Gly Gly Thr Val Tyr Phe Ala Ala Lys Ser 305 310 315 320 Asp Leu Ser Thr Leu Leu Glu Asp Ile Ala Leu Val Arg Pro Thr Gln 325 330 335 Met Thr Phe Val Pro Arg Val Trp Glu Met Ile His Gln Glu Val Gln 340 345 350 Ser Glu Val Asp Arg Arg Ala Leu Asp Gly Val Ser Glu Gln Gln Val 355 360 365 Leu Asp Glu Arg Ser Val Ser Leu Ile Gly Gly Arg Gln Leu Val Ala 370 375 380 Met Thr Gly Ser Ala Pro Ile Ser Pro Glu Leu Lys Ala Trp Val Gln 385 390 395 400 Lys Phe Leu Gly Leu Glu Leu Met Glu Ala Tyr Gly Ser Thr Glu Ala 405 410 415 Gly Gly Val Met Ile Ser Gly His Leu Ser Arg Pro Pro Val Leu Asp 420 425 430 Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Leu Ser Thr Asp Arg 435 440 445 Pro His Pro Arg Gly Glu Leu Leu Leu Lys Ser Thr Asp Leu Ile Pro 450 455 460 Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Val Asp 465 470 475 480 Gly Phe Tyr Arg Thr Gly Asp Ile Val Ala Glu Leu Gly Pro Asp His 485 490 495 Leu Gln Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly 500 505 510 Glu Phe Val Thr Val Ser Lys Leu Glu Ala Ala Phe Gly Thr Ser Pro 515 520 525 Leu Ile Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ser Arg Ser Tyr Leu 530 535 540 Leu Ala Val Ile Val Pro Thr Ser Asp Ala Leu Ala Gly Val Ser Gly 545 550 555 560 Ala Glu Ala Leu Arg Pro Glu Leu Ala Asp Ala Leu Gln Thr Val Ala 565 570 575 Arg Glu Ser Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile Ile 580 585 590 Glu Thr Glu Pro Phe Ser Leu Glu Asn Gly Leu Leu Thr Gly Val Arg 595 600 605 Lys Leu Ala Trp Pro Lys Leu Lys Ala Arg Tyr Gly Ala Glu Leu Glu 610 615 620 Gln Leu Tyr Thr Glu Leu Ala Glu Gly Gln Ala Ala Glu Leu Arg Ala 625 630 635 640 Leu Arg Ser Leu Arg Ala Ser Asp Ala Pro Val Leu Glu Thr Val Leu 645 650 655 Arg Ala Val Gly Ala Thr Leu Gly Ala Ala Ser Ser Asp Val Ala Gly 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Gly Asn Leu Leu Glu Glu Ile Phe Glu Val Glu Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Thr Asp Leu Ala Gly Val Ala Ala Tyr Val 705 710 715 720 Glu Gly Glu Arg Ala Pro Gly Ser Lys Arg Pro Thr Phe Ser Thr Val 725 730 735 His Gly Arg Gly Ala Thr Glu Ala Arg Ala Ala Asp Leu Thr Leu Asp 740 745 750 Lys Phe Ile Asp Ala Ala Thr Leu Ala Ala Ala Pro Ser Leu Pro Gly 755 760 765 Pro Val Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Leu Val 785 790 795 800 Asp Gly Lys Val Ile Cys Leu Val Arg Gly Lys Ser Asp Ala Asp Ala 805 810 815 Arg Ala Arg Leu Asp Ala Thr Phe Asp Ser Gly Asp Pro Lys Leu Leu 820 825 830 Gln His Tyr Arg Ser Leu Ser Asp His Leu Glu Val Ile Ala Gly Asp 835 840 845 Lys Gly Glu Ala Asn Leu Gly Leu Pro Gln Glu Val Trp Gln Arg Leu 850 855 860 Ala Asp Thr Val Asp Phe Ile Val Asp Pro Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala Leu Gly Thr Ala 885 890 895 Glu Leu Ile Arg Ile Ala Leu Thr Thr Arg Ile Lys Pro Phe Ala Tyr 900 905 910 Val Ser Thr Ile Ala Val Gly Gly Gly Val Ala Pro Gly Gln Phe Val 915 920 925 Glu Asp Ala Asp Val Arg Val Met Ser Ala Val Arg Ser Val Asp Asp 930 935 940 Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Glu Ala Asn Asp Leu Cys Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Met Met Phe Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Tyr Ser Phe Tyr Glu Leu Ala Thr Asp Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Val Ser Glu Ser 1025 1030 1035 Ile Ser Thr Leu Ala Val Gln Val Ala Ala Gly Glu Ser Asp Ser 1040 1045 1050 Thr Phe Glu Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Ile 1055 1060 1065 Gly Met Asp Glu Phe Val Asp Trp Leu Ile Glu Ala Gly Tyr Ser 1070 1075 1080 Ile Ala Arg Val Asp Asp Tyr Ala Asp Trp Leu Ala Arg Phe Glu 1085 1090 1095 Thr Gly Leu Arg Gly Leu Pro Asp Arg Gln Arg Gln Ala Ser Leu 1100 1105 1110 Leu Pro Leu Leu His Asn Tyr Gln Gln Pro Ser Tyr Pro Val Pro 1115 1120 1125 Gly Ser Ile Ala Pro Val Glu Arg Phe Arg Ala Ala Val Gln Asn 1130 1135 1140 Ala Lys Val Gly Ala Asp Lys Asp Ile Pro His Ile Gly Ala Pro 1145 1150 1155 Val Ile Val Lys Tyr Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 220 <211> 1175 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. 06-469-3-2 <400> 220 Met Thr His Thr Leu Ala Val Asp Ser Glu Arg Glu Arg Glu Ile Arg 1 5 10 15 Gly Arg Asp Arg Phe Thr Glu Leu His Arg Ile Asp Asp Glu Phe Arg 20 25 30 Ala Ala Glu Pro Asp Ser Ala Val Ala Asp Ala Ala Gln Glu Leu Ser 35 40 45 Pro Asn Leu Ala Arg Val Val Ala Glu Ile Met Thr Arg Tyr Ser Asp 50 55 60 Arg Pro Ala Leu Gly Arg Arg Ala Arg Glu Ile Ala Arg Val Asp Asp 65 70 75 80 Thr Thr Thr Leu Arg Leu Leu Pro Arg Phe Glu Thr Val Thr Tyr Gly 85 90 95 Arg Ala Trp Asn Asp Ala Gly Ala Leu Ala Ser Ala Leu Thr His Asp 100 105 110 Ala Phe Gly Ile Ala Ser Gly Asp Phe Phe Ala Thr Leu Gly Phe Ala 115 120 125 Ser Ala Asp Tyr Val Val Ala Glu Leu Ala Thr Ile Arg Leu Gly Ala 130 135 140 Ile Ala Val Pro Leu Gln Ala Gly Ala Thr Ala Gly Gln Leu Ser Ala 145 150 155 160 Ile Ala Ala Glu Val Glu Pro Val Val Leu Ala Ala Asp Val Asp Asn 165 170 175 Leu Ser Val Ala Val Gln Val Ala Thr His Cys Arg Ser Ile Arg Arg 180 185 190 Ile Val Val Leu Asp Tyr Asp Gly Ala Ile Asp Ala His Thr Gln Ile 195 200 205 Met Glu Thr Ala Arg Ser Val Ala Glu Gln Ala Gly Val Phe Val Arg 210 215 220 Pro Leu Thr Glu Leu Val Arg Asp Gly Ala Gln Leu Pro Ser Val Pro 225 230 235 240 Leu Pro Asp Ala Glu Asp Pro Asp Arg Leu Ala Thr Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met His Thr Glu Arg Ile 260 265 270 Val Cys Gly Ala Trp Thr Gly Ala Trp His His Thr Gly Ala Ser Ser 275 280 285 Glu Ser Thr Asp Gly Pro Ala Phe Pro Val Ile Thr Leu Asp Tyr Leu 290 295 300 Pro Met Ser His Leu Ala Gly Arg Gly Leu Val Phe Ser Thr Leu Ala 305 310 315 320 Ala Gly Gly Thr Val His Phe Ala Gly Ala Ser Asp Leu Ser Thr Leu 325 330 335 Phe Glu Asp Phe Ala Leu Ala Arg Pro Thr Met Ala Leu Leu Ile Pro 340 345 350 Arg Val Cys Glu Met Ile Arg His Asn Val Leu Ala Glu Ile Asp Arg 355 360 365 Glu Thr Glu Arg Thr Ala Gly Gly Asp Ala Asp Arg Thr Arg Arg Glu 370 375 380 Val Leu Glu Arg Asn Arg Ile Glu Gln Phe Gly Gly Arg Val Leu Ala 385 390 395 400 Ala Met Val Gly Thr Ala Pro Ile Ala Asp Glu Val Lys Asp Phe Val 405 410 415 Ser Glu Leu Leu Asp Ile Arg Val Arg Asp Asn Tyr Gly Ser Thr Glu 420 425 430 Ala Gly Met Val Leu His Asp Gly Val Val Gln Arg Pro Pro Val Ile 435 440 445 Glu Tyr Lys Leu Asp Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp 450 455 460 Thr Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Thr Ser Ile Ile 465 470 475 480 Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Ser 485 490 495 Glu Gly Phe Tyr Arg Thr Gly Asp Val Val Ala Glu Ile Glu Pro Asp 500 505 510 Arg Leu Ala Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ala Gln 515 520 525 Gly Glu Phe Val Ala Leu Ala Arg Leu Glu Ala Leu Phe Gly Thr Ser 530 535 540 Glu Leu Val Asn Gln Ile Phe Val Tyr Gly Asn Ser Gln Arg Ala Tyr 545 550 555 560 Leu Leu Ala Val Val Val Pro Ala Asp Pro Asp Thr Thr Ala Gly Ser 565 570 575 Val Ile Glu Ser Leu Gln Gln Ile Ala Arg Thr Glu Ala Leu Asn Ser 580 585 590 Tyr Glu Ile Pro Arg Glu Val Val Ile Glu His Asp Pro Phe Thr Gln 595 600 605 Glu Asn Gly Leu Leu Ser Gly Ala Gly Lys Gln Leu Arg Pro Lys Leu 610 615 620 Val Glu Arg Tyr Gly Glu Glu Leu Glu Arg Arg Tyr Ala Glu Leu Glu 625 630 635 640 Thr Gly Gln Asn Asp Arg Leu Arg Glu Leu Arg Arg Thr Gly Ala Asp 645 650 655 Ala Pro Val Leu Thr Thr Val Gly Asp Ala Ala Gln Ala Leu Leu Gly 660 665 670 Cys Ala Gly Ser Asp Ile Arg Pro Asp Ala His Phe Ser Asp Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Thr Leu Leu Arg Glu Ile 690 695 700 Tyr Asp Val Asp Val Pro Val Gly Val Ile Thr Gly Pro Ala Met Asp 705 710 715 720 Leu Ala Ala Leu Ala Glu Tyr Ile Ser Ser Ala Arg Asp Asn Asp Ser 725 730 735 Asp Thr Ala Thr Phe Ala Ser Val His Gly Arg Gly Ala Ala Val Ala 740 745 750 Arg Ala Ser Asp Leu Arg Leu Ser Ala Phe Leu Asp Asp Ala Leu Leu 755 760 765 Asp Ala Ala His Arg Ile Ala Gly Pro Arg Glu Arg Thr Gly Thr Val 770 775 780 Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu 785 790 795 800 Trp Leu Gly Arg Met Ala Glu Thr Gly Gly Lys Val Ile Cys Leu Val 805 810 815 Arg Gly Arg Ser Asp Ser Asp Ala Arg Ala Arg Leu Asp Ala Ala Phe 820 825 830 Asp Ser Gly Asp Ala Arg Leu Ser Glu Arg Tyr Arg Thr Leu Ala Asp 835 840 845 Ala Ala Leu Glu Val Val Ala Gly Asp Leu Gly Thr Pro His Phe Gly 850 855 860 Leu Asp Arg Asp Val Phe Glu Ala Leu Ala Glu Arg Val Asp Arg Ile 865 870 875 880 Val His Pro Ala Ala Leu Val Asn His Ala Leu Pro Tyr Glu His Leu 885 890 895 Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Arg Leu Ala Leu 900 905 910 Thr Asp His Val Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala 915 920 925 Ala Gly Val Glu Glu Phe Arg Glu Asn Gly Asp Ile Arg Val Asp Ser 930 935 940 Pro Ser Arg Ala Val Asp Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser 945 950 955 960 Lys Trp Ala Gly Glu Val Leu Leu Arg Asn Ala Phe Asp Glu Phe Gly 965 970 975 Leu Pro Val Ser Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Thr 980 985 990 Trp Thr Gly Gln Leu Asn Val Pro Asp Val Phe Thr Arg Leu Ile Leu 995 1000 1005 Ser Val Val Ala Thr Gly Leu Ala Pro His Thr Phe Tyr Ala Thr 1010 1015 1020 Asp Thr Gly Ala Pro Thr Asp Glu Lys Gly Arg Pro Leu Ala His 1025 1030 1035 Tyr Asp Gly Leu Pro Ala Asp Phe Ser Ala Ser Ala Ile Thr Ser 1040 1045 1050 Ile Ala Gly Gly Asp Thr Ser Gly Tyr Arg Thr Phe Asp Ile Leu 1055 1060 1065 Asn Pro His Asp Asp Asp Ile Ser Leu Asp Thr Phe Val Asp Trp 1070 1075 1080 Ile Arg Asp Ala Gly Arg Asp Ile Glu Ile Val Glu Asn Tyr Asp 1085 1090 1095 Glu Trp Phe Glu Arg Phe Asn Ala Ala Val Glu Ala Leu Pro Glu 1100 1105 1110 Lys Gln Arg Ser His Ser Leu Leu Pro Leu Ile Asp Ser Tyr Ala 1115 1120 1125 Arg Pro Gln His Pro Ser Ser Gly Ala Ile Leu Pro Ala Asp Glu 1130 1135 1140 Phe Ala Ser Ala Val Gly Asp Ile Pro His Leu Gly Arg Glu Leu 1145 1150 1155 Ile Glu Lys Tyr Leu Ser Asp Leu Leu Ala Leu Glu Leu Val Ser 1160 1165 1170 Thr Arg 1175 <210> 221 <211> 1148 <212> PRT <213> Artificial Sequence <220> <223> Gordonia sputi NBRC 100414 <400> 221 Met Ser Thr His Leu Ser Ala Asp Pro Ala Ala Ala Val Ser Ala Arg 1 5 10 15 His Pro Asp Ser Asp Val Ala Ala Arg Leu Arg Glu Glu Thr Ser Val 20 25 30 Glu Gly Ala Leu Arg Val Leu Phe Glu Gly Tyr Ala Asp Arg Pro Ala 35 40 45 Leu Gly Phe Arg Asp Ala Glu His Glu Ser Arg Trp Ser Thr Ser Ser 50 55 60 Phe Arg Glu Val Gly Asn Arg Val Ala Ala Phe Ala Ser Leu Leu Arg 65 70 75 80 Asp Ala Ala Gly Val Arg Pro Gly Asp Arg Ile Ala Thr Leu Gly Phe 85 90 95 Thr Ser Ala Asp Tyr Thr Ala Val Ser Leu Ala Ile Leu Gly Pro Leu 100 105 110 His Ala Val Glu Val Pro Leu Gln Ser Gly Ala Ala Asp Ser Val Phe 115 120 125 Ala Asp Ile Leu Asp Glu Thr Glu Ala Lys Val Leu Ala Val Ser Thr 130 135 140 Asn Ser Leu Ser Arg Val Thr Thr Leu Ile Glu Asn Gly Thr Arg Ala 145 150 155 160 Asp Leu Ala His Leu Val Val Phe Asp Val Ser Glu Ala Ala Leu Asp 165 170 175 Ala Val Glu Arg Ala Arg Ala Leu Leu Glu Pro Leu Gly Ile Thr Val 180 185 190 His His Ala His Phe Asp Ala Glu Ser Ser Ile Thr Asp Asp Ala Glu 195 200 205 Glu Ala Leu Gln Val Ser Gly Asp Ala Gln Pro Asp Asp Leu Ala Leu 210 215 220 Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr 225 230 235 240 Thr Gln Asp Ala Val Leu Arg Leu Ile Arg Gln Gly Phe Gly Leu Glu 245 250 255 Thr Asp Cys Ala Thr Gly Glu Asp Asp Ala Ser Glu Asp His Ala Trp 260 265 270 Val Thr Leu Asn Phe Leu Pro Met Ser His Val Met Gly Arg Ala Thr 275 280 285 Leu Met Arg Thr Leu Gly Asn Gly Gly Thr Ala Tyr Phe Thr Ala Arg 290 295 300 Pro Asp Leu Ser Glu Leu Leu Asp Asp Leu Ala Ala Val Ala Pro Thr 305 310 315 320 Glu Leu His Phe Val Pro Arg Ile Trp Glu Met Leu His Gln Gln Tyr 325 330 335 Leu Ser Glu Ile Glu Gly Val Glu Ser Asp Ser His Ala Asp Ala Leu 340 345 350 Ala Ala Met Arg Arg Arg Tyr Phe Glu Arg Ala Gln Leu Ala Val Thr 355 360 365 Gly Ser Ala Pro Ile Ser Pro Glu Val Val Asp Phe Val Glu Ser Met 370 375 380 Leu Asp Ala Pro Leu Val Glu Gly Tyr Gly Ser Thr Glu Ala Gly Gly 385 390 395 400 Val Ile Arg Asp Gly Ala Val Ile Arg Pro Pro Val Val Asp Tyr Lys 405 410 415 Leu Val Asp Val Pro Glu Leu Gly Tyr Arg Thr Thr Asp Thr Pro His 420 425 430 Pro Arg Gly Glu Leu Leu Val Lys Thr Thr Asp Ile Phe Ala Gly Tyr 435 440 445 Tyr Arg Arg Pro Glu Leu Thr Ala Glu Met Phe Asp Asp Asp Gly Phe 450 455 460 Tyr Arg Thr Gly Asp Val Met Ala Glu Thr Gly Pro Asp Gln Leu Val 465 470 475 480 Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe 485 490 495 Val Thr Val Ala Arg Val Glu Ser Ala Leu Thr Ser Pro Pro Ile Arg 500 505 510 Gln Ile Tyr Val Tyr Gly Asn Ser Ala Arg Pro Tyr Leu Leu Ala Val 515 520 525 Val Val Pro Thr Asp Asp Ala Val Asp Gly Ala Ser Asp Asp Gly Glu 530 535 540 Leu His Ala Thr Leu Leu Arg Ala Val Arg Asp Ile Gly Glu Arg Asn 545 550 555 560 Gly Leu Ala Pro Val Glu Ile Pro Arg Asp Ile Ile Val Glu Arg Thr 565 570 575 Ala Phe Ser Glu Ala Asn Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala 580 585 590 Arg Pro Arg Leu Lys Glu Ala Tyr Gly Pro Ala Leu Glu Asp Leu Tyr 595 600 605 Leu His Leu Ala Asn Ala Arg Ala Asp Arg Leu Arg Asp Ala Arg Val 610 615 620 Ser Ala Ala Ser Arg Pro Thr Leu Asp Val Leu Ile Asp Ile Val Ser 625 630 635 640 Ala Thr Leu Asp Leu Ala Gly Asn Glu Val Thr Ala His Ser Arg Phe 645 650 655 Thr Asp Leu Gly Gly Asp Ser Leu Thr Ala Val Thr Leu Gly Asn Thr 660 665 670 Leu Arg Asp Val Phe Asp Ala Gln Val Ser Val Gly Val Leu Thr Ser 675 680 685 Pro Ser Ser Asp Leu Ala Ala Ile Ala Asp Tyr Ile Asp Gly Arg Glu 690 695 700 Gly Glu Ala Arg Pro Thr Ala Asp Thr Val His Ala Asp Gln Gln His 705 710 715 720 Leu Arg Ala Asp Glu Leu Thr Val Asp Ala Phe Leu Asp Glu Ala Thr 725 730 735 Leu Ala Gly Ala Ser Thr Val Pro Pro Ala Ala Glu Thr Val Arg Glu 740 745 750 Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Thr Val 755 760 765 Glu Trp Leu Arg Arg Val Ala Cys Val Asp Gly His Val Thr Cys Leu 770 775 780 Val Arg Ala Ser Asp Asp Asp Thr Ala Arg Arg Arg Leu Asp Ala Val 785 790 795 800 Phe Asp Val Gly Asp Gly Pro Leu Arg Ser Asp Tyr Leu Arg Leu Ala 805 810 815 Pro Asp His Leu Thr Val Leu Ala Gly Asp Lys Asp Ser Pro Ser Leu 820 825 830 Gly Leu Asp Asp Ala Val Trp Asn Arg Leu Ala Ala Asp Val Asp Leu 835 840 845 Ile Val Asp Pro Ala Ala Leu Val Asn His Leu Leu Pro Tyr Arg Glu 850 855 860 Leu Phe Gly Pro Asn Val Ser Gly Thr Ala Glu Leu Ile Arg Leu Ala 865 870 875 880 Leu Thr Thr Thr Arg Lys Pro Tyr Val Tyr Ile Ser Thr Val Gly Val 885 890 895 Ala Asp Gln Val Gly Ser Ala Glu Leu Val Glu Asp Lys Asp Ile Arg 900 905 910 Glu Leu Asn Ala Thr Arg Glu Val His Glu Gly Tyr Ala Asn Gly Tyr 915 920 925 Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Ala Asp Ala His Asp 930 935 940 Arg Phe Gly Leu Pro Val Ser Val Phe Arg Cys Asp Met Ile Val Ala 945 950 955 960 Asp Asp Ser Asp Leu Gly Gln Leu Asn Leu Pro Asp Met Phe Thr Arg 965 970 975 Leu Leu Met Ser Val Leu Ala Thr Gly Leu Ala Pro Gln Ser Phe Tyr 980 985 990 Arg Leu Asp Ala Asp Gly Gly Arg Gly Thr Ala His Tyr Asp Ala Leu 995 1000 1005 Pro Val Asp Phe Leu Ala Ala Ala Ile Ser Thr Leu Ala Val Ser 1010 1015 1020 Asp Gly His Val Thr Tyr Asn Ala Val Asn Pro His Ser Asp Gly 1025 1030 1035 Ile Asp Leu Asp Thr Phe Val Gly Trp Leu Ile Glu Ser Gly Glu 1040 1045 1050 Glu Ile Ala Leu Val Asp Glu Tyr Asp His Trp Tyr Arg Leu Phe 1055 1060 1065 Ser Asp Ala Leu Val Asp Leu Pro Glu Lys Gln Arg Arg His Ser 1070 1075 1080 Leu Ile Pro Leu Leu His Asn Tyr Val Arg Pro Val Glu Pro Val 1085 1090 1095 Asp Ala Gly Val Val Asn Ala Pro Leu Phe Ala Glu Ala Val Arg 1100 1105 1110 Ser Gly Gln Val Thr Thr Ala Thr Ala Glu Tyr Ala Asp Ile Pro 1115 1120 1125 His Ile Thr Ser Gln Val Ile Ala Asn Tyr Ala Arg Arg Leu Arg 1130 1135 1140 Thr Leu Gly Val Val 1145 <210> 222 <211> 1172 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. abscessus <400> 222 Met Ser Ile Asp His Ala Glu Ser Ala Thr Asp Glu Leu Ala Arg Arg 1 5 10 15 Ile Ala Asp Leu Ala Ala Asn Asp Pro Gln Phe Ala Ala Ala Val Pro 20 25 30 Leu Leu Ser Val Ala Gln Ser Val Glu Lys Pro Gly Met Arg Leu Pro 35 40 45 Glu Ile Val Lys Thr Val Leu Glu Gly Tyr Ala Asp Arg Thr Ala Leu 50 55 60 Gly Gln Arg Ala Val Glu Phe Val Thr Glu Asn Gly Arg Thr Val Ala 65 70 75 80 Arg Leu Leu Pro Lys Tyr Asp Thr Ile Thr Tyr Gly Glu Leu Trp Asp 85 90 95 Arg Ile Arg Ala Val Ala Ala Ala Leu His Ala Asp Gly Val Lys Ala 100 105 110 Gly Asp Arg Val Ala Ile Leu Gly Phe Thr Ser Thr Asp Tyr Thr Val 115 120 125 Ile Asp Thr Ala Leu Gly Gln Ile Gly Ala Val Ser Val Pro Leu Gln 130 135 140 Thr Ser Ser Ala Ser Ser Ser Leu Leu Pro Ile Val Ala Glu Thr Glu 145 150 155 160 Pro Val Leu Ile Ala Val Ser Ala Asp Tyr Val Ala Asp Ala Val Glu 165 170 175 Leu Ala Val Gly Gly Pro Ala Pro Ala Arg Phe Leu Val Phe Asp His 180 185 190 His Val Glu Val Asp Asp Glu Arg Asp Ala Ile Asp Arg Ala Arg Glu 195 200 205 Ala Leu Ala Gly Leu Asn Val Thr Val Glu Thr Phe Gly Asp Val Leu 210 215 220 Ser Arg Gly Arg Glu Leu Pro Asp Ala Pro Thr Pro Val Phe Asp Glu 225 230 235 240 Ala Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala 245 250 255 Pro Lys Gly Ala Met Tyr Pro Glu Ser Asn Met Thr Ser Phe Trp Arg 260 265 270 Arg Ala Ser Thr Ala Trp Phe Gly Pro Ser Glu Ala Ser Ile Asn Leu 275 280 285 Ala Phe Met Pro Met Ser His Val Met Gly Arg Gly Ile Leu Tyr Ser 290 295 300 Ser Leu Ala Asn Gly Gly Ile Val Tyr Phe Ala Ala Lys Ser Asp Leu 305 310 315 320 Ser Thr Leu Leu Glu Asp Phe Ala Leu Ala Arg Pro Thr Glu Leu Asn 325 330 335 Leu Val Pro Arg Val Trp Glu Met Leu Tyr Leu Glu Phe Gln Ser Arg 340 345 350 Val Asp Lys Leu Val Pro Ala Gly Ala Gly Glu Ala Glu Arg Asp Asp 355 360 365 Ile Glu Gln Gln Val Met Ala Asp Met Arg Gln Asn Leu Val Gly Gly 370 375 380 Arg Tyr Ile Lys Ala Met Thr Gly Ser Ala Pro Ile Thr Asp Glu Leu 385 390 395 400 Lys Ala Trp Val Glu Lys Phe Leu Gly Ile His Leu Leu Glu Gly Tyr 405 410 415 Gly Ser Thr Glu Ala Gly Met Val Phe Phe Asp Gly Val Ile Gln Arg 420 425 430 Pro Pro Thr Leu Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr 435 440 445 Tyr Leu Thr Asp Gln Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Thr 450 455 460 Gln Tyr Leu Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Val Thr Ala Ser 465 470 475 480 Val Phe Asp Glu Asp Gly Phe Tyr Arg Thr Gly Asp Val Val Ala Glu 485 490 495 Ile Gly Pro Asp Gln Ile Gln Tyr Val Asp Arg Arg Asn Asn Val Leu 500 505 510 Lys Leu Ala Gln Gly Glu Phe Val Thr Leu Ala Lys Leu Glu Ala Ala 515 520 525 Phe Ser Asn Asn Ser Pro Leu Val Arg Gln Ile Tyr Val Tyr Gly Asn 530 535 540 Ser Ala Gln Pro Tyr Leu Leu Ala Val Val Val Pro Thr Glu Asp Ala 545 550 555 560 Leu Ala Arg Trp Asp Ser Ala Glu Leu Lys Gln Arg Ile Ser Asp Ser 565 570 575 Leu Gln Glu Val Ala Lys Ala Ala Glu Leu Gln Ser Tyr Glu Ile Pro 580 585 590 Arg Asp Phe Ile Ile Glu Thr Glu Pro Phe Ser Leu Glu Asn Gly Leu 595 600 605 Leu Thr Gly Ile Arg Lys Leu Ala Trp Pro Lys Leu Lys Ala His Tyr 610 615 620 Gly Pro Ala Leu Glu Asp Leu Tyr Val Ser Leu Ala Ala Gly Gln Ala 625 630 635 640 Asp Glu Leu Arg Gln Leu Arg Gln His Gly Ala Glu Gly Pro Ala Leu 645 650 655 Pro Thr Val Ile Arg Ala Ala Ser Ala Leu Leu Gly Ala Ser Gly Glu 660 665 670 Val Ser Ala Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser 675 680 685 Ala Leu Thr Phe Gly Asn Leu Leu Glu Glu Ile Phe Gly Val Glu Val 690 695 700 Gln Val Gly Ile Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Leu Ala 705 710 715 720 Ala Tyr Ile Glu Asn Glu Arg Ser Gly Gly Ala Lys Arg Pro Ser Phe 725 730 735 Ser Ser Val His Gly Lys Asn Ala Val Glu Val Arg Ala Ala Asp Leu 740 745 750 Thr Leu Asp Lys Phe Leu Asp Ala Ala Thr Leu Ala Ala Ala Pro Ser 755 760 765 Leu Pro Gly Pro Ala Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ala 770 775 780 Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met 785 790 795 800 Asp Leu Val Asp Gly Lys Val Ile Ala Leu Val Arg Ala Lys Ser Asp 805 810 815 Asp Glu Ala Arg Ala Arg Leu Asp Ala Thr Phe Asp Ser Arg Asp Pro 820 825 830 Lys Leu Leu Ala His Tyr Gln Ala Leu Ala Ala Asp His Leu Glu Val 835 840 845 Ile Ala Gly Asp Lys Gly Asp Glu Asn Leu Gly Leu Ser Gln Glu Val 850 855 860 Trp Gln Arg Leu Ala Asp Glu Val Asp Val Ile Val Asp Pro Ala Ala 865 870 875 880 Leu Val Asn His Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala 885 890 895 Leu Gly Thr Ala Glu Leu Ile Arg Ile Ala Leu Thr Thr Arg Gln Lys 900 905 910 Pro Tyr Ile Tyr Val Ser Thr Ile Gly Val Gly Asp Gln Leu Thr Pro 915 920 925 Gly Thr Phe Thr Glu Glu Ala Asp Val Arg Val Met Ser Pro Val Arg 930 935 940 Ala Val His Asp Gly Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala 945 950 955 960 Gly Glu Val Leu Leu Arg Glu Ala Asn Asp Leu Cys Gly Leu Pro Val 965 970 975 Ser Val Phe Arg Cys Asp Met Ile Leu Ala Asp Thr Ser Tyr Ala Gly 980 985 990 Gln Leu Asn Leu Pro Asp Met Phe Thr Arg Met Met Phe Ser Leu Val 995 1000 1005 Ala Thr Gly Ile Ala Pro Tyr Ser Phe Tyr Glu Arg Asp Ala Glu 1010 1015 1020 Gly Lys Arg Gln Ala Ala His Tyr Asp Gly Leu Pro Val Glu Phe 1025 1030 1035 Ile Ala Glu Ala Ile Asp Thr Leu Gly Val Arg Pro Ala Gly Glu 1040 1045 1050 Phe Val Thr Tyr His Val Met Asn Pro His Ser Asp Gly Leu Gly 1055 1060 1065 Met Asp Glu Phe Val Asp Trp Leu Ile Glu Ala Gly Tyr Ser Ile 1070 1075 1080 Ala Arg Val Asp Asp Tyr Ala Glu Trp Leu Ala Arg Phe Glu Thr 1085 1090 1095 Thr Leu Arg Ala Leu Pro Asp Arg Gln Arg Gln Ala Ser Leu Leu 1100 1105 1110 Pro Leu Leu His Asn Tyr Gln Lys Pro Glu His Pro His Asn Gly 1115 1120 1125 Ser Ile Ala Pro Val Val Val Phe Arg Glu Ala Val Gln Glu Ala 1130 1135 1140 Lys Leu Gly Pro Asp Lys Asp Ile Pro His Val Thr Ala Pro Val 1145 1150 1155 Ile Val Lys Tyr Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 223 <211> 1165 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. <400> 223 Met Phe Ala Glu Asp Asp Gln Phe Arg Gln Ala Arg Pro Asp Val Ala 1 5 10 15 Val Arg Ala Ala Ala Arg Gln Pro Gly Leu Arg Leu Pro Gln Val Ile 20 25 30 Glu Thr Leu Val Arg Gly Tyr Ala Asp Arg Pro Ala Met Gly Trp Arg 35 40 45 Ala Arg Gly Leu Thr Asn Asp Pro Glu Thr Gly Arg Thr Ile Gly Thr 50 55 60 Leu Leu Pro Arg Phe Glu Thr Ile Thr Tyr Arg Glu Leu Trp Ser Asn 65 70 75 80 Val Ala Ala Ile Ala Ala Ala Trp Arg Gly Asp Pro Glu Asn Pro Ala 85 90 95 Ala Ala Gly Asp Phe Val Ala Thr Val Gly Phe Ala Ser Val Asp Tyr 100 105 110 Leu Thr Ile Asp Leu Val Ser Gly Tyr Leu Gly Leu Val Ala Val Pro 115 120 125 Leu Gln His Asn Thr Thr Ala Ser Arg Leu Gln Pro Ile Leu Ala Glu 130 135 140 Val Gln Pro Gln Ile Leu Ala Ala Gly Ala Asp Tyr Leu Asp Leu Ala 145 150 155 160 Val Asp Ala Ala Leu Gly Ser Asp Ser Val Arg Arg Leu Val Val Phe 165 170 175 Asp Tyr Arg Pro Glu Ile Asp Asp Gln Arg Glu Ser Leu Ala Arg Ala 180 185 190 Gln Gln Lys Leu Ala Ser Ala Gly Met Thr Val His Ile Glu Thr Leu 195 200 205 Asp Asp Val Ile Thr Arg Gly Arg Thr Leu Pro Pro Glu Pro Thr Tyr 210 215 220 Thr Gly Gly Asp Asp Gln Arg Leu Ala Met Ile Met Tyr Thr Ser Gly 225 230 235 240 Ser Thr Gly Leu Pro Lys Gly Ala Met Tyr Ser Glu Arg Met Val Ala 245 250 255 Lys Ile Trp Thr Asn Glu Leu Met Pro Asp Arg Glu Asp Val Pro Val 260 265 270 Phe Asn Val Asn Phe Met Pro Leu Asn His Leu Gly Gly Arg Ile Pro 275 280 285 Leu Ser Thr Ala Phe Gln Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu 290 295 300 Ser Asp Leu Ser Thr Leu Phe Glu Asp Trp Asn Leu Val Arg Pro Ile 305 310 315 320 Glu Met Gly Leu Val Pro Arg Val Ala Glu Met Leu Tyr Gln Arg Tyr 325 330 335 Gln Ser Ala Val Asp Arg Arg Val Phe Asp Gly Met Ser Val Ala Glu 340 345 350 Ala Glu Ala Gln Ala His Val Glu Leu Arg Glu Gln Val Leu Gly Gly 355 360 365 Arg Val Leu Thr Ser Phe Thr Gly Thr Ala Pro Leu Ala Ala Glu Met 370 375 380 Lys Thr Phe Val Glu Thr Cys Leu Gly Val His Leu Leu Asp Gly Tyr 385 390 395 400 Gly Leu Thr Glu Val Gly Met Val Thr Lys Asp Gly Leu Val Thr Lys 405 410 415 Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr 420 425 430 Phe Arg Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser 435 440 445 Ala Thr Ala Met Ser Gly Tyr Tyr Gln Arg Pro Asp Val Thr Ala Ala 450 455 460 Ala Phe Asp Ser Glu Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Gln 465 470 475 480 Ile Gly Pro Asp Arg Leu Thr Tyr Val Asp Arg Arg Asn Asn Val Leu 485 490 495 Lys Leu Ala Gln Gly Glu Phe Val Ala Val Ala Arg Leu Glu Ala Ile 500 505 510 Phe Ala Thr Ala Pro Leu Ile Arg Gln Ile Phe Val Tyr Gly Asn Ser 515 520 525 Glu Arg Pro Tyr Leu Leu Ala Val Val Val Pro Thr Asp Glu Ala Leu 530 535 540 Gly Arg Phe Pro Asp Asp Asp Ala Ala Ile Ser Ala Ala Leu Ser Glu 545 550 555 560 Ser Leu Arg Gln Thr Ala Lys Leu Ala Glu Leu Gln Ser Tyr Glu Val 565 570 575 Pro Ala Glu Phe Leu Ile Glu Arg Glu Pro Phe Ser Thr Asp Asn Gly 580 585 590 Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu Arg 595 600 605 Tyr Gly Asp Glu Leu Glu Gln Leu Tyr Ala Gln Leu Ala Asp Thr Arg 610 615 620 Asp Ala Gln Leu Arg Ser Leu Arg His Gly Ala Ala Asp Arg Pro Val 625 630 635 640 Ile Asp Thr Val Ala His Ala Ala Glu Ala Leu Leu Gly Leu Val Gly 645 650 655 Gly Ala Pro Asp Pro Ala Glu His Phe Met Asp Leu Gly Gly Asp Ser 660 665 670 Leu Ser Ala Leu Thr Phe Ala Asn Leu Leu Gln Asp Ile Phe Asp Val 675 680 685 Glu Val Pro Val Ala Leu Ile Ile Gly Pro Thr Ser Ser Leu Arg Leu 690 695 700 Ile Ala Asp His Ile Glu Ala Gly Arg Glu Ser Gly Ser Gln Arg Pro 705 710 715 720 Ser Phe Ala Thr Val His Gly Arg Gly Ala Ser Gln Val Arg Ala Thr 725 730 735 Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Ala Thr Leu Ser Ala Val 740 745 750 Ala Ser Leu Pro Arg Ala Thr Gly Thr Pro Arg Thr Val Leu Leu Thr 755 760 765 Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Ala Leu Glu Trp Leu Glu 770 775 780 Arg Leu Asn Glu Thr Gly Gly Arg Leu Leu Cys Leu Val Arg Gly Thr 785 790 795 800 Asp Pro Glu Ala Ala Tyr Arg Arg Leu Glu Asp Val Phe Arg Ser Gly 805 810 815 Asp Pro Gln Leu Leu Gln Arg Phe Gln Thr Leu Ala Ala Asp His Leu 820 825 830 Glu Ile Ile Val Gly Asp Ile Gly Glu Pro Asn Leu Gly Leu Ser Glu 835 840 845 Glu Val Trp His Gln Leu Ala Gln Arg Val Asp Leu Ile Val His Pro 850 855 860 Ala Ala Leu Val Asn His Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro 865 870 875 880 Asn Val Val Gly Thr Ala Glu Leu Ile Arg Leu Ala Ile Ser Gly Arg 885 890 895 Val Lys Pro Ile Thr Tyr Leu Ser Thr Val Ala Val Ala Met Ser Val 900 905 910 Asp Ala Phe Thr Glu Asp Gly Asp Ile Arg Ala Val Ser Pro Thr Arg 915 920 925 Pro Val Asp Asp Ser Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala 930 935 940 Gly Glu Val Leu Leu Arg Tyr Ala His Asp Leu Cys Gly Leu Pro Val 945 950 955 960 Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Ser His Phe Ala Gly 965 970 975 Gln Leu Asn Val Pro Asp Ala Phe Thr Arg Leu Ile Phe Ser Leu Leu 980 985 990 Val Ala Gly Ile Ala Pro Gly Ser Phe Tyr Arg Ala Asp Gly Ser Arg 995 1000 1005 Pro Arg Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Val Ala Glu 1010 1015 1020 Ala Val Ala Thr Leu Gly Glu Leu Thr Ala Thr Glu Thr Ala Pro 1025 1030 1035 Val Phe Arg Ser Phe Asp Val Met Asn Pro His Asp Asp Gly Ile 1040 1045 1050 Ser Leu Asp Val Phe Val Asp Trp Leu Ile Asp Ala Gly His Asp 1055 1060 1065 Ile His Arg Ile Ala Asp Tyr Asp Glu Trp Leu Gly Arg Phe Glu 1070 1075 1080 Thr Ala Leu Arg Ala Leu Pro Asp Lys Gln Arg Gln Tyr Ser Leu 1085 1090 1095 Leu Pro Leu Leu Asp Ala Tyr Arg Ile Pro Gln Asp Ala Leu Pro 1100 1105 1110 Gly Ala Pro Ala Pro Thr Glu Val Phe Arg Gly Ala Val Arg Asp 1115 1120 1125 Ala Lys Ile Gly Val Asp Asn Asp Ile Pro His Leu Ser Ala Thr 1130 1135 1140 Leu Ile Asp Lys Tyr Val Ala Asp Leu Gln Leu Leu Gly Val Ile 1145 1150 1155 Pro Gly Arg Ser Ala Arg Ser 1160 1165 <210> 224 <211> 1141 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium decipiens <400> 224 Met Arg Leu Arg Thr Ile Met Met Ser Ala Phe Asp His Phe Ala Glu 1 5 10 15 Arg Pro Ala Leu Ala Glu Arg Arg His Ile Pro Thr Thr Asn Glu Gln 20 25 30 Ile Ser Ser Met Asp Asn Arg Val Leu Gly Ala Tyr Glu Thr Leu Thr 35 40 45 Tyr Lys Ala Val Gly Gln Arg Val Ala Ser Val Ala Ala Gln Leu Arg 50 55 60 Ser Glu Thr Gly Thr Arg Pro Ser Ile Leu Pro Gly Asp Arg Val Ala 65 70 75 80 Leu Leu Gly Phe Ala Gly Ile Asp Phe Thr Thr Val Asp Phe Ala Ser 85 90 95 Asn Leu Thr Gly Ile Thr Thr Val Pro Leu Gln Thr Ser Gly Thr Tyr 100 105 110 Glu Gln Gln Ser Ala Val Met Lys Glu Thr Met Pro Arg Val Leu Ala 115 120 125 Val Thr Val Ala Leu Leu Asp Arg Ala Ala Arg Leu Val Ala Asp His 130 135 140 Ala Ser Val Glu Arg Val Ile Val Leu Asp Tyr Arg Gly Gly Glu Ser 145 150 155 160 Glu His His Ser Ala Val Glu Ala Ala Ala Arg Glu Ile Ser Ile Ser 165 170 175 Leu Glu Ile Leu Asp Leu Asp Asn Gly Gln Tyr Val Ala Asp Pro Glu 180 185 190 His Glu Gly Thr Gly Glu Asp Ala Leu Ala Met Leu Leu Tyr Thr Ser 195 200 205 Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Arg Leu Leu 210 215 220 Ala Glu Met Trp Gly Gly Glu Gly Trp Ser Glu Phe Phe Ala Glu Ala 225 230 235 240 Val Asp Ile Ala Asn Phe His Tyr Met Pro Met Ser His Val Ala Gly 245 250 255 His Ser Ser Val Arg Ser Thr Leu Ala Arg Gly Gly Val Thr Tyr Phe 260 265 270 Ala Ser Thr Thr Asn Leu Ser Ser Phe Phe Asp Asp Leu Ser Leu Ala 275 280 285 Gln Pro Thr Glu Leu Ser Leu Val Pro Arg Val Cys Glu Leu Leu His 290 295 300 Gln Glu Tyr Gln Arg Arg Leu Gln Ala Ile Ala Thr Gln Pro Ala Gly 305 310 315 320 Lys Ser Thr Pro Asp Thr Asp Ser Asp Ala Ala Ala Met Lys Val Leu 325 330 335 Ala Asp Met Arg Gln Gly Thr Leu Gly Gly Asn Ile Gln Trp Ala Ser 340 345 350 Cys Thr Ser Ala Pro Val Ser Ala Glu Leu Lys Ser Phe Met Glu Ser 355 360 365 Leu Leu Gly Ile Glu Leu His Glu Leu Tyr Gly Thr Thr Glu Ile Gly 370 375 380 Gly Val Leu Ala Asp Gly Arg Phe Leu Arg Pro Pro Val Ile Ser Tyr 385 390 395 400 Gln Leu Gln Asp Val Pro Glu Leu Gly Tyr Phe Ser Ser Asp Arg Pro 405 410 415 His Ala Arg Gly Glu Leu Leu Ile Lys Ser Thr Ser Thr Val Pro Gly 420 425 430 Tyr Tyr Asn Arg Pro Glu Leu Asn Arg Glu Ile Phe Thr Asp Asp Gly 435 440 445 Tyr Tyr Arg Thr Gly Asp Ile Ala Ser Val Asp Asp Asp Gly Arg Val 450 455 460 Arg Ile Ile Asp Arg Lys Asn Ala Ile Ile Lys Leu Ser Gln Gly Glu 465 470 475 480 Phe Val Ala Leu Pro Ser Leu Glu Ala Lys Tyr Thr Ala Gly Ser Asp 485 490 495 Val Ile Arg Gln Ala Phe Leu Tyr Gly Glu Ser Asp Gln Ser Ser Ile 500 505 510 Val Gly Val Val Val Pro Ser Asp Glu Leu Arg Thr Glu Leu Ala Asp 515 520 525 Asp Leu Ala Ala Ile Gln Thr Arg Ile Val Arg Glu Phe Arg Lys Val 530 535 540 Ala Gly Asp Glu Asn Leu Asn Ser Tyr Glu Ile Pro Ser Ala Val Leu 545 550 555 560 Ile Asp Phe Glu Pro Phe Ser Glu Thr Asn Gly Leu Leu Ser Asp His 565 570 575 Arg Lys Pro Val Arg Pro Arg Leu Val Glu Lys Tyr Gly Pro Arg Leu 580 585 590 Ser Ala Leu Tyr Gln Glu Leu Arg Ser Gly Arg Asp Gln Leu Leu Asp 595 600 605 Trp Leu Val Ala His Gly Ala Glu Gly Glu Thr Val Ser Thr Val Arg 610 615 620 Thr Ala Ile Ala Val Ala Ile Gln Ala Asp Val Glu Asp Ile Ala Glu 625 630 635 640 Ser Ala Lys Phe Arg Asp Leu Gly Gly Asp Ser Leu Thr Ala Val Tyr 645 650 655 Leu Ser Arg Leu Phe Glu Gln Ile Tyr Ser Ile Arg Val Pro Val Asp 660 665 670 Thr Val Val Ser Glu Ser Tyr Thr Ile Arg Gln Leu Ala Glu Tyr Ile 675 680 685 Asp Thr Lys Gln Leu Ser Gly Leu Asp Ser Ala Ser Phe Glu Glu Ile 690 695 700 His Gly Ala Glu Pro His Leu Leu Gln Ala Ala Asp Leu Thr Leu Pro 705 710 715 720 Arg Phe Phe Asp Asp Glu Ile Pro Leu Pro Asp Pro Leu Pro Ala Ala 725 730 735 Gly Asp Ala Lys Ser Val Leu Ile Thr Gly Ala Ser Gly Tyr Leu Gly 740 745 750 His Phe Leu Cys Leu Gln Trp Leu Arg Gln Phe Ala Gly Thr Asp Asn 755 760 765 Arg Val Thr Cys Leu Ile Arg Ala Ser Asp Asp Val Ala Ala Arg Ser 770 775 780 Arg Leu Arg Lys Ala Phe Ser Thr Ser Glu Thr Leu Leu Ala Glu Phe 785 790 795 800 Asp Gly Leu Ser Ala Asn Leu Asp Val Ile Ala Gly Asp Ile Ser Glu 805 810 815 Asp Gln Leu Gly Leu Asp Asp Pro Thr Trp Lys Arg Leu Thr Gln Asp 820 825 830 Leu Thr Glu Ile Ile His Ala Gly Ala Met Val Asn His Ala Leu Ser 835 840 845 Tyr Arg Glu Leu Phe Ala Ala Asn Val Ser Gly Thr Ala Gly Val Ile 850 855 860 Arg Leu Ala Ile Thr Gly Pro Leu Lys Pro Val Thr Phe Met Ser Ser 865 870 875 880 Ile Ala Thr Ala Leu Leu Thr Gly Thr Ser Ser Leu Pro Leu Asp Glu 885 890 895 Leu Ser Asp Ile Arg Gln Ala Leu Pro Glu Ile Glu Met Ala Gly Gly 900 905 910 Ile Val Asp Gly Tyr Ala Ala Thr Lys Trp Ala Gly Glu Val Leu Leu 915 920 925 Arg Asp Ala His Ala Arg Tyr Asp Leu Pro Val Thr Val Ile Arg Ser 930 935 940 Ser Met Ile Leu Ala His Ser Glu Phe Arg Gly Gln Ile Asn Val Pro 945 950 955 960 Asp Thr Phe Thr Arg Leu Leu Tyr Ser Leu Ile Arg Thr Gly Leu Ala 965 970 975 Pro Ser Ser Phe Tyr Thr His Asp Gly Asp Arg Ala His Tyr Asp Gly 980 985 990 Leu Pro Ala Asp Val Val Ala Gln Ala Ile Ala Ser Leu Thr His Arg 995 1000 1005 Asp Glu Arg Lys Thr Phe Ala Thr Phe His Leu Val Asn Pro Phe 1010 1015 1020 Asp Asp Gly Ile Ser Leu Asp Arg Met Val His Trp Leu Ile Glu 1025 1030 1035 Met Gly Val Pro Leu Ile Arg Ile Glu Ser Tyr Gly Glu Trp Leu 1040 1045 1050 His Arg Phe Thr Ala Ala Leu Asn Ala Leu Asp Lys Asp Asp Lys 1055 1060 1065 Arg Pro Ser Val Leu Pro Leu Leu Glu Gly Phe Ser Gln Pro Glu 1070 1075 1080 Glu Pro Ala His Gly Ser Leu Ile Gly Ser Pro Glu Leu Thr Ala 1085 1090 1095 Ala Leu Ser Ala Thr Gly Ser Asp Ala Thr Leu Ser Val Leu Thr 1100 1105 1110 Ser Asp Phe Ile Arg Lys Cys Val Glu Asp Leu Glu Tyr Val Phe 1115 1120 1125 Gly Gln Pro Ile Pro His Gly Ser Leu Ala Ser Ala Arg 1130 1135 1140 <210> 225 <211> 1184 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. Bolletii <400> 225 Met Thr Val Thr Asn Glu Thr Asn Pro Gln Gln Glu Gln Leu Ser Arg 1 5 10 15 Arg Ile Glu Ser Leu Arg Glu Ser Asp Pro Gln Phe Arg Ala Ala Gln 20 25 30 Pro Asp Pro Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu 35 40 45 Ser Glu Ala Ile Ala Ala Leu Met Thr Gly Tyr Ala Glu Arg Pro Ala 50 55 60 Leu Gly Glu Arg Ala Arg Glu Leu Val Thr Asp Gln Asp Gly Arg Thr 65 70 75 80 Thr Leu Arg Leu Leu Pro Arg Phe Asp Thr Thr Thr Tyr Gly Glu Leu 85 90 95 Trp Ser Arg Thr Thr Leu Val Ala Ala Ala Trp His His Asp Ala Ala 100 105 110 His Pro Val Lys Ala Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser 115 120 125 Ile Asp Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val 130 135 140 Ala Val Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Cys Thr Thr Ile 145 150 155 160 Leu Ala Glu Ala Glu Pro Asn Thr Leu Ala Val Ser Ile Glu Leu Ile 165 170 175 Gly Ala Ala Met Glu Ser Val Arg Ala Thr Pro Ser Ile Lys Gln Val 180 185 190 Val Val Phe Asp Tyr Thr Pro Glu Val Asp Asp Gln Arg Glu Ala Phe 195 200 205 Glu Ala Ala Ser Thr Gln Leu Ala Gly Thr Gly Ile Ala Ile Glu Thr 210 215 220 Leu Asp Ala Val Ile Ala Arg Gly Ala Ala Leu Pro Ala Ala Pro Leu 225 230 235 240 Tyr Ala Pro Ser Ala Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile 260 265 270 Val Arg Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn 275 280 285 Leu Pro Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly 290 295 300 Arg Gly Thr Leu Thr Ser Thr Leu Ser Thr Gly Gly Thr Gly Tyr Phe 305 310 315 320 Ala Ala Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile 325 330 335 Arg Pro Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe 340 345 350 Gln Arg Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Ser Gly Asp Ala 355 360 365 Ala Ser Ala Glu Ala Val Ala Ala Glu Val Lys Ala Asp Ile Arg Asp 370 375 380 Asn Leu Phe Gly Gly Arg Val Ser Ala Val Met Val Gly Ser Ala Pro 385 390 395 400 Leu Ser Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu Asn 405 410 415 Leu Thr Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp 420 425 430 Gly Ile Val Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val 435 440 445 Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro His Pro Arg Gly Glu 450 455 460 Leu Leu Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro 465 470 475 480 Glu Val Thr Ala Gly Val Phe Asp Ala Asp Gly Phe Tyr Met Thr Gly 485 490 495 Asp Ile Val Ala Glu Leu Ala His Asp Asn Ile Glu Ile Ile Asp Arg 500 505 510 Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala 515 520 525 Thr Leu Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr 530 535 540 Val Tyr Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro 545 550 555 560 Thr Pro Glu Ala Val Ala Ala Ala Lys Gly Asp Ala Ala Ala Leu Lys 565 570 575 Thr Thr Ile Ala Asp Ser Leu Gln Asp Ile Ala Lys Glu Ile Gln Leu 580 585 590 Gln Ser Tyr Glu Val Pro Arg Asp Phe Ile Ile Glu Pro Gln Pro Phe 595 600 605 Thr Gln Gly Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro 610 615 620 Asn Leu Lys Ala His Tyr Gly Pro Gln Leu Glu Gln Met Tyr Ala Glu 625 630 635 640 Ile Ala Glu Gln Gln Ala Ala Glu Leu Arg Ala Leu His Gly Val Asp 645 650 655 Pro Asp Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala Leu 660 665 670 Leu Gly Val Ser Ser Ala Glu Leu Ala Ala Asp Ala His Phe Thr Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Asp Leu Leu Arg 690 695 700 Asp Ile Phe Ala Val Glu Val Pro Val Gly Val Ile Val Ser Ala Ala 705 710 715 720 Asn Asp Leu Gly Gly Val Ala Lys Phe Val Asp Glu Gln Arg Tyr Ser 725 730 735 Gly Gly Thr Arg Pro Thr Ala Glu Thr Val His Gly Ala Gly His Thr 740 745 750 Glu Ile Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala 755 760 765 Thr Leu His Ala Ala Pro Ser Leu Pro Lys Ala Val Gly Ile Pro His 770 775 780 Thr Val Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly His Tyr Leu Ala 785 790 795 800 Leu Glu Trp Leu Glu Arg Leu Asp Lys Thr Asp Gly Lys Leu Ile Ala 805 810 815 Ile Val Arg Gly Lys Asn Ala Glu Ala Ala Tyr Arg Arg Leu Glu Glu 820 825 830 Ala Phe Asp Thr Gly Asp Thr Gln Leu Leu Ala His Phe Arg Ser Leu 835 840 845 Ala Arg Gln His Leu Glu Val Leu Ala Gly Asp Ile Gly Asp Pro Asn 850 855 860 Leu Gly Leu Asp Ala Asp Thr Trp Gln Arg Leu Ala Asp Thr Val Asp 865 870 875 880 Val Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser 885 890 895 Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Lys Leu 900 905 910 Ala Ile Thr Thr Lys Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ala 915 920 925 Val Ala Ala Tyr Val Asp Pro Thr Thr Phe Asp Glu Glu Ser Asp Ile 930 935 940 Arg Ala Ile Ser Ala Val Arg Pro Val Asp Glu Leu Tyr Ala Asn Gly 945 950 955 960 Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 965 970 975 Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 980 985 990 Ala His Ser Arg Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr 995 1000 1005 Arg Leu Ile Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Gly Ser 1010 1015 1020 Phe Tyr Gln Ala His Ala Thr Gly Glu Arg Pro Leu Ala His Tyr 1025 1030 1035 Asp Gly Leu Pro Gly Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu 1040 1045 1050 Gly Thr Gln Val Val Asp Ser Tyr Glu Thr Tyr Asp Cys Val Asn 1055 1060 1065 Pro His Ala Asp Gly Val Ser Leu Asp Asn Phe Val Asp Trp Leu 1070 1075 1080 Ile Glu Gly Gly Tyr Pro Ile Ala Arg Ile Asp Asn Tyr Thr Glu 1085 1090 1095 Trp Phe Thr Arg Phe Asp Thr Ala Ile Arg Gly Leu Pro Glu Lys 1100 1105 1110 Gln Lys Gln His Ser Leu Leu Pro Leu Leu His Ala Phe Glu Gln 1115 1120 1125 Pro Ser Ala Ala Glu Asn His Gly Val Val Pro Ala Lys Arg Phe 1130 1135 1140 Gln His Ala Val Gln Ala Ala Gly Ile Gly Pro Ala Gly Gln Asp 1145 1150 1155 Gly Thr Thr Asp Ile Pro His Leu Ser Arg Arg Leu Ile Val Lys 1160 1165 1170 Tyr Ala Lys Asp Leu Glu Gln Leu Gly Leu Leu 1175 1180 <210> 226 <211> 1132 <212> PRT <213> Artificial Sequence <220> <223> Pseudomonas fragi <400> 226 Met Ser Leu Ala Ser Ile Val Ala Thr Thr Met Thr Leu His Ala Asp 1 5 10 15 Ser Pro Ala Leu Gly Glu Arg His Tyr Arg Leu Ile Thr Asn Asn Ile 20 25 30 Thr Lys Glu Val Arg Ser Gln Leu Leu Pro Gly Tyr Thr Thr Val Thr 35 40 45 Tyr Ser Glu Leu Trp Gln Arg Val Lys Phe Leu Ala Ala Glu Leu His 50 55 60 His His Pro Tyr Ala Pro Ile Thr Ala Gly Cys Pro Val Ala Phe Leu 65 70 75 80 Ala Phe Thr Ser Gly Asp Tyr Ala Thr Leu Asp Leu Ala Cys Ile Tyr 85 90 95 Leu Gly Ala Val Thr Val Ala Leu Gln Thr Asn Ala Ser Gly Ser His 100 105 110 Ile Asn Ser Ile Leu Lys Glu Thr Ala Pro Leu Ile Ile Ala Val Ser 115 120 125 Ile Asp His Leu Asp Val Ala Ile Asp Ala Val Leu Asn Thr Pro Ser 130 135 140 Ile Ser Arg Ile Val Leu Leu Asn Tyr Tyr Pro Ala Val Ser Glu His 145 150 155 160 Ser Ser Lys Arg Ser Thr Ala Arg Arg Arg Leu Ser Glu His Ser Ser 165 170 175 Thr Val Ser Ile Asp Cys Leu Asn Glu Ile Ile Thr Thr Gly Lys Ser 180 185 190 Leu Pro Asp Ala Pro Leu Tyr Asn Ser Pro Asn Ala Asp Asp Glu Leu 195 200 205 Ser Met Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 210 215 220 Met Tyr Thr Gln Lys Leu Ala Ser Gly Met Trp Gly Gly Ser Trp Ala 225 230 235 240 Thr Ile Phe Ser Lys Glu Pro Pro Ile Ser Phe His Tyr Met Pro Met 245 250 255 Ser His Val Ala Gly His Ser Ser Leu Lys Ser Thr Leu Ala Arg Gly 260 265 270 Gly Thr Cys Tyr Phe Thr Ala Lys Ser Asn Leu Ser Thr Leu Leu Glu 275 280 285 Asp Ile Ser Leu Cys Arg Pro Thr Glu Leu Ser Leu Val Pro Arg Ile 290 295 300 Cys Glu Leu Ile Ser Gln Thr Tyr Gln Leu Ala Leu Ile Lys His Asn 305 310 315 320 Val Ala Gln Gly Asp Gln Lys Ala Thr Ser Ile Leu Glu Tyr Ile Arg 325 330 335 Thr Asn Thr Leu Gly Gly Arg Ile Ala Trp Ala Ser Cys Ser Ser Ala 340 345 350 Pro Leu Pro Asp Thr Leu Lys Leu Phe Met Glu Thr Leu Leu Asn Ile 355 360 365 Pro Ile His Asn Val Tyr Gly Ser Thr Glu Ala Gly Ala Val Trp Ile 370 375 380 Asp Asn Glu Leu Leu Asn Pro Pro Val Leu Asn Phe Lys Leu Ile Asp 385 390 395 400 Ala Pro Glu Leu Gly Tyr Phe Thr Thr Asp Leu Pro Phe Pro Arg Gly 405 410 415 Glu Leu Leu Leu Lys Thr Leu Ser Ile Ile Pro Gly Tyr Tyr Lys Arg 420 425 430 Pro Asp Leu Ala Thr Glu Leu Phe Asp Glu Leu Gly Tyr Tyr Lys Thr 435 440 445 Gly Asp Ile Val Ala Gln Thr Gly Ser His Arg Leu Glu Phe Val Asp 450 455 460 Arg Arg Lys Asn Ile Leu Lys Leu Ser Gln Gly Glu Phe Ile Ala Thr 465 470 475 480 Ser Gln Leu Glu Thr Leu Tyr Ser Ala Ile Pro Glu Ile Gln Asn Ile 485 490 495 Tyr Ile Tyr Gly Lys Gly Glu Trp Ser Tyr Phe Leu Ala Val Ile Ile 500 505 510 Pro Tyr Asn Asn Leu Thr Lys Arg Leu Asp Glu Lys Ala Glu Thr Ile 515 520 525 Lys Gln Phe Phe Met Asn Ala Ile Arg Gln His Ala Lys Ile Asn Lys 530 535 540 Leu Arg Ser Tyr Glu Ile Pro Arg Asp Val Leu Ile Asp Asn Thr Pro 545 550 555 560 Phe Thr Gln Gln Asn Gly Leu Leu Ser Asp His Gly Lys Pro Met Trp 565 570 575 Pro Lys Leu Arg Gln Lys Tyr Ala Leu His Leu Glu Asn Leu Asn Ser 580 585 590 Gln Leu Ile Ser Gln Asp Arg Gly Lys Leu Gln Asn Leu His Gln Arg 595 600 605 Val Asp Lys Gln Pro Val Leu Glu Ile Leu Lys Asn Ala Val Cys Ser 610 615 620 Leu Val Gly Gly Thr Ala Glu Met Ile Ser Pro Glu Ala Gln Phe Arg 625 630 635 640 Asp Leu Gly Gly Asp Ser Ile Ser Ala Val Asn Leu Ala Ser Leu Leu 645 650 655 Ser Asp Phe Tyr Ala Ile Asn Val Pro Val Asp Leu Leu Ile Ser Pro 660 665 670 Gly Tyr Asp Leu Gln Tyr Ile Ser Glu His Ile Glu Lys Ala Leu Gln 675 680 685 Thr His Lys Ser Arg Pro Ser Cys Glu Ser Ile His Ser Leu Thr Pro 690 695 700 Phe Thr Phe His Ala Lys Asp Leu Gln Leu Glu His Phe Ile Asn Pro 705 710 715 720 Asp Ile Leu His Lys Ala Asn Thr Leu Asn Thr Pro Pro His Pro Val 725 730 735 Lys Thr Ile Leu Leu Thr Gly Ser Ser Gly Tyr Leu Gly Arg Phe Leu 740 745 750 Ala Leu Gln Leu Leu Glu Ser Leu Gly Ala Gln Gly Gly Thr Leu Ile 755 760 765 Cys Val Val Arg Ala Lys Asp Ile Gln Thr Ala Asn Lys Arg Phe Gln 770 775 780 Glu Ser Phe Gly Arg Gly Asp Thr Ala Ile Ser Arg Lys Val Arg Ala 785 790 795 800 Leu Ser Lys Leu His Leu Glu Val Leu Ala Gly Asp Ile Gly Glu Pro 805 810 815 Lys Leu Gly Leu Asp Glu Ala Thr Trp Glu Arg Leu Ser Ser Glu Val 820 825 830 Asp Cys Ile Phe His Ala Ala Ala Leu Val Asn His Leu Leu Pro Tyr 835 840 845 Ala Ser Leu Phe Asn Ala Asn Val Asn Gly Thr Ser Glu Ile Ile Ser 850 855 860 Leu Ala Leu Ser Cys His Leu Lys Pro Ile Val Phe Leu Ser Ser Ile 865 870 875 880 Ala Val Ala Ser Leu Ala Gly Ala Gln Pro Thr Leu Asp Glu Asp Met 885 890 895 Asp Ile Arg Ile Ala Ala Pro Val Val Glu Ala His Asp Thr Tyr Ala 900 905 910 Val Gly Tyr Gly Leu Ser Lys Trp Ala Cys Glu Val Leu Leu Arg Glu 915 920 925 Ala Asn Ser Gln Tyr Gly Leu Pro Val Thr Thr Phe Arg Ser Ser Met 930 935 940 Ile Leu Ala His Ser Ser Tyr Pro Glu Gln Leu Asn Ile Pro Asp Met 945 950 955 960 Phe Thr Arg Leu Leu Leu Ser Leu Val Gln Thr Gly Ile Ala Pro Gln 965 970 975 Ser Phe Tyr Arg Gln Ala Glu Lys Glu Gln Lys Pro His Tyr Asp Gly 980 985 990 Leu Pro Val Asp Phe Thr Ala Asn Ala Ile Val Arg Ile Gly Leu Asp 995 1000 1005 Lys Gln Lys Asn Ser Tyr Arg Ser Ile Asn Leu Val Asn Ser His 1010 1015 1020 Asn Asp Gly Ile Ser Leu Asp Thr Val Val Asp Trp Leu Ser Glu 1025 1030 1035 Leu Gly Ile Asn Ile Lys Lys Ile Ser Lys Tyr Ala Asp Trp His 1040 1045 1050 Gln Gln Phe Glu Arg Lys Leu Leu Ala Leu Pro Lys Ser Leu Gln 1055 1060 1065 Gln His Thr Ser Leu Pro Leu Ile His Ser Leu Ser Glu Pro Ala 1070 1075 1080 Glu Val Ile Ser Gly Ser Thr Ile Ser Ser Lys Arg Leu His Glu 1085 1090 1095 Thr Phe Gln Ala Val Asn Ser Asp Lys Val Thr Val Pro His Leu 1100 1105 1110 Ser Lys Thr Leu Ile His Lys Tyr Leu Thr Asp Leu Gln Ser Leu 1115 1120 1125 Gly Leu Leu Asn 1130 <210> 227 <211> 1179 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. 15-1154-1 <400> 227 Met Lys Ser Met Pro Ile Thr Glu Gly Asn Ser Arg Met Thr Ser Ser 1 5 10 15 Thr Ala Thr Thr Ala Thr Asp His Ala Leu Arg Arg Arg Phe Ala Glu 20 25 30 Leu His Arg Thr Asp Glu Gln Phe Arg Ser Ala Glu Pro Asp His Gly 35 40 45 Val Ala Ala Ala Ala Leu Ala Leu Lys Pro Asn Leu Ala Ala Val Val 50 55 60 Gln Gln Val Met Ile Gly Tyr Gly Asp Arg Pro Ala Leu Gly Arg Arg 65 70 75 80 Ala Arg Thr Ile Val Asp Gly Ala Ala Ser Leu Leu Pro Ser Ile Asp 85 90 95 Thr Ile Thr Tyr Ala Glu Thr Trp Asp Arg Ala Gly Ala Thr Ala Ala 100 105 110 Ala Leu Val His Gly Glu Asn Pro Val Gln Pro Gly Asp Phe Val Ala 115 120 125 Thr Leu Gly Phe Ala Ser Val Asp Tyr Ala Val Val Glu Leu Ala Thr 130 135 140 Val Arg Leu Gly Ala Val Ala Val Pro Leu Gln Ala Gly Ala Ser Ala 145 150 155 160 Thr Gln Leu Ile Asp Ile Val Ala Glu Val Glu Pro Ala Val Ile Ala 165 170 175 Ala Asp Ser Glu Asn Leu Ala Val Ala Ile Glu Ile Ala Gln Gln Ser 180 185 190 Pro Ser Val His Thr Val Ile Val Leu Asp His Asp Asp Arg Val Asp 195 200 205 Ala Asp Arg Glu Arg Leu Thr Ala Ala Arg Val Leu Asp Ala Val Ser 210 215 220 Leu Ser Thr Leu Ala Asp Val Ile Glu Arg Gly Arg Ala Gln Gly Pro 225 230 235 240 Tyr Pro Leu Val Glu Ser Asp Asp Pro Glu Arg Leu Ala Thr Leu Ile 245 250 255 Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Ile His Thr Glu 260 265 270 Ala Ile Val Thr Gly Thr Trp Thr Gly Ala Trp His Ser Thr Gly Ser 275 280 285 Glu Ser Asp Ser Asp Ala Gly Pro Gly Phe Pro Val Ile Thr Leu Asp 290 295 300 Tyr Leu Pro Met Ser His Leu Ala Gly Arg Gly Leu Val Phe Ser Thr 305 310 315 320 Leu Ala Ala Gly Gly Thr Val Thr Phe Ala Gly Ser Ser Asp Leu Ser 325 330 335 Thr Leu Phe Asp Asp Phe Ser Leu Thr Arg Pro Thr Leu Ala Leu Leu 340 345 350 Val Pro Arg Val Cys Glu Met Ile Arg His Thr Ala Leu Ala Glu Ile 355 360 365 Asp Arg Arg Val Asp Ala Gly Ala Asp Pro Ala Thr Val Arg Asp Val 370 375 380 Val Leu Gly Glu Phe Arg Arg Asp Thr Phe Gly Gly Arg Val Leu Ala 385 390 395 400 Ala Val Val Gly Thr Ala Pro Ile Ala Thr Glu Val Lys Asp Phe Val 405 410 415 Ala Glu Leu Leu Asp Ala Gln Val Gln Asp Asn Tyr Gly Ser Thr Glu 420 425 430 Ala Gly Met Val Leu His Asp Gly Val Val Arg Arg Pro Pro Val Ile 435 440 445 Asp Tyr Lys Leu Asp Asp Val Pro Glu Leu Gly Tyr Phe Val Thr Asp 450 455 460 Thr Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Glu Ser Ile Thr 465 470 475 480 Pro Gly Tyr Tyr Lys Arg Pro Glu Val Thr Ala Glu Met Phe Asp Ala 485 490 495 Glu Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Ala Pro Asp 500 505 510 His Leu Ala Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ala Gln 515 520 525 Gly Glu Phe Val Ala Leu Ala Arg Leu Glu Ser Val Phe Gly Thr Ser 530 535 540 Asp Leu Val Asp Gln Ile Phe Val Tyr Gly Asn Ser Gln Arg Ser Tyr 545 550 555 560 Leu Leu Ala Val Val Val Pro Ala Pro Gly Val Asp Asp Pro Gly Ser 565 570 575 Ile Leu Ala Ser Leu Gln Thr Ile Ala Arg Asp Ala Gly Leu Asn Ser 580 585 590 Tyr Glu Val Pro Arg Glu Val Ile Val Glu Thr Glu Ser Phe Thr Gln 595 600 605 Asp Asn Gly Leu Leu Ser Gly Ala Gly Lys Gln Leu Arg Pro Lys Leu 610 615 620 Val Asp Arg Tyr Gly Ala Thr Leu Glu Ala Arg Tyr Thr Glu Leu Glu 625 630 635 640 Glu Ser Gln Ser Gly Arg Leu Arg Asp Leu Arg Arg Arg Gly Pro Asp 645 650 655 Ala Pro Val Leu Ala Thr Val Gly Asp Ser Ala Val Ala Leu Leu Gly 660 665 670 Cys Ala Gly Thr Asp Val Ser Pro Asp Val Arg Phe Ala Asp Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Asn Leu Leu Arg Asp Ile 690 695 700 Phe Asp Ile Glu Val Pro Val Gly Val Ile Thr Gly Pro Ser Thr Asp 705 710 715 720 Leu Arg Gly Ile Ala Asp Tyr Ile Ser Ala Arg Gln Asp Ser Asp Thr 725 730 735 Asp Ala Val Thr Phe Asp Ser Val His Gly Arg Gly Ala Thr Val Val 740 745 750 Lys Ala Ser Asp Leu Thr Leu Asp Ala Phe Leu Ser Ala Asp Ala Leu 755 760 765 Lys Ala Ala Gln Asp Ala Glu Arg Pro Arg Pro Thr Thr Arg Thr Val 770 775 780 Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Ala Leu Glu 785 790 795 800 Trp Leu Glu Arg Met Ala Asp Val Gly Gly Thr Val Val Cys Leu Val 805 810 815 Arg Gly Arg Asp Ala Ala Asp Ala Arg Ala Arg Leu Asp Ala Ala Phe 820 825 830 Asp Ser Gly Asp Ala Glu Leu Ser Ala Arg Tyr Arg Ala Leu Ala Tyr 835 840 845 Ala Ala Leu Glu Val Val Ala Gly Asp Ile Gly Glu Ser Arg Leu Gly 850 855 860 Leu Asp Glu Asn Thr Trp Asn Ser Leu Ala Thr Arg Val Asp Arg Ile 865 870 875 880 Val His Pro Ala Ala Leu Val Asn His Ala Leu Pro Tyr Pro His Met 885 890 895 Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Val Arg Leu Ala Thr 900 905 910 His His His Leu Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala 915 920 925 Ala Gly Val Asp Glu Phe Val Glu Asn Gly Asp Ile Arg Val Glu Ser 930 935 940 Ser Ser Arg Ser Val Asp Glu Ser Tyr Ala Asn Gly Tyr Gly Thr Ser 945 950 955 960 Lys Trp Ala Gly Glu Val Leu Leu Arg Asn Ala Phe Asp Asp Leu Gly 965 970 975 Leu Pro Val Thr Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Thr 980 985 990 Trp Ser Gly Gln Leu Asn Val Pro Asp Val Phe Thr Arg Leu Val Leu 995 1000 1005 Ser Ile Ala Ala Thr Gly Ile Ala Pro Asn Ser Phe Tyr Arg Ser 1010 1015 1020 Asp Thr Gly Ala Pro Leu Asp Asp Ala Gly Arg Pro Arg Ala His 1025 1030 1035 Tyr Asp Gly Leu Pro Ala Asp Phe Ser Ala Ala Ala Ile Thr Thr 1040 1045 1050 Leu Gly Gly Asp Thr Val Asp Gly Tyr Thr Thr Tyr Asp Val Leu 1055 1060 1065 Asn Pro His Asp Asp Gly Ile Ser Leu Asp Thr Phe Val Asp Trp 1070 1075 1080 Met Ile Glu Ser Gly Arg Ser Ile Glu Arg Ile Glu Asp Tyr Asp 1085 1090 1095 Glu Trp Phe Ala Lys Phe Ser Ala Ala Ile Asp Glu Leu Pro Glu 1100 1105 1110 Pro Gln Arg Ser Arg Ser Leu Leu Pro Leu Leu His Ala Tyr Glu 1115 1120 1125 His Pro Asp Val Pro Ala Ala Gly Ser His Leu Pro Ala Asp Val 1130 1135 1140 Phe Arg Ala Ala Val Arg Glu Glu Ser Asp Asp Ile Pro His Leu 1145 1150 1155 Asp Arg Ala Leu Ile Glu Lys Tyr Leu Ser Asp Leu Glu Gln Leu 1160 1165 1170 Gly Leu Leu Ala Pro Val 1175 <210> 228 <211> 1175 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. 05-340-1 <400> 228 Met Thr His Thr Leu Ala Val Asp Ser Glu Arg Glu Arg Glu Ile Arg 1 5 10 15 Gln Arg Asp Arg Phe Thr Glu Leu His Arg Ser Asp Arg Glu Phe Arg 20 25 30 Ala Ala Glu Pro Asp Ser Ala Val Ala Asp Ala Ala Gln Glu Leu Ser 35 40 45 Pro Asn Leu Ala Arg Val Val Ala Glu Ile Met Thr Arg Tyr Ser Asp 50 55 60 Arg Pro Ala Leu Gly Arg Arg Ala Arg Glu Ile Ala Arg Ile Asp Asp 65 70 75 80 Lys Asn Thr Leu Arg Leu Leu Pro Arg Phe Asp Thr Val Thr Tyr Gly 85 90 95 Gln Ala Trp Ser Asp Ala Gly Ala Leu Ala Ser Ala Leu Thr His Asp 100 105 110 Ala Ile Gly Ile Ala Ser Gly Asp Phe Phe Ala Thr Leu Gly Phe Ala 115 120 125 Ser Ala Asp Tyr Val Val Ala Glu Leu Ala Thr Ile Arg Leu Gly Ala 130 135 140 Ile Ala Val Pro Leu Gln Ala Gly Ala Thr Ala Gly Gln Leu Ser Ala 145 150 155 160 Ile Ala Asp Glu Val Glu Pro Val Val Leu Ala Ala Asp Val Asp Asn 165 170 175 Leu Ser Val Ala Val Gln Val Ala Thr Gln Cys Arg Ser Ile Arg Arg 180 185 190 Ile Val Val Leu Asp His Asp Gly Ala Ile Asp Ala His Ala Arg Ile 195 200 205 Met Glu Ser Ala Arg Ser Asp Ala Asp Arg Val Gly Val Ser Val Arg 210 215 220 Pro Leu Thr Glu Leu Val Gly Asp Gly Ala Gln Leu Pro Glu Val Pro 225 230 235 240 Leu Pro Asp Asp Glu Asp Pro Asp Arg Leu Ala Thr Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met His Thr Glu Arg Ile 260 265 270 Val Cys Gly Ala Trp Thr Gly Ala Trp His His Thr Gly Ala Ser Ser 275 280 285 Glu Ala Ser Asp Arg Pro Ala Phe Pro Val Ile Thr Leu Asp Tyr Leu 290 295 300 Pro Met Ser His Leu Ala Gly Arg Gly Leu Val Phe Ser Thr Leu Ala 305 310 315 320 Ala Gly Gly Thr Val His Phe Ala Gly Ala Ser Asp Leu Ser Thr Leu 325 330 335 Phe Glu Asp Phe Ala Leu Ala Arg Pro Thr Met Ala Leu Leu Ile Pro 340 345 350 Arg Val Cys Glu Met Ile Arg His Asn Val Leu Ala Glu Ile Asp Arg 355 360 365 Glu Val Glu Arg Ser Ala Gly Gly Asp Ala Asp Ser Thr Arg Arg Glu 370 375 380 Val Leu Glu Arg Asn Arg Ile Glu Gln Phe Gly Gly Arg Ile Leu Ala 385 390 395 400 Ala Met Val Gly Thr Ala Pro Ile Ala Pro Glu Val Lys Asp Phe Val 405 410 415 Ser Glu Leu Leu Asp Ile Arg Val Arg Asp Asn Tyr Gly Ser Thr Glu 420 425 430 Ala Gly Met Val Leu His Asp Gly Val Val Gln Arg Pro Pro Val Ile 435 440 445 Glu Tyr Lys Leu Asp Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp 450 455 460 Thr Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Ala Ser Ile Ile 465 470 475 480 Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Ser 485 490 495 Glu Gly Phe Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Glu Pro Asp 500 505 510 Arg Leu Ala Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ala Gln 515 520 525 Gly Glu Phe Val Ala Leu Ala Arg Leu Glu Ala Leu Phe Gly Thr Ser 530 535 540 Glu Leu Val Asp Gln Ile Phe Leu Tyr Gly Asn Ser Gln Arg Ala Tyr 545 550 555 560 Leu Leu Ala Val Val Val Pro Ala Arg Pro Asp Thr Thr Ala Gly Ser 565 570 575 Val Ile Glu Ser Leu Gln Glu Ile Ala Arg Gln Glu Ser Leu Asn Ser 580 585 590 Tyr Glu Ile Pro Arg Asp Val Thr Val Glu His Gln Pro Phe Thr Gln 595 600 605 Glu Asn Gly Leu Leu Ser Gly Ala Gly Lys Gln Leu Arg Pro Lys Leu 610 615 620 Val Glu Arg Tyr Gly Asp Glu Leu Glu Arg Arg Tyr Ala Glu Leu Glu 625 630 635 640 Ser Gly Gln Asn Glu Arg Leu Arg Glu Leu Arg Arg Ser Gly Ala Asp 645 650 655 Ala Pro Val Leu Thr Thr Val Gly Asp Ala Ala Gln Ala Leu Leu Gly 660 665 670 Cys Ala Gly Ser Asp Val Arg Pro Asp Ala His Phe Ser Asp Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Thr Leu Leu Arg Glu Ile 690 695 700 Tyr Asp Val Asp Val Pro Val Gly Val Ile Thr Gly Pro Ala Met Asp 705 710 715 720 Leu Ala Ala Leu Ala Glu Tyr Ile Ser Ser Ala Arg Asp Asn Asp Ser 725 730 735 Asp Thr Ala Thr Phe Ala Ser Ile His Gly Arg Gly Ala Thr Val Ala 740 745 750 Glu Ala Ser Asp Leu Arg Leu Ser Ala Phe Leu Asp Asp Ala Leu Leu 755 760 765 Asp Ala Ala His His Ile Pro Gly Pro Arg Glu Gln Thr Ser Thr Val 770 775 780 Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu 785 790 795 800 Trp Leu Glu Arg Met Ala Glu Ile Gly Gly Lys Val Val Cys Leu Val 805 810 815 Arg Gly Arg Ser Asp Ser Asp Ala Arg Ala Arg Leu Asp Ala Ala Phe 820 825 830 Asp Ser Gly Asp Ala Glu Leu Ser Glu Arg Tyr Arg Thr Leu Ala Asp 835 840 845 Ala Ala Leu Glu Val Val Ala Gly Asp Leu Gly Thr Pro Arg Phe Gly 850 855 860 Leu Gly Asp Glu Asp Phe Arg Thr Leu Ser Glu Arg Val Asp Arg Ile 865 870 875 880 Val His Pro Ala Ala Leu Val Asn His Ala Leu Pro Tyr Glu His Leu 885 890 895 Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Arg Leu Ala Leu 900 905 910 Thr His His Val Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala 915 920 925 Ala Gly Val Glu Asp Phe Arg Glu Asn Gly Asp Ile Arg Ala Asp Ser 930 935 940 Pro Ser Arg Ala Val Asp Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser 945 950 955 960 Lys Trp Ala Gly Glu Val Leu Leu Arg Asn Ala Phe Asp Glu Phe Gly 965 970 975 Leu Pro Val Ser Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Thr 980 985 990 Trp Thr Gly Gln Leu Asn Val Pro Asp Val Phe Thr Arg Leu Ile Leu 995 1000 1005 Ser Val Val Glu Thr Gly Leu Ala Pro His Thr Phe Tyr Ala Thr 1010 1015 1020 Asp Thr Gly Ala Pro Thr Asp Glu Lys Gly Arg Pro Leu Ala His 1025 1030 1035 Tyr Asp Gly Leu Pro Ala Asp Phe Ser Ala Ser Ala Ile Thr Ser 1040 1045 1050 Ile Ala Gly Gly Asp Thr Ser Gly Tyr Arg Thr Phe Asp Ile Leu 1055 1060 1065 Asn Pro His Asp Asp Asp Ile Ser Leu Asp Thr Phe Val Asp Trp 1070 1075 1080 Ile Arg Ala Ala Gly Arg Asp Ile Glu Ile Val Asp Asn Tyr Asp 1085 1090 1095 Glu Trp Phe Glu Arg Phe Asn Ala Ala Val Glu Ala Leu Pro Glu 1100 1105 1110 Lys Gln Arg Ser His Ser Leu Leu Pro Leu Ile Asp Ser Tyr Ala 1115 1120 1125 His Pro Gln His Pro Ser Ser Gly Ala Met Leu Pro Ala Asp Glu 1130 1135 1140 Phe Ala Ser Ala Val Gly Asp Ile Pro His Leu Gly Arg Glu Leu 1145 1150 1155 Ile Glu Lys Tyr Leu Ser Asp Leu Val Ala Leu Glu Leu Val Ser 1160 1165 1170 Thr Arg 1175 <210> 229 <211> 1177 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium dioxanotrophicus <400> 229 Met Thr Asp Asp Ala Arg Gln Gln Arg Leu Val Gln Arg Ile Gln Gln 1 5 10 15 Leu His Ala Thr Asp Pro Gln Phe Arg Ala Ala Ala Pro Asp Pro Asp 20 25 30 Val Ser Leu Arg Ile Gln Asp Pro Glu Leu Arg Leu Trp Gln Ala Ile 35 40 45 Asp Ala Cys Leu Thr Gly Tyr Ala Asp Arg Pro Ala Leu Gly Leu Arg 50 55 60 Ser Arg Glu Val Val Arg Asp Pro Ala Thr Gly Arg Thr Thr Thr Ser 65 70 75 80 Leu Leu Ala Gly Phe Asp Thr Ile Thr Tyr Gly Arg Leu Arg Asp Asn 85 90 95 Val Val Ala Leu Thr Asn Thr Trp His Ala Ser Gly Phe Lys Pro Gly 100 105 110 Asp Phe Ile Ala Val Leu Gly Phe Thr Ser Ile Gly Tyr Thr Val Ile 115 120 125 Gln Leu Ala Cys Ala Arg Leu Gly Ala Val Phe Val Pro Leu Gln Thr 130 135 140 Ser Ser Ser Ala Arg Gln Leu Ala Pro Ile Ile Ala Glu Thr Thr Pro 145 150 155 160 Arg Ile Phe Ala Ala Ser Val Glu Ser Leu Asp Thr Ala Val Glu Leu 165 170 175 Ile Ile Glu Ala Pro Ser Val Gln Arg Leu Val Val Phe Asp Tyr Ser 180 185 190 Glu Ala Asp Asp Asp Gln Arg Glu His Val Glu Ala Ala Thr Ala Arg 195 200 205 Leu Ala Ala Ala Gly Arg Ala Val Glu Val Val Pro Leu Val Ala Asp 210 215 220 Met Asp Ala Gly Arg Ser Met Ala Glu Ala Ala Pro Phe Leu Pro Ala 225 230 235 240 Pro Gly Glu Asn Pro Leu Ala Thr Leu Val Tyr Thr Ser Gly Ser Thr 245 250 255 Gly Ala Pro Lys Gly Ala Met Tyr Thr Thr Asp Leu Met Thr Arg Leu 260 265 270 Trp Gln Arg Pro Arg Ser Pro Ser Leu Asp Ile Gly Ile Glu Ile Pro 275 280 285 Ala Ile His Leu Gln Tyr Met Pro Leu Ser His Val Tyr Gly Met Ala 290 295 300 Trp Leu Ile Ser Thr Leu Thr Ser Gly Gly Ile Gly Tyr Phe Ala Ala 305 310 315 320 Lys Ser Asp Met Ser Thr Leu Phe Asp Asp Ile Thr Leu Val Arg Pro 325 330 335 Thr Ala Leu Asn Leu Val Pro Arg Val Cys Asp Met Phe Phe Arg Arg 340 345 350 Tyr Arg Lys Glu Leu Asp Gln Arg Thr Ala Ala Glu Pro Thr Ala Ala 355 360 365 Asp Leu Glu Glu Thr Val Lys Ala Glu Leu Arg Glu Asp Phe Leu Gly 370 375 380 Gly Arg Val Ile Ser Ala Met Cys Gly Ser Ala Pro Leu Ser Lys Asp 385 390 395 400 Met His Ala Phe Val Glu Ser Leu Leu Asp Thr Ala Val Ser Asp Gly 405 410 415 Tyr Gly Ser Thr Glu Asn Gly Gly Gly Ile Met Arg Asn Gly Val Val 420 425 430 Gln Arg Pro Pro Val Thr Glu Tyr Lys Leu Val Asp Val Pro Glu Leu 435 440 445 Gly Tyr Ala Thr Thr Asp Lys Pro His Pro Arg Gly Glu Leu Tyr Leu 450 455 460 Lys Thr Thr Thr Leu Ile Pro Gly Tyr Tyr Lys His Pro Glu Leu Ser 465 470 475 480 Ala Asp Ile Phe Asp Ala Asp Gly Phe Tyr Lys Thr Gly Asp Val Met 485 490 495 Ala Glu Ile Gly Pro Asp His Leu Val Tyr Leu Asp Arg Arg Asn Asn 500 505 510 Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ser Asn Leu Glu 515 520 525 Ala Ser Tyr Ser Thr Ser Pro Tyr Ile Arg Gln Ile Tyr Ile Tyr Gly 530 535 540 Ser Ser Asp Gln Pro Phe Leu Leu Ala Val Ile Val Pro Asn Ala Asp 545 550 555 560 Gly Val Gly Ala Gly Asp Ala Arg Ser Leu Ile Thr Asn Ser Leu Gln 565 570 575 His Ile Ala Ala Glu Asn His Leu Asn Pro Tyr Glu Ile Pro Arg Asp 580 585 590 Phe Leu Leu Glu Pro Glu Pro Phe Thr Arg Asp Asn Gly Leu Leu Ser 595 600 605 Gly Val Gly Lys Leu Leu Arg Pro Ala Leu Lys Arg His Tyr Gln Asp 610 615 620 Arg Leu Asp Ala Ile Tyr Ala Glu Ile Thr Ala Gly Gln Asp Asn Gln 625 630 635 640 Leu Asp Ala Leu Arg Ala Ala Ser Arg His Gln Pro Thr Ile Glu Thr 645 650 655 Val Arg Gly Ala Ala Ala Ala Thr Leu Gly Leu Glu Thr Gly Gly Leu 660 665 670 Asp Leu Pro Ala Asp Ala Lys Phe Ile Asp Leu Gly Gly Asp Ser Leu 675 680 685 Ser Ala Phe Ser Phe Ala Thr Leu Leu Glu Gly Ile Phe Ser Ile Asp 690 695 700 Val Pro Val Gln Thr Ile Val Ser Pro Thr Ala Thr Leu Thr Thr Thr 705 710 715 720 Ala Glu Tyr Val Asp Gly Glu Arg Gln Ser Ala Ser Thr Arg Pro Thr 725 730 735 Phe Ala Ser Val His Gly Arg Asp Ala Glu Val Ala Lys Ala Thr Asp 740 745 750 Leu Thr Leu Asp Lys Phe Ile Asp Ala Ala Thr Leu Ala Ala Ala Pro 755 760 765 Thr Leu Pro Ala Pro Ser Ala Thr Val Asn Thr Val Leu Met Thr Gly 770 775 780 Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Asp Trp Leu Glu Arg 785 790 795 800 Leu Ala Pro Thr Gly Gly Arg Leu Ile Cys Leu Ala Arg Gly Ala Asp 805 810 815 Pro Ile Ala Ala Arg Gln Arg Ile Glu Ala Ala Ile Asp Ser Gly Asp 820 825 830 Glu Thr Leu Ser Lys Arg Phe Arg Glu Leu Ala Asp Lys His Leu Glu 835 840 845 Val Leu Val Gly Asp Val Gly Ala Ala Asn Leu Gly Val Asp Thr Ala 850 855 860 Thr Trp Lys Arg Leu Ala Asp Ser Val Asp Leu Ile Val His Ser Ala 865 870 875 880 Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn 885 890 895 Ala Val Gly Thr Ala Glu Ile Ile Lys Leu Ala Ile Thr Asp Arg Leu 900 905 910 Lys Gly Val Asn Tyr Ile Ser Thr Val Ala Val Thr Ala Leu Pro Asp 915 920 925 Gly Thr Tyr Val Gly Glu Asp Val Asp Val Arg Ala Ala Ser Pro Ala 930 935 940 Arg Ser Leu Gly Ala Ala Tyr Ala Gly Gly Tyr Ala Thr Ser Lys Trp 945 950 955 960 Ala Gly Glu Val Leu Leu Arg Glu Ala Asn Asp Leu Cys Gly Leu Pro 965 970 975 Val Thr Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Thr Tyr Ser 980 985 990 Gly Gln Val Asn Val Thr Asp Met Phe Thr Arg Leu Ile Phe Ser Ile 995 1000 1005 Val Ala Thr Gly Leu Ala Pro Lys Ser Phe Tyr Thr Leu Asp Ala 1010 1015 1020 Ala Gly Asn Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Ala Asp 1025 1030 1035 Phe Thr Ser Ala Ala Ile Thr Ala Leu Gly Ala Ala Ser Thr Thr 1040 1045 1050 Gly Tyr His Thr Tyr Asn Val Leu Asn Thr His Asp Asp Gly Ile 1055 1060 1065 Ser Leu Asp Glu Phe Val Asp Trp Leu Ile Ala Gln Gly Leu Pro 1070 1075 1080 Ile Glu Arg Ile Asp Asp Tyr Asp Glu Trp Arg Glu Arg Phe Glu 1085 1090 1095 Glu Ala Met Lys Ala Leu Pro Glu Asp Gln Arg Lys Asn Ser Val 1100 1105 1110 Leu Pro Leu Met Ser Ala Tyr Ala His Pro Ala Pro Pro Thr Gly 1115 1120 1125 Gly Val Ala Met Pro Ala Glu Lys Phe Arg Ala Ala Val Gln Ser 1130 1135 1140 Ala Gly Ile Gly Ala Gly Arg Asp Val Pro His Leu Ser Glu Glu 1145 1150 1155 Leu Ile Ala Lys Tyr Ile Ala Asp Leu Arg Gln Leu Gly Leu Leu 1160 1165 1170 His Asp Ala Gly 1175 <210> 230 <211> 1168 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium kubicae <400> 230 Met Phe Ala Asn Asp Pro Gln Phe Arg Ala Ala Ala Val Ile Pro Glu 1 5 10 15 Val Thr Gln Ala Ala His Arg Pro Gly Leu Arg Leu Ser Glu Ile Val 20 25 30 Asp Thr Tyr Leu Gln Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg 35 40 45 Ala Gly Glu Val Thr Arg Asp Asp Thr Thr Gly Asn Ala Thr Thr Thr 50 55 60 Leu Leu Ser Gly Phe Glu Thr Ile Thr Tyr Arg Glu Leu Arg Glu Arg 65 70 75 80 Val Val Ala Leu Ala Asn Ala Trp His Ala Gly Leu Pro Gly Gly Phe 85 90 95 Thr Pro Gly Asp Phe Val Ala Val Leu Gly Phe Thr Ser Val Asp Tyr 100 105 110 Ala Val Asn Tyr Leu Ala Cys Ile Arg Leu Gly Ala Val Phe Val Pro 115 120 125 Leu Gln Thr Ser Ser Thr Ala Ala Gln Leu Lys Pro Ile Val Thr Glu 130 135 140 Thr Gln Pro Arg Val Phe Ala Val Ser Val Glu Ser Leu Glu Val Ala 145 150 155 160 Val Asp Val Ile Ser Asp Val Ala Ser Val Gln Arg Leu Val Val Phe 165 170 175 Asp Tyr Thr Gly Glu Asp Asp Ser Gln Arg Gln Arg Phe Glu His Ala 180 185 190 Thr Ala Arg Leu Val Asp Ala Gly His Arg Ala Gln Val Val Ser Leu 195 200 205 Ala Ala Glu Leu Glu Ser Gly Arg Thr Leu Glu Pro Asn Pro Ala Phe 210 215 220 Val Pro Ala Ala Gly Glu Asn Pro Leu Ala Thr Leu Ile Tyr Thr Ser 225 230 235 240 Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr Thr Ser Asp Met Lys 245 250 255 Thr Arg Leu Trp Gln Arg Pro His Ser Pro Ser Val Asp Ile Gly Ile 260 265 270 Gln Ile Pro Ala Ile His Leu Gln Tyr Met Pro Leu Ser His Val Tyr 275 280 285 Gly Leu Glu Trp Leu Ile Ala Thr Leu Ser Ser Gly Gly Ile Gly Tyr 290 295 300 Phe Ala Ala Lys Ser Asp Met Ser Thr Leu Phe Glu Asp Ile Ala Leu 305 310 315 320 Val Arg Pro Thr Ala Leu Asn Leu Val Pro Arg Val Cys Asp Met Phe 325 330 335 Phe Arg Arg Tyr Arg Arg Glu Leu Asp Gln Arg Ser Ala Gly Gly Leu 340 345 350 Thr Glu Glu Gln Leu Asp Asp Met Val Lys Ala Glu Leu Arg Gln Asp 355 360 365 Phe Ile Gly Gly Arg Val Leu Ser Ala Met Cys Gly Ser Ala Pro Leu 370 375 380 Ser Lys Gln Met His Ala Phe Met Glu Ser Leu Leu Asp Val Ser Val 385 390 395 400 Thr Asn Gly Tyr Gly Ala Thr Glu Thr Gly Gly Gly Ile Leu Arg Asn 405 410 415 Gly Ile Ile Arg Arg Pro Pro Val Thr Glu Tyr Lys Leu Val Asp Val 420 425 430 Pro Glu Leu Gly Tyr Phe Thr Thr Asp Lys Pro His Pro Arg Gly Glu 435 440 445 Leu His Val Lys Ala Thr Thr Val Ile Pro Gly Tyr Phe Lys His Pro 450 455 460 Glu Leu Ser Ala Gln Ile Phe Asp Asp Asp Gly Phe Tyr Lys Thr Gly 465 470 475 480 Asp Ile Met Ala Glu Val Gly Pro Asp His Leu Val Tyr Leu Asp Arg 485 490 495 Ser Asn Asn Val Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ser 500 505 510 Gln Leu Glu Ala Thr Phe Ser Thr Ser Pro Tyr Ile Arg Gln Ile Phe 515 520 525 Leu Tyr Gly Ser Ser Glu Gln Pro Phe Leu Leu Ala Val Ile Val Pro 530 535 540 Asn Thr Asp Ala Ile Gly Asp Ala Asp Pro His Ala Leu Ile Ala Glu 545 550 555 560 Ser Leu Gln Arg Ile Ala Gly Glu Ala His Leu Asn Ala Tyr Glu Val 565 570 575 Pro Arg Asp Phe Leu Leu Glu Ser Glu Arg Phe Thr Arg Asp Asn Gly 580 585 590 Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Ala Leu Lys Ala Arg 595 600 605 Tyr Gly Glu Arg Leu Glu Ala Met Tyr Ala Asp Ile Glu Ala Ser Gln 610 615 620 Gly Asn Gln Leu Asp Glu Leu Arg Ala Ala Ser Arg Glu Leu Pro Thr 625 630 635 640 Leu Asp Thr Val Arg Arg Ala Ala Ala Ala Thr Leu Gly Val Pro Val 645 650 655 Asp Asp Gly Leu Gly Ala Asp Ala Arg Phe Ile Glu Leu Gly Gly Asp 660 665 670 Ser Leu Ser Ala Phe Ser Phe Ala Thr Leu Leu Glu Ser Ile Tyr Asp 675 680 685 Ile Asp Val Pro Val Gln Thr Ile Val Ser Pro Thr Ala Thr Leu Ala 690 695 700 Thr Ile Ala Lys Tyr Ile Asp Gly Glu Arg Thr Ser Val Ser Thr Arg 705 710 715 720 Pro Thr Phe Ala Ser Val His Gly Arg Gly Ala Thr Val Ala Arg Ala 725 730 735 Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Asp Thr Leu Thr Ala 740 745 750 Ala Arg Asp Met Thr Ala Pro Ser Gly Pro Val Asn Thr Val Leu Leu 755 760 765 Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu 770 775 780 Glu Arg Leu Ala Ala Ser Gly Gly Thr Val Ile Cys Leu Ala Arg Gly 785 790 795 800 Ala Asp Pro Ile Ala Gly Arg Gln Arg Ile Glu Ala Ala Met Asp Ser 805 810 815 Gly Asp Asp Glu Leu Cys Ser Arg Phe Arg Glu Leu Ala Asp Lys His 820 825 830 Leu Lys Val Leu Val Gly Asp Val Gly Ala Ala Asn Leu Gly Leu Asp 835 840 845 Gln Ala Thr Tyr Asp Arg Leu Ala Glu Ser Val Asp Leu Ile Val His 850 855 860 Ser Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly 865 870 875 880 Pro Asn Val Val Gly Thr Ser Glu Ile Ile Lys Leu Ala Ile Thr Lys 885 890 895 Arg Leu Lys Pro Ile Asn Tyr Ile Ser Thr Val Ala Val Thr Ala Leu 900 905 910 Pro Asp Gly Gly Phe Leu Gly Glu Asp Val Asp Val Arg Ser Ala Ser 915 920 925 Pro Ser Arg Ser Leu Asp Glu Ser Tyr Ala Ser Gly Tyr Ala Thr Ser 930 935 940 Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly 945 950 955 960 Val Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Thr Arg 965 970 975 Tyr Ser Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg Leu Met Leu 980 985 990 Ser Val Val Ala Thr Gly Leu Ala Pro Arg Ser Phe Tyr Gln Leu Asp 995 1000 1005 Ala Ser Gly Asn Pro Gln Arg Ala His Tyr Asp Gly Leu Pro Ala 1010 1015 1020 Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu Gly Gly His Cys Thr 1025 1030 1035 Glu Gly Tyr His Thr Tyr Asn Val Leu Asn Thr His Asp Asp Gly 1040 1045 1050 Val Ser Leu Asp Thr Phe Val Asp Trp Leu Val Ala Ser Gly His 1055 1060 1065 His Ile Asp Arg Ile Asp Asp Tyr Arg Asp Trp Leu Thr Arg Phe 1070 1075 1080 Glu Ala Ala Met Lys Ala Leu Pro Glu Thr Gln Arg Arg Asn Ser 1085 1090 1095 Leu Leu Pro Leu Met Thr Ala Tyr Ala Lys Pro Gly Lys Pro Thr 1100 1105 1110 Gln Gly Thr Gly Val Pro Ala Glu Lys Phe Arg Ala Ala Val Gln 1115 1120 1125 Ser Ala Gly Ile Gly Ala Thr Lys Asp Val Pro His Leu Asp Glu 1130 1135 1140 Ala Leu Ile Asp Lys Tyr Val Thr Asp Leu Glu Gln Leu Gly Leu 1145 1150 1155 Leu Asp Ala His Ala Gly Ala Ser Ala Arg 1160 1165 <210> 231 <211> 1156 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium colombiense <400> 231 Met Leu Arg Ser Arg Ile Ala Glu Leu Cys Asp Glu Asp Pro Glu Val 1 5 10 15 Asn Arg Ser Arg Pro Ser Pro Ser Val Asp Ala Ala Leu Arg Arg Pro 20 25 30 Arg Leu Lys Leu Ala Glu Ile Val Gln Thr Ala Met Glu Gly Tyr Ala 35 40 45 Asp Arg Pro Ala Val Gly Gln Arg Arg Arg Glu Phe Val Thr Asp Pro 50 55 60 Ala Thr Ser Arg Thr Ser Thr Arg Leu Leu Pro Glu Phe Glu Thr Met 65 70 75 80 Ser Tyr Arg Gln Leu Trp Ser Arg Val Arg Ala Val Ala Thr Glu Trp 85 90 95 Arg Gly His Glu Arg His Pro Leu Ser Pro Gly Asp Phe Val Cys Ile 100 105 110 Leu Gly Phe Ala Ser Ile Asp Tyr Ala Thr Val Asp Leu Ala Cys Leu 115 120 125 Cys Ser Gly Ala Val Val Val Pro Leu Gln Ala Gly Ala Pro Ala Ala 130 135 140 Gln His Arg Leu Ile Met Thr Glu Thr Asn Pro Leu Ile Leu Ala Ala 145 150 155 160 Ala Leu Glu Tyr Leu Asp Ala Ala Val Glu Ala Val Leu Ala Gly Thr 165 170 175 Ala Pro Gln Arg Leu Met Val Leu Asp Tyr Glu Pro Arg Asp Pro Asp 180 185 190 Ala Lys Thr Arg Leu Asp Asp Ala Arg Ser Arg Leu Ala Asp Ala Gly 195 200 205 Val Arg Val Asp Thr Leu Asp Asp Val Ile Ala Ala Glu Ser Ser Ala 210 215 220 Pro Ser Val Pro Leu His Ile Pro Ala Ala Asp Asp Asp Pro Val Leu 225 230 235 240 Ala Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met 245 250 255 Tyr Thr Asp Ser Met Leu Asn Arg Thr Trp Leu Arg Pro Ser Gln Ala 260 265 270 Pro Val Ile Asn Val Asn Tyr Leu Pro Met Ser His Met Tyr Gly Arg 275 280 285 Gly Thr Leu Ala Tyr Ala Leu Ala Asn Gly Gly Thr Cys His Phe Ala 290 295 300 Ala Lys Ser Asp Met Ser Thr Leu Phe Asp Asp Ile Arg Leu Val Arg 305 310 315 320 Pro Thr Glu Leu Ser Leu Val Pro Arg Val Val Glu Leu Met Tyr Gln 325 330 335 His Phe Leu Arg Gln Arg Asp Arg Leu Leu Ser Ala Glu Asn Pro Ser 340 345 350 Asp Asp Val Glu Gln Asp Leu Lys Arg Glu Ile Arg Asn Ser Asp Phe 355 360 365 Gly Gly Arg Val Leu Ser Ala Asn Thr Ala Ser Ala Pro Leu Ala Pro 370 375 380 Glu Leu Arg Ser Phe Val Glu Thr Cys Leu Gly Val Arg Leu His Thr 385 390 395 400 Thr Tyr Gly Ser Thr Glu Met Gly Gly Val Leu Val Asp Asn Met Ile 405 410 415 Asn Arg Ala Asn Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu Leu 420 425 430 Gly Tyr Phe Thr Thr Asp Lys Pro Phe Pro Arg Gly Glu Leu Leu Ile 435 440 445 Lys Thr Arg Thr Met Thr Pro Gly Tyr Tyr Arg Arg Pro Glu Ala Thr 450 455 460 Ala Ser Thr Phe Asp Glu Asp Gly Phe Tyr Arg Ser Gly Asp Val Met 465 470 475 480 Ala Leu Val Gly Pro Asp Glu Leu Arg Tyr Leu Asp Arg Arg Asn Asn 485 490 495 Val Met Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala Gln Leu Glu 500 505 510 Asn Ala Phe Thr Thr Ser Pro Leu Ile His Gln Met Phe Ile Tyr Gly 515 520 525 Ser Ser Ala Glu Ala Phe Leu Leu Ala Val Val Val Pro Asp Arg Asp 530 535 540 Val Ile Ala Arg Ile Asp Ser Leu Gly Met Ala Gln Ile Lys Arg Leu 545 550 555 560 Ile Ala Glu Ser Leu His Gln Ile Ala Ala Gln Arg His Leu Asn Gly 565 570 575 Tyr Glu Val Pro Arg Asp Phe Leu Ile Glu Thr Glu Pro Phe Ser Val 580 585 590 Glu Asn Gly Leu Leu Thr Gly Ala Ala Lys Met Ala Arg Pro Gln Leu 595 600 605 Asn Arg Arg Tyr Gly Pro Arg Leu Asp Asp Leu Tyr Ala Gln Leu Arg 610 615 620 Ala Ala Gln Ala Ser Glu Leu Gln Ala Leu Arg Ala Asp Ala Arg Gln 625 630 635 640 Ala Pro Val Leu Asp Thr Val Leu Arg Ala Ala Ala Ala Ser Ile Gly 645 650 655 Leu Ser Arg Ser Gly Val Gly Arg Asp Ser Lys Phe Thr Asp Leu Gly 660 665 670 Gly Asp Ser Leu Ser Ala Leu Asn Phe Ser Gln Leu Leu Glu Glu Val 675 680 685 Leu Asp Val Thr Val Pro Val Gly Val Val Ile Asp Pro Thr Ala Asp 690 695 700 Leu Glu Arg Val Ala Arg Tyr Ile Glu Ala Gln Arg Thr Pro Glu Ala 705 710 715 720 Asn Thr Arg Pro Asn Phe Thr Ala Val His Gly Arg Asp Ala Ala Glu 725 730 735 Ile Gln Ala Cys Asp Leu Met Leu Asp Lys Phe Ile Asp Ile Gln Thr 740 745 750 Leu Thr Asp Ala Thr Arg Leu Arg Lys Pro Ser Thr Ala Ile Gln Ser 755 760 765 Val Leu Leu Thr Gly Val Thr Gly Phe Leu Gly Arg Phe Val Cys Leu 770 775 780 Asn Trp Met Gln Arg Leu Ala Asp Thr Gly Gly Lys Val Val Cys Leu 785 790 795 800 Val Arg Gly Ala Asp Ala Ile Glu Ala Arg Arg Arg Ile Asp Glu Ala 805 810 815 Val Gly Thr Asp Pro Ala Leu Arg Glu Arg Phe Gln Thr Leu Ala Asp 820 825 830 Asp His Leu Glu Val Leu Val Gly Asp Leu Gly Ser Pro Asn Val Gly 835 840 845 Leu Ser Gln Ala Glu Trp Asp Arg Leu Ala Gly Glu Ile Asp Leu Ile 850 855 860 Val His Pro Gly Ala His Val Asn His Met Leu Pro Tyr Ser Gln Leu 865 870 875 880 Phe Thr Ala Asn Val Val Gly Thr Ala Asp Leu Ile Lys Leu Ala Met 885 890 895 Thr Ala Lys Leu Lys Thr Phe His Tyr Val Ser Ser Ile Gly Ala Ala 900 905 910 Leu Thr Glu Asp Gly Thr Val Asp Glu Asp Ala Asp Met Arg Thr Ala 915 920 925 Cys Pro Lys Arg Ser Met Ile Thr Asn Glu Tyr Ala Gly Gly Tyr Ala 930 935 940 Ala Ser Lys Trp Ala Ala Glu Val Leu Met Arg Glu Ala His Asp Leu 945 950 955 960 Cys Gly Leu Pro Val Val Val Phe Arg Pro Asp Met Ile Met Ala Asp 965 970 975 Ser Arg Tyr Val Gly Gln Ile Asn Ser Pro Asp Leu Ile Thr Arg Leu 980 985 990 Leu Phe Ser Leu Ile Val Ser Gly Ile Ala Pro Arg Ser Phe Tyr Arg 995 1000 1005 Gly Gln His Cys Gly Gln Val Arg Pro His Phe Asp Gly Leu Pro 1010 1015 1020 Val Asp Phe Val Ala Lys Val Val Ser Glu Val Gly Ala Gln Cys 1025 1030 1035 Thr Thr Gly Tyr His Thr Tyr Asn Ile Val Asn Pro His Asp Asp 1040 1045 1050 Gly Val Ser Leu Asn Asp Phe Val Asp Trp Leu Ile Ala Ala Gly 1055 1060 1065 Asn Pro Ile Val Cys Val Asp Asp Tyr Asp Ala Trp Leu Ser Arg 1070 1075 1080 Phe Glu Ile Ala Leu Arg Gly Leu Pro Asp Lys Gln Arg His Gln 1085 1090 1095 Ser Val Leu Ala Leu Leu Asp Val Tyr Arg His Pro Leu Glu Pro 1100 1105 1110 Thr His Gly Ser Ala Ala Pro Cys Thr Arg Leu Glu Gln Ala Val 1115 1120 1125 Arg Ala Met Gly Ala Glu Ile Pro His Leu Ser Ala Glu Leu Ile 1130 1135 1140 Glu Lys Tyr Ser Ala Gly Leu Arg Leu Met Gly Leu Val 1145 1150 1155 <210> 232 <211> 1171 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium ahvazicum <400> 232 Met Ala Phe Val Gly Arg Ser Asp Val Lys Asp Pro Gly Ala Gln Gln 1 5 10 15 Asp Gln Trp Glu Arg Leu Ala Arg Arg Arg Glu Arg Leu Tyr Ala Glu 20 25 30 Asp Ala Gln Phe Ser Ala Thr Arg Pro Asp Glu His Ile Ala Ala Ala 35 40 45 Ala Arg Ala Pro Gly Leu Arg Ile Gly Glu Val Met Ala Thr Val Leu 50 55 60 Gln Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg Val Arg Glu Val 65 70 75 80 Thr Thr Asp Pro Ala Thr Gly Arg Ser Thr Val Asn Phe Leu Pro Arg 85 90 95 Phe Glu Thr Val Ser Tyr Ala Glu Leu Trp Ala Arg Val Gln Ala Val 100 105 110 Ala Gly Asp Trp His His His Gly Arg His Pro Leu Arg Thr Gly Asp 115 120 125 Phe Val Cys Val Leu Gly Phe Ala Ser Ile Asp Tyr Thr Ala Ile Glu 130 135 140 Cys Ala Cys Ile His Leu Gly Ala Val Val Val Pro Leu Gln Thr Ser 145 150 155 160 Ala Pro Ala Ala Gln His Ala Pro Ile Leu Asp Glu Thr Gln Pro Arg 165 170 175 Ile Phe Ala Val Gly Ile Asp Asn Leu Glu Ile Ala Val Glu Ala Val 180 185 190 Leu Ala Ala Ser Arg Thr Gly Thr Ala Pro Gln Arg Leu Ile Val Phe 195 200 205 Asp Tyr Glu Pro Arg Asp Asp Asp Gln Arg Ala Ser Tyr Glu Ala Ala 210 215 220 Arg Asp Arg Leu Ala Ala Thr Gly Thr Gly Leu Thr Ile Glu Thr Leu 225 230 235 240 Asp Asn Val Val Ala Gln Gly Gln Ser Leu Pro Ala Pro Pro Leu His 245 250 255 Val Ala Ala Ala Asp Glu Asp Pro Leu Ala Trp Val Phe Tyr Thr Ser 260 265 270 Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Phe Thr Glu Ser Leu Cys 275 280 285 Ile Gly Thr Trp Leu Ala Gln Ser Asp Gln Pro Val Ile Thr Leu Ser 290 295 300 Tyr Met Pro Met Ser His Leu Ile Gly Tyr Gly Tyr Val Ile Leu Thr 305 310 315 320 Leu Ala Asn Gly Gly Thr Ser Tyr Phe Ala Ala Arg Ser Asp Leu Ser 325 330 335 Thr Leu Phe Asp Asp Leu Ala Leu Val Arg Pro Thr Ser Met Ser Leu 340 345 350 Val Pro Arg Val Cys Glu Met Phe Tyr His His Tyr Gln Arg Glu Leu 355 360 365 Asp Arg Arg Ser Leu Thr Gly Glu Ala Ser Asp Glu Ala Ala Asp Glu 370 375 380 Leu Thr Thr Ala Ile Arg Glu Gln Ile Leu Gly Gly Arg Val Leu Ala 385 390 395 400 Val Gly Cys Gly Ser Ala Ala Leu Ser Pro Glu Ile Lys Glu Phe Met 405 410 415 Glu Val Val Leu Asp Gln His Leu Leu Ile Gly Tyr Ser Ser Thr Glu 420 425 430 Ile Ala Gly Arg Met Ile Val Ala Asp Glu His Val Leu Arg Pro Pro 435 440 445 Val Ile Asp Tyr Lys Leu Leu Asp Val Pro Glu Leu Gly Tyr Phe Ser 450 455 460 Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Ala Val Lys Ser Ala Arg 465 470 475 480 Phe Met Ala Gly Tyr Tyr Asn Arg Pro Asp Leu Thr Ala Thr Met Phe 485 490 495 Asp Ala Asp Gly Tyr Tyr Lys Thr Gly Asp Ile Met Ala Glu Val Gly 500 505 510 Pro Asp Arg Leu Arg Tyr Val Asp Arg Arg Asn Asn Val Ile Lys Leu 515 520 525 Ala Gln Gly Glu Phe Val Ala Val Ser Arg Leu Glu Ala Leu Tyr Ser 530 535 540 Thr Ser Ser Leu Ile His Gln Ile Tyr Ile Tyr Gly Asn Ser Glu Arg 545 550 555 560 Ser Phe Leu Leu Ala Val Ile Val Pro Ile Asp Thr Gly Val Gly Thr 565 570 575 Ser Leu Ile Ala Asp Ser Leu Arg Gln Ile Ala Arg Asp Asn Gly Leu 580 585 590 Asn Gly Tyr Glu Ile Pro Arg Asp Phe Leu Ile Glu Thr Glu Pro Phe 595 600 605 Ser Leu Thr Asn Gly Leu Leu Ser Gly Val Gly Lys Phe Leu Arg Pro 610 615 620 Arg Leu Lys Glu Arg Tyr Gly Glu Arg Leu Glu Gln Leu Tyr Ala Ala 625 630 635 640 Met Ala Asp Asp Gln Leu Gly Gln Leu Arg Ala Leu Arg Thr Gly Gly 645 650 655 Ala Asp Gln Pro Val Leu Ala Thr Val Ser Lys Ala Val Gln Ala Thr 660 665 670 Leu Gly Val Pro Ala Ala Asp Val Ser Pro Glu Ala Arg Phe Ile Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Thr Leu Leu Ala 690 695 700 Asp Ile Tyr Gly Val Glu Val Pro Val Gly Val Val Ile Asp Pro Thr 705 710 715 720 Gly Asp Leu Leu Arg Ile Thr Asp His Ile Glu Arg Gln Arg Asn Ser 725 730 735 Asp Val Pro Arg Pro Thr Phe Gly Ser Val His Asp Thr Ala Gly Arg 740 745 750 Glu Val Ser Ala Cys Asp Leu Arg Leu Asp Lys Phe Ile Asp Asp Asp 755 760 765 Ile Leu Lys Asn Ala Met Leu Leu Pro Ala Pro Thr Ser Glu Ile Arg 770 775 780 Thr Val Leu Leu Thr Gly Ser Thr Gly Phe Leu Gly Arg Phe Leu Gly 785 790 795 800 Leu Glu Trp Leu Gln Arg Leu Ala Asp Ser Gly Gly Thr Leu Val Cys 805 810 815 Leu Thr Arg Gly Ala Asp Ala Ala His Ala Arg Arg Arg Ile Glu Ala 820 825 830 Ala Leu Asp Ser Asp Pro Lys Leu Leu Asp Arg Phe Arg Ser Leu Ala 835 840 845 Glu Gly His Leu Glu Val Val Ala Gly Asp Ile Gly Glu Ala Gly Phe 850 855 860 Gly Ile Asp Asp Ala Thr Trp Arg Arg Met Ser Glu Thr Val Asp Leu 865 870 875 880 Ile Val His Pro Ala Ala His Val Asn His Val Leu Pro Tyr Arg Gln 885 890 895 Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Arg Leu Ala 900 905 910 Ile Thr Thr Lys Leu Lys Pro Val His Tyr Ile Ser Thr Leu Gly Val 915 920 925 Ser Ala Val Ala His Gln Leu Val Asp Glu Asp Thr Asp Ile Arg Arg 930 935 940 Ser Val Pro Glu Cys Val Ala Asp Asp Ser Tyr Ala Asn Gly Tyr Gly 945 950 955 960 Ile Ser Lys Trp Ala Gly Glu Val Leu Met Arg Glu Ala His Asp Leu 965 970 975 Cys Gly Leu Pro Val Ala Val Phe Arg Pro Gly Met Ile Leu Ala Asp 980 985 990 Ser Arg Tyr Ala Gly Gln Leu Asn Val Pro Asp Ile Phe Thr Arg Leu 995 1000 1005 Leu Phe Ser Leu Val Thr Thr Gly Val Ala Pro Arg Ser Phe Tyr 1010 1015 1020 Arg Thr Gly Ala Ala Arg Pro His Tyr Glu Gly Leu Pro Val Asp 1025 1030 1035 Phe Leu Ala Glu Ser Ile Ala Ala Ile Gly Pro Arg His Gly Ser 1040 1045 1050 Gly Phe Ala Thr Tyr Asn Thr Thr Asn Pro Tyr Asp Asp Gly Ile 1055 1060 1065 Ser Met Asp Thr Phe Val Asp Trp Ile Ile Ala Ala Gly Tyr Pro 1070 1075 1080 Val Glu Arg Ile Asp Asp Tyr Ser Ser Trp Leu Thr Arg Phe Glu 1085 1090 1095 Thr Ala Met Gly Ala Leu Pro Glu Arg Gln Arg Ala Gln Ser Val 1100 1105 1110 Leu Thr Val Leu Asp Val Tyr Arg Glu Pro Met Leu Ala Ile Ala 1115 1120 1125 Gly Ser Pro Val Pro Gly Ala Gln Phe Gln Ser Ala Val Ala His 1130 1135 1140 Ser Gly Arg Ala Ile Pro His Val Thr Gln Gln Leu Ile Glu Lys 1145 1150 1155 Tyr Leu Ala Asp Leu Glu Gln Ile Gly Ile Leu Ser Arg 1160 1165 1170 <210> 233 <211> 1167 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium colombiense <400> 233 Met Ala Phe Val Gly Arg Ser Asp Val Lys Asp Pro Gly Ala Gln Gln 1 5 10 15 Asp Gln Trp Glu Arg Val Ala Arg Arg Arg Glu Arg Leu Tyr Ala Asp 20 25 30 Asp Ala Gln Phe Arg Asn Thr Lys Pro Asp Asp Glu Ile Ala Ala Ala 35 40 45 Ala Arg Ala Pro Gly Leu Arg Ile Ala Glu Val Met Ala Thr Val Leu 50 55 60 Gln Gly Tyr Ala Gly Arg Pro Ala Leu Ala Gln Arg Ala Arg Glu Val 65 70 75 80 Val Thr Asp Pro Ala Thr Gly Arg Ser Leu Leu His Phe Leu Pro Arg 85 90 95 Phe Glu Thr Ile Thr Tyr Thr Asp Leu Trp Ala Arg Val Gln Ala Thr 100 105 110 Ala Ala Asp Trp His His His Gln Arg His Pro Val Arg Ala Gly Asp 115 120 125 Phe Val Cys Val Leu Gly Phe Ala Ser Ile Asp Tyr Thr Ala Leu Glu 130 135 140 Cys Ala Cys Ile His Leu Gly Ala Val Val Val Pro Leu Gln Thr Ser 145 150 155 160 Ala Pro Ala Ala Gln His Ala Pro Ile Leu Ala Glu Thr Arg Pro Arg 165 170 175 Ile Leu Ala Val Gly Ile Asp Asn Leu Ala Ser Ala Val Glu Ala Thr 180 185 190 Leu Ala Gly Thr Ala Pro Asp Arg Leu Ile Val Phe Asp Tyr Glu Pro 195 200 205 Gly Asp Asp Asp Gln Arg Ala Gly Phe Glu Ala Ala Val Ala Arg Leu 210 215 220 Ser Gly Ala Gly Ser Ala Leu Thr Ile Glu Thr Ile Asp Ala Val Ala 225 230 235 240 Thr His Gly Ala Val Leu Pro Pro Ala Pro Leu His Val Ala Pro Glu 245 250 255 Gly Glu Asp Pro Leu Ala Trp Val Phe Tyr Thr Ser Gly Ser Thr Gly 260 265 270 Thr Pro Lys Gly Ala Met Phe Thr Glu Ser Leu Cys Ile Gly Thr Trp 275 280 285 Leu Ala Gln Ser Asp Gln Pro Val Ile Thr Leu Ser Tyr Met Pro Met 290 295 300 Ser His Leu Ile Gly Tyr Gly Tyr Val Ile Leu Thr Leu Ala Asn Gly 305 310 315 320 Gly Thr Ser Tyr Phe Ala Ala Lys Ser Asp Leu Ser Thr Leu Phe Glu 325 330 335 Asp Leu Ala Leu Val Arg Pro Thr Ser Met Ser Leu Val Pro Arg Val 340 345 350 Cys Glu Met Phe Phe His His Tyr Gln Arg Glu Leu Asp Arg Ala Leu 355 360 365 Met Ala Gly Ala Asp Pro Asp Ala Ala Gly Ala Gln Ile Thr Thr Ala 370 375 380 Ile Arg Glu Glu Ile Leu Gly Gly Arg Val Leu Ala Val Gly Cys Gly 385 390 395 400 Ser Ala Ala Leu Ser Pro Glu Ile Lys Glu Phe Met Glu Glu Val Leu 405 410 415 Asp Gln His Leu Leu Ile Gly Tyr Ser Ser Thr Glu Ile Ala Gly Gly 420 425 430 Met Ile Val Ala Asp Glu His Val Leu Arg Pro Pro Val Ile Asp Tyr 435 440 445 Lys Leu Leu Asp Val Pro Glu Leu Gly Tyr Phe Asn Thr Asp Lys Pro 450 455 460 Tyr Pro Arg Gly Glu Leu Ala Val Lys Ser Ala Arg Phe Met Ala Gly 465 470 475 480 Tyr Tyr Asn Arg Pro Asp Leu Thr Ala Thr Met Phe Asp Glu Asp Gly 485 490 495 Tyr Tyr Lys Thr Gly Asp Ile Met Ala Glu Val Gly Pro Asp Arg Leu 500 505 510 Arg Tyr Val Asp Arg Arg Asn Asn Val Ile Lys Leu Ala Gln Gly Glu 515 520 525 Phe Val Ala Val Ser Arg Leu Glu Ala Leu Tyr Ser Thr Ser Pro Leu 530 535 540 Ile His Gln Ile Tyr Ile Tyr Gly Asn Ser Ala Arg Ser Phe Leu Leu 545 550 555 560 Ala Val Val Val Pro Thr Asp Val Gly Ala Asp Pro Ser Ala Ile Ala 565 570 575 Gln Ser Leu Arg Gln Val Ala Arg Asp Asn Gln Leu Asn Gly Tyr Glu 580 585 590 Leu Pro Arg Glu Phe Leu Ile Glu Thr Glu Pro Phe Ser Leu Ala Asn 595 600 605 Gly Leu Leu Ser Gly Val Gly Lys Phe Leu Arg Pro Lys Leu Lys Ala 610 615 620 Arg Tyr Gly Asp Arg Leu Glu Glu Leu Tyr Ala Arg Ile Ala Asp Asp 625 630 635 640 Gln Arg Gly Gln Leu Arg Val Leu Arg Thr Gly Gly Ala Asp Gln Pro 645 650 655 Val Leu Ser Thr Val Thr Lys Ala Val Gln Ala Thr Leu Gly Val Ala 660 665 670 Ala Ala Asp Val Ser Pro Glu Ala Arg Phe Ile Asp Leu Gly Gly Asp 675 680 685 Ser Leu Ser Ala Leu Thr Phe Ser Thr Leu Leu Ala Asp Ile Tyr Gly 690 695 700 Phe Glu Val Pro Val Gly Val Val Ile Asp Pro Thr Gly Asp Leu Leu 705 710 715 720 Thr Ile Ala Gly His Ile Glu Arg Gln Arg Ala Pro Gly Thr Gly Arg 725 730 735 Pro Thr Tyr Ala Ser Val His Gly Ala Ser Ala Thr Glu Val His Ala 740 745 750 Glu Asp Leu Thr Leu Asn Lys Phe Ile Asp Asp Asp Ile Leu Lys Ser 755 760 765 Ala Thr Leu Leu Ser Gln Pro Thr Ala Glu Val Arg Thr Val Leu Leu 770 775 780 Thr Gly Ala Thr Gly Phe Leu Gly Arg Phe Leu Ala Met Glu Trp Leu 785 790 795 800 Glu Gly Leu Ala Glu Ser Gly Gly Thr Leu Ile Cys Leu Thr Arg Gly 805 810 815 Ala Asp Ala Thr Gln Ala Arg Gln Arg Ile Glu Ala Val Leu Gly Ser 820 825 830 Asp Ser Ala Leu Leu Glu Arg Phe Arg Ala Leu Ala Ala Asp His Leu 835 840 845 Glu Val Val Ala Gly Asp Ile Gly Glu Pro Arg Phe Gly Leu Asp Glu 850 855 860 Ala Thr Trp Arg Arg Leu Val Asp Thr Val Asp Leu Val Val His Pro 865 870 875 880 Ala Ala His Val Asn His Val Leu Pro Tyr Arg Gln Leu Phe Ala Pro 885 890 895 Asn Val Val Gly Thr Ala Glu Ile Ile Arg Leu Ala Ile Thr Arg Arg 900 905 910 Leu Lys Pro Ile His Tyr Val Ser Thr Leu Gly Val Ser Ala Val Ala 915 920 925 His Gln Leu Val Asp Glu Asp Thr Asp Ile Arg Arg Ser Val Pro Ser 930 935 940 Cys Thr Ile Asp Asp Gly Tyr Ala Asn Gly Tyr Gly Ile Ser Lys Trp 945 950 955 960 Ala Gly Glu Val Leu Met Arg Glu Thr His Asp Leu Cys Gly Leu Pro 965 970 975 Ile Ala Val Phe Arg Pro Gly Met Ile Leu Ala Asp Ser Arg Tyr Ala 980 985 990 Gly Gln Leu Asn Val Pro Asp Ile Phe Thr Arg Leu Leu Phe Ser Leu 995 1000 1005 Val Thr Thr Gly Val Ala Pro Arg Ser Phe Tyr Arg Gly Gly Gly 1010 1015 1020 Gly Arg Pro His Tyr Glu Gly Leu Pro Val Asp Phe Leu Ala Asp 1025 1030 1035 Ala Ile Ala Ala Ile Gly Pro Gln His Gly Ser Ser Phe Asp Thr 1040 1045 1050 Tyr Asn Thr Thr Asn Pro His Asp Asp Ala Ile Ser Leu Asp Thr 1055 1060 1065 Phe Val Asp Trp Ile Ile Ala Ala Gly Tyr Pro Val Glu Lys Ile 1070 1075 1080 Asp Asp Tyr Ser Ala Trp Leu Ala Arg Phe Glu Thr Ala Met Arg 1085 1090 1095 Ala Leu Pro Glu Asn Pro Arg Gly Gln Ser Val Leu Ala Val Leu 1100 1105 1110 Asp Val Tyr Arg Glu Pro Met Ala Ala Val Ser Gly Ser Pro Val 1115 1120 1125 Pro Gly Glu Arg Phe Arg Ala Ala Val Arg Ala Ala Gly Arg Ala 1130 1135 1140 Ile Pro His Val Ser Arg Glu Leu Ile Asp Lys Tyr Leu Ala Asp 1145 1150 1155 Leu Gln Arg Ile Gly Val Leu Thr Arg 1160 1165 <210> 234 <211> 1131 <212> PRT <213> Artificial Sequence <220> <223> Clavibacter michiganensis subsp. michiganensis NCPPB 382 <400> 234 Met Ser Thr Glu Gln Met Gly Thr Glu Gln Met Gly Ser Gln His Glu 1 5 10 15 Asp Thr Ser Ile Glu Ala Ile Phe Ala Gln His Ala Asp Arg Thr Ala 20 25 30 Leu Arg Gln Arg Ser Gly Pro Asp Ile Thr Asp Met Gly Phe Arg Glu 35 40 45 Leu Trp Asp Arg Ala Gly Ala Leu Ala Ala Ala Leu Gly Glu Thr Val 50 55 60 Ser Ala Gly Asp Arg Ile Ala Val Leu Gly Thr Ala Thr Ala Asp Ala 65 70 75 80 Val Thr Leu Asp Leu Ala Ala Trp Ile Leu Gly Ala Val Ser Val Pro 85 90 95 Leu Gln Ala Ser Ala Pro Val Ala Ala Leu Arg Ala Ile Val Glu Glu 100 105 110 Thr Thr Pro Val Trp Ile Ala Ala Thr Ala Asp Gln Ala Ala Thr Ala 115 120 125 Arg Ala Val Ala Glu Ala Ser Gly Asp Gly Ile Arg Thr Met Arg Leu 130 135 140 Asp Thr Asp Thr Asp Ala Asp Thr Asp Thr Asp Ala Ala Leu Thr Leu 145 150 155 160 Gly Ala Leu Val Ala Arg Gly Ala Gly Leu Arg Arg Arg Ser Pro Trp 165 170 175 His Pro Ala Pro Gly Asp Asp Pro Leu Ala Leu Leu Leu Tyr Thr Ser 180 185 190 Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr Arg Ser Met Val 195 200 205 Glu Arg Met Trp His Ala Leu Arg Pro Asp Pro Ala Ala Pro Ala Asp 210 215 220 Ala Ser Thr Thr Ala Asp Asp Gly Asp Ala Ala Ala Ile Val Gly Tyr 225 230 235 240 Ala Tyr Leu Pro Met Ser His Leu Thr Gly Arg Ser Ser Leu Leu Ala 245 250 255 Thr Leu Gly Arg Gly Gly Thr Val Ala Leu Ala Thr Ser Thr Asp Leu 260 265 270 Ser Thr Leu Phe Asp Asp Leu Arg Thr Phe Ala Pro Thr Glu Phe Val 275 280 285 Phe Val Pro Arg Val Ala Glu Leu Val Arg Gln Glu Gly Asp Arg Glu 290 295 300 Glu Gln Arg Arg Leu Thr Ala Gly Ser Thr Asp Arg Asp Ala Val Arg 305 310 315 320 Ala Glu Val Gln Ala Asp Leu Arg Ala Arg Ala Phe Gly Gly Arg Ile 325 330 335 His Arg Ala Ile Cys Thr Ser Ala Pro Leu Thr Pro Glu Leu Arg Thr 340 345 350 Tyr Ile Glu Gly Cys Leu Gly Leu Thr Leu His Asp Leu Tyr Gly Ser 355 360 365 Thr Glu Ala Gly Gly Ile Leu His Asp Gly Val Ile Gln Gln Pro Pro 370 375 380 Val Thr Glu His Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Arg Thr 385 390 395 400 Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Val Lys Ser Ala Ser 405 410 415 Val Ile Ala Gly Tyr Phe Arg Arg Pro Asp Val Thr Ala Ala Val Phe 420 425 430 Asp Glu Asp Gly Phe Tyr Arg Thr Gly Asp Val Met Ala Gln Thr Gly 435 440 445 Pro Gly Thr Tyr Glu Tyr Val Asp Arg Arg Asn Asn Val Ile Lys Leu 450 455 460 Ser Gln Gly Glu Phe Val Ala Val Ala Ser Leu Glu Ala Thr Tyr Gly 465 470 475 480 Gly Thr Pro Glu Val His Gln Ile Ala Leu His Gly Asp Ser Arg His 485 490 495 Ala Phe Leu Val Ala Val Val Val Pro Ala Asp Pro Ala Ala Ser Glu 500 505 510 Arg Asp Ile Leu Ala Ala Leu Gln Arg Thr Ala Arg Glu His Gly Leu 515 520 525 Ala Pro Tyr Glu Val Pro Arg Gly Val Ile Val Glu Pro Asp Pro Phe 530 535 540 Thr Val Asp Gly Gly Met Leu Ser Asp Ala Gly Lys Leu Leu Arg Leu 545 550 555 560 Arg Leu Thr Gln Arg Tyr Gly Glu Arg Leu Ala Ala Leu Tyr Asp Ala 565 570 575 Leu Glu Glu Gln Gln Ser Gly Thr Leu Val Ala Ala Leu Arg Glu Arg 580 585 590 Ala Asp Asp Glu Pro Thr Val Asp Thr Val Val Arg Ala Ala Leu Leu 595 600 605 Leu Leu Gly Ala Glu Val Ser Pro Ala Thr Ala Ala Ala Ala Arg Phe 610 615 620 Ser Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Gly Ile 625 630 635 640 Leu Glu Asp Val Phe Gly Thr Glu Val Pro Val Gly Val Leu Thr Asp 645 650 655 Pro Thr Asn Asp Leu Ala Ala Val Ala Ala Tyr Val Glu Arg Ser Ala 660 665 670 Ser Asp Asp Arg Pro Thr Val Thr Arg Val His Gly Ala Gly Ala Ser 675 680 685 Thr Leu Arg Val Gly Asp Leu Arg Leu Asp Arg Met Leu Gly Gly Ile 690 695 700 Pro Thr Pro Val Pro Arg Ala Ser Ala Ala Arg Pro Gly Ser Arg Thr 705 710 715 720 Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Ala Ile 725 730 735 Asp Trp Leu Glu Arg Leu Ala Ala Thr Gly Gly Thr Leu Val Cys Ile 740 745 750 Val Arg Gly Ala Asp Asp Ala Asp Ala Arg Arg Arg Leu Glu Ala Ala 755 760 765 Phe Ala Ala Asp Pro Ala Phe Ala Arg Arg Phe Ala Glu Leu Ser Gly 770 775 780 Ser Leu Glu Val Leu Ala Gly Asp Val Ser Glu His Arg Leu Gly Leu 785 790 795 800 Asp Asp Glu Arg Trp Ile Asp Leu Ala Ala Arg Val Asp Leu Val Ala 805 810 815 His Ala Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Ala Leu Phe 820 825 830 Gly Pro Asn Val Val Gly Thr Ala Glu Ala Ile Arg Leu Ala Ile Ala 835 840 845 Ala Gly Ser Val Pro Val Thr Phe Val Ser Ser Val Ala Val Ala Gly 850 855 860 Gly Ala Arg Pro Gly Ala Thr Ala Asp Ala Glu Pro Ser Ala Pro Gly 865 870 875 880 Ala Leu Asp Glu His Ala Asp Ile Arg Ala Thr Ile Pro Glu Trp Ala 885 890 895 Val Gly Asp Glu Tyr Ala Asn Gly Tyr Gly Ala Ser Lys Trp Ala Ser 900 905 910 Glu Val Leu Leu Arg Glu Ala His Glu His His Gly Val Pro Val Ala 915 920 925 Val Phe Arg Ser Asp Met Ile Leu Ala His Pro Arg Trp Arg Gly Gln 930 935 940 Val Asn Leu Pro Asp Val Phe Thr Arg Leu Ile Trp Ser Val Leu Thr 945 950 955 960 Thr Gly Leu Ala Pro Ala Ser Phe Val Arg Arg Gly Pro Asp Gly Glu 965 970 975 Arg Gln Arg Ser His Tyr Asp Gly Leu Pro Ala Asp Phe Thr Ala Ala 980 985 990 Ala Ile Asp Gly Ile Gly Ala Ala Leu Thr Glu Gly His Arg Thr Phe 995 1000 1005 Asn Val Val Asn Pro His Asp Asp Gly Val Ser Leu Asp Thr Phe 1010 1015 1020 Val Asp Trp Ile Arg Glu Asp Gly His Asp Ile Ala Arg Val Asp 1025 1030 1035 Asp His Ala Glu Trp Val Asp Arg Phe Arg Ala Ala Leu Gly Ala 1040 1045 1050 Leu Pro Asp Ala Asp Arg Ala Arg Ser Val Leu Pro Leu Met His 1055 1060 1065 Ala Phe Ala Ser Pro Glu Glu Pro His Ala Gly Ser Ala Ile Pro 1070 1075 1080 Ala Asp Ala Phe Ala Glu Ala Val Arg Ala Val Arg Pro Leu Gly 1085 1090 1095 Ser Pro Asp Ile Pro Ser Leu Asp His Ala Leu Ile Ala Lys Val 1100 1105 1110 Ala Asp Asp Leu Ala Phe Leu Gly Leu Leu Ala Pro Ala Arg Ala 1115 1120 1125 Ala Ala Ala 1130 <210> 235 <211> 1165 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. bolletii 50594 <400> 235 Met Thr Asp Ala Ala Ala Leu Ala Ala Lys Leu Val Glu Ser Asp Pro 1 5 10 15 Gln Phe Gln Ala Ala Ile Pro Asp Pro Glu Val Met Asp Ser Leu Leu 20 25 30 Val Pro Gly Leu Arg Leu Ser Gln Val Leu His Ala Leu Leu Thr Gly 35 40 45 Tyr Ala Asp Arg Pro Val Met Gly Phe Arg Ser Arg Glu Ser Val Val 50 55 60 Asp Pro Ala Thr Gly Arg Thr Val Asp Arg Leu Leu Pro Ala Phe Glu 65 70 75 80 Thr Ile Thr Tyr Gly Glu Leu Arg Glu Asn Ile Ser Ala Ile Leu Ala 85 90 95 Glu Trp Gln His Gly Pro Asn Ala Met Gly Ala Asp Asp Phe Val Ala 100 105 110 Thr Ile Gly Phe Ser Ser Pro Asp Tyr Val Thr Leu Asp Leu Ala Thr 115 120 125 Leu Met Asn Gly Ser Val Ser Ile Pro Leu Gln His Asn Ala Ser Ala 130 135 140 Ala Gln Leu Arg Met Met Leu Glu Glu Thr Ser Pro Arg Leu Val Ala 145 150 155 160 Ala Ser Ala Asp Ser Leu Asp Leu Ala Val Glu Ala Ala Leu Gly Leu 165 170 175 Thr Glu Leu Arg Arg Val Val Val Phe Asp Tyr Arg Pro Asp Thr Asp 180 185 190 Asp His Arg Glu Lys Leu Ala Ala Ala Arg Gly Arg Leu Arg Glu Ala 195 200 205 Gly Met Asn Val Val Val Glu Ser Leu Ala Asp Val Ile Ala Lys Gly 210 215 220 Arg Gln Leu Pro Glu Pro Val Leu Tyr Thr Ala Gly Asp Asp Gln Arg 225 230 235 240 Thr Ala Leu Ile Met Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly 245 250 255 Ala Thr Phe Thr Glu Trp Thr Val Thr Arg Phe Trp Ser Ser Gly Ala 260 265 270 Ala Pro Asn Arg Asp Thr Pro Ile Ile Asn Val Asn Phe Leu Pro Leu 275 280 285 Asn His Leu Ala Gly Arg Val Gly Leu Leu Thr Ala Phe Ile Pro Gly 290 295 300 Gly Thr Cys Tyr Phe Val Pro Glu Ser Asp Leu Ser Thr Leu Phe Glu 305 310 315 320 Asp Trp Gln Leu Val Arg Pro Thr His Met Gly Val Val Pro Arg Val 325 330 335 Val Asp Met Leu Phe Gln His Tyr Gln Thr Arg Val Asp Ala Leu Ile 340 345 350 Ala Glu Gly Ala Asp Ala Thr Ser Ala Asp His Thr Ala Lys Thr Glu 355 360 365 Leu Arg Glu Asp Val Leu Gly Gly Arg Val Val Ala Gly Leu Leu Ala 370 375 380 Thr Ala Pro Leu Ser Pro Glu Met Lys Thr Phe Leu Glu Ser Ser Leu 385 390 395 400 Asn Phe His Leu Leu Asp Leu Tyr Gly Leu Thr Glu Val Gly Gly Val 405 410 415 Phe Arg Asp Gly Lys Ile Ser Arg Pro Pro Val Leu Asp Tyr Lys Leu 420 425 430 Ala Asp Val Pro Glu Leu Gly Tyr Tyr Thr Thr Asp Lys Pro His Pro 435 440 445 Arg Gly Glu Leu Leu Val Lys Ser Ala Thr Ala Thr Pro Gly Tyr Tyr 450 455 460 Lys Arg Pro Asp Val Thr Ala Glu Val Phe Asp Ala Asp Gly Tyr Tyr 465 470 475 480 Arg Thr Gly Asp Val Met Ala Glu Ile Ala Pro Asp Glu Leu Val Tyr 485 490 495 Val Asp Arg Arg Asn Asn Val Ile Lys Leu Ala Gln Gly Glu Phe Val 500 505 510 Ala Val Ala Asn Leu Glu Thr Val Tyr Val Gly Ala Pro Leu Val Arg 515 520 525 Gln Ile Phe Ile Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala Val 530 535 540 Ile Val Pro Thr Glu Glu Thr Leu Gln Arg Tyr Thr Asn Ser Pro Ile 545 550 555 560 Asp Met Lys Asn Ser Ile Arg Glu Ser Leu Gln Arg Thr Ala Arg Ala 565 570 575 Asn His Leu His Ser Tyr Glu Leu Pro Ala Asp Phe Ile Ile Glu Thr 580 585 590 Thr Pro Phe Thr Ile Glu Ser Gly Met Leu Ala Ala Val Gly Lys Pro 595 600 605 Ile Arg Pro Lys Met Ile Glu His Tyr Gly Gly Arg Leu Glu Gln Leu 610 615 620 Tyr Ala Asp Leu Ala Glu Ala Arg Val Gln Glu Leu Arg Leu Leu Arg 625 630 635 640 Asp Thr Ala Gln Gln Arg Pro Ile Ile Glu Thr Val Thr Glu Ala Ala 645 650 655 Gln Ala Leu Leu Gly Met Ser Ser Asp Ala Val Arg Pro Asp His His 660 665 670 Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Asn 675 680 685 Leu Leu Arg Asp Leu Phe Asp Val Asp Val Pro Val Gly Val Ile Thr 690 695 700 Gly Pro Ala Ala Asp Leu Arg Lys Leu Ala Ala Tyr Ile Glu Thr Ala 705 710 715 720 Arg Glu Ser Asn Val Ala Thr Ala Ala Ser Val His Gly Pro Asp Ala 725 730 735 Ala Val Ile Asn Ala Asp Glu Leu Thr Leu Asp Lys Phe Ile Asp Ala 740 745 750 Glu Thr Leu Gly Asn Ala Ser Thr Leu Pro Ala Pro Ser Gly Ala Val 755 760 765 His Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu 770 775 780 Cys Leu Glu Trp Leu Gln Arg Leu Ala Pro Ser Asp Gly Gln Leu Ile 785 790 795 800 Cys Leu Val Arg Gly Asp Asp Asn Asp Asp Ala Leu Ala Arg Leu Glu 805 810 815 Ala Ala Tyr Gly Asp Thr Asp Gln Ala Leu Leu Asp Glu Phe Arg Ala 820 825 830 Leu Ala Arg Arg His Leu Arg Val Val Ala Ala Asp Ile Ala Gln Pro 835 840 845 Arg Leu Gly Leu Gly Asp Ala Thr Trp Glu Gln Leu Ala Arg Glu Val 850 855 860 Asp Lys Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Asn Gln Leu Phe Gly Pro Asn Val Phe Gly Thr Ala Glu Val Ile Arg 885 890 895 Leu Ala Leu Thr Thr Arg Met Lys Pro Val Thr Tyr Leu Ser Thr Met 900 905 910 Ala Val Ala Met Ala Val Pro Asp Phe Asp Glu Asp Gly Asp Ile Arg 915 920 925 Thr Val Ser Pro Ala Arg His Ile Gly Ala Gly Tyr Ala Asn Gly Tyr 930 935 940 Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 945 950 955 960 Leu Cys Gly Leu Pro Ala Ser Val Phe Arg Ser Asp Met Ile Leu Thr 965 970 975 His Arg Leu Tyr Ser Gly Gln Leu Asn Val Thr Asp Ala Phe Thr Arg 980 985 990 Met Leu Leu Ser Leu Val Leu Thr Gly Ile Ala Pro Arg Ser Phe Tyr 995 1000 1005 Gln Gly Gly Ser Glu Gly Asp Arg Pro Arg Ala His Tyr Glu Gly 1010 1015 1020 Leu Pro Val Asp Phe Val Thr Glu Ala Ile Thr Thr Leu Gly Leu 1025 1030 1035 Ala Asn Ser Glu Gly Phe Arg Ser Tyr Asp Val Met Asn Pro His 1040 1045 1050 Asp Asp Gly Ile Ser Val Asp Thr Phe Val Asp Trp Leu Ile Glu 1055 1060 1065 Asp Gly His Ile Ile Asp Ile Ile Asp Asp Tyr Asp Glu Trp Leu 1070 1075 1080 Ser Arg Phe Glu Thr Ala Leu Arg Gly Leu Pro Asp Glu Leu Arg 1085 1090 1095 Arg Ser Ser Val Leu Pro Leu Leu Asp Ala Tyr Arg Ala Pro Gly 1100 1105 1110 His Pro Arg Arg Gly Ala Asp Ile Ser Thr Asp Met Phe Arg Lys 1115 1120 1125 Ala Val Arg Asp Asn Lys Ile Gly Ser Asp Gly Asp Ser Ala Asp 1130 1135 1140 Ile Pro His Ile Asp Arg Ala Leu Ile Ser Lys Tyr Ile Ser Asp 1145 1150 1155 Leu Arg Ala His Gly Leu Leu 1160 1165 <210> 236 <211> 1187 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium rhodesiae JS60 <400> 236 Met Thr Thr Glu Leu Arg Ile Asp Thr Asp Asp Val Asp Ala His Asn 1 5 10 15 Ile Gln Arg Pro Gly Gly Val Gly Glu Arg Val Thr Tyr Leu Tyr Glu 20 25 30 Asn Asp Arg Gln Phe Arg Ala Ala Ser Pro Arg Leu Asp Val Leu Asp 35 40 45 Ala Ala Arg Lys Pro Gly Leu Arg Leu Ser Gln Val Leu Arg Thr Leu 50 55 60 Ala Glu Gly Tyr Ser Asp Arg Pro Ala Val Gly Thr Arg Ala Val Gln 65 70 75 80 Thr Ile Gly Asp Glu Leu Thr Gly Arg Cys Ala Thr Gln Leu Leu Pro 85 90 95 Ala Phe Asn Thr Ile Ser Tyr Gly Glu Leu Trp Ser Arg Val Gln Ala 100 105 110 Val Ala Asn Ala Trp His His Asp Thr Gln Ala Pro Val Glu Ala Gly 115 120 125 Asp Phe Val Ala Thr Ile Gly Phe Ser Ser Ala Asp Tyr Leu Thr Ile 130 135 140 Asp Leu Val Cys Gly Tyr Leu Gly Leu Val Ala Val Pro Leu Gln His 145 150 155 160 Asn Thr Ser Ala Ser Arg Leu Val Pro Ile Leu Glu Glu Ser Ala Pro 165 170 175 Arg Val Leu Ala Val Ser Ala Asp Tyr Leu Asp Leu Ala Val Glu Ala 180 185 190 Ala Leu Gly Ser Gly Trp Leu Ser Arg Leu Val Val Phe Asp Tyr Arg 195 200 205 Pro Gln Asp Asp Asn His Arg Asp Arg Val Gln His Ala Arg Asp Ser 210 215 220 Leu Ala Gly Ala Gly Met Glu Val Ile Val Glu Thr Leu Pro Asp Ile 225 230 235 240 Ile Ala Arg Gly Thr Arg Ala Pro Glu Ala Pro Leu Phe Thr Asp Gly 245 250 255 Ser Asp Asp Arg Leu Ala Met Ile Leu Tyr Thr Ser Gly Ser Thr Gly 260 265 270 Ala Pro Lys Gly Ala Met Trp Thr Glu Arg Met Val Arg Thr Leu Trp 275 280 285 Thr Ile Pro Met Lys Ser Thr Glu Ser Val Val Ile Asn Leu Asn Phe 290 295 300 Met Pro Leu Asn His Leu Gly Gly Arg Leu Pro Leu Ala Ala Ser Phe 305 310 315 320 Gln Thr Gly Gly Thr Ser Tyr Phe Val Ala Glu Ser Asp Leu Ser Thr 325 330 335 Leu Phe Asp Asp Trp Met Leu Val Arg Pro Thr Asp Leu Gly Leu Val 340 345 350 Pro Arg Val Val Asp Met Leu Tyr Gln Arg Tyr Gln Gln Ile Val Asp 355 360 365 Arg Leu Ser Ala Asp Gly Leu Asp Leu Asp Thr Ala Glu Arg Thr Ala 370 375 380 Lys Thr Glu Ile Arg Glu Thr Leu Leu Gly Gly Arg Val Leu Gly Gly 385 390 395 400 Phe Val Ser Thr Ala Pro Leu Ser Ala Glu Met Arg Leu Phe Leu Glu 405 410 415 Ser Cys Leu Gln Ala Asp Ile Val Asp Thr Tyr Gly Leu Thr Glu Ile 420 425 430 Gly Ala Val Thr Thr Asp Gly Leu Val Val Arg Pro Leu Val Leu Asp 435 440 445 Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys 450 455 460 Pro His Pro Arg Gly Glu Leu Leu Val Lys Ser Ala Ala Ala Met Pro 465 470 475 480 Gly Tyr Tyr Lys Arg Pro Glu Ile Thr Ala Glu Val Phe Asp Ala Asp 485 490 495 Gly Tyr Tyr Arg Thr Gly Asp Ile Val Ala Glu Leu Glu Pro Asp Arg 500 505 510 Leu Ala Tyr Val Asp Arg Arg Asn Asn Val Ile Lys Leu Ser Gln Gly 515 520 525 Glu Phe Val Ala Val Ala Asn Leu Glu Ala Glu Phe Ala Arg Thr Pro 530 535 540 Leu Ile Arg Gln Ile Tyr Val Tyr Gly Asn Ser Glu Arg Ser Ser Leu 545 550 555 560 Leu Ala Val Val Val Pro Thr Glu Glu Ala Leu Ala Val His Gly Gly 565 570 575 Val Asn Asp Gln Leu Arg Ala Ala Val Arg Ala Ala Met Ser Gln Thr 580 585 590 Ala Arg Asp Ala Gly Leu Gln Pro Tyr Glu Val Pro Val Asp Phe Leu 595 600 605 Ile Glu Thr Glu Pro Phe Ser Val Ala Asp Gly Leu Leu Ser Gly Val 610 615 620 Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu Arg Tyr Gly Ala Glu Leu 625 630 635 640 Glu Ala Leu Tyr Asp Gln Val Asp Ala Ala Arg Ala Asp Asp Val Arg 645 650 655 Ala Leu Arg Asp Ala Ala Gln His Gln Pro Val Val Asp Thr Val Ile 660 665 670 Gln Ala Ala Ala Ala Leu Leu Gly Ile Pro Ser Ala Ser Val Thr Arg 675 680 685 Asp Asp His Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 690 695 700 Phe Ser Asn Leu Leu Gln Glu Leu Phe Gly Ile Glu Thr Pro Val Gly 705 710 715 720 Thr Leu Thr Gly Pro Thr Thr Thr Leu Gly Asp Val Ala Ser His Leu 725 730 735 Glu Gln Gly Ala Gly Asp Gly Val Ala Arg Pro Thr Ala Thr Ser Val 740 745 750 His His Ser Asp Thr Thr Ile His Ala Ala Asp Leu Thr Leu Asp Lys 755 760 765 Phe Leu Pro Ala Asn Leu Leu Asp Asp Ala Arg Ala Leu Pro Leu Pro 770 775 780 Val Asp Ala Glu Pro His Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr 785 790 795 800 Leu Gly Arg Phe Leu Ala Leu Glu Trp Leu Gln Arg Leu Ala Gln Thr 805 810 815 Gly Gly Thr Leu Ile Cys Leu Leu Arg Gly Ser Asp Asn Glu Ser Ala 820 825 830 Arg Met Arg Leu Glu Gln Ile Phe Asp Asp Gly Asp Ala Gln Met Ser 835 840 845 Glu Arg Phe His Asp Leu Ala Ala Glu His Leu Glu Val Ile Ala Gly 850 855 860 Asp Ile Ser Gln Pro Gln Leu Gly Val Asp Pro Gln Thr Trp Asp Ala 865 870 875 880 Leu Thr Gln Arg Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn 885 890 895 His Val Leu Pro Tyr Arg Gln Leu Phe Gly Pro Asn Val Val Gly Thr 900 905 910 Ala Glu Val Ile Ala Leu Ala Leu Ser Ser Arg Leu Lys Pro Ile Asn 915 920 925 Tyr Leu Ser Thr Val Ser Val Ala Met Thr Val Glu Pro Glu Arg Phe 930 935 940 Glu Glu Asp Gly Asp Ile Arg Thr Ile Ser Pro Thr Arg Pro Ile Asp 945 950 955 960 Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val 965 970 975 Leu Leu Arg Gln Ala His Asp Leu Cys Gly Leu Pro Val Ser Val Phe 980 985 990 Arg Ser Gly Met Ile Leu Ala Asp Arg Arg Tyr Asp Gly Gln Leu Asn 995 1000 1005 Val Ser Asp Met Phe Thr Arg Leu Ile Tyr Ser Leu Val Arg Thr 1010 1015 1020 Gly Leu Ala Pro Glu Ser Phe Tyr Gln Arg Ser Glu Ser Gly Glu 1025 1030 1035 Arg Thr Arg Ser His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala 1040 1045 1050 Glu Ser Ile Thr Thr Leu Gly Ala Gly Ala Arg Arg Gly Phe Arg 1055 1060 1065 Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly Ile Ser Leu Asp 1070 1075 1080 Val Phe Val Asp Trp Leu Ile Glu Thr Gly His Ser Ile Thr Arg 1085 1090 1095 Val Asp Asp Tyr Asp Asp Trp Leu Ser Gln Phe Asp Ser Ala Leu 1100 1105 1110 Arg Ala Leu Pro Asp Ala Gln Arg Gln Gln Ser Val Leu Pro Leu 1115 1120 1125 Leu Thr Ala Tyr Ser Arg Pro Glu Arg Pro Leu Leu Gly Ser Leu 1130 1135 1140 Ala Pro Ala Gln Val Phe Arg Lys Ala Val Gln Glu Asn Arg Ile 1145 1150 1155 Gly Ala Asp Gln Asp Ile Pro His Leu Ser Arg Gln Leu Ile Glu 1160 1165 1170 Lys Tyr Val Ser Gly Leu Arg Gly Gln Asp Leu Leu Pro Asn 1175 1180 1185 <210> 237 <211> 1164 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides immunogenum <400> 237 Met Thr Ala Gly Thr Ala Ala Arg Val Ala Glu Leu Phe Glu Ser Asp 1 5 10 15 Pro Gln Phe Arg Ala Ala Met Pro Asp Pro Glu Val Met Asp Ser Leu 20 25 30 Leu Val Pro Gly Leu Arg Leu Ser Gln Val Leu His Ala Leu Leu Ser 35 40 45 Gly Tyr Ala Asp Arg Pro Val Met Gly Phe Arg Ser Arg Glu Ser Val 50 55 60 Ile Asp Ala Glu Ser Gly Arg Thr Val Asp Arg Leu Leu Pro Ala Phe 65 70 75 80 Glu Thr Ile Thr Tyr Gly Gln Leu Leu Ala Asn Ile Ser Ala Leu Leu 85 90 95 Ala Glu Trp Gln His Gly Thr Val Pro Ile Gly Ala Gly Asp Phe Ile 100 105 110 Ala Thr Ile Gly Phe Ser Ser Pro Glu Tyr Val Thr Leu Asp Leu Ala 115 120 125 Ala Leu Met Asn Gly Ser Val Ser Ile Pro Leu Gln His Asn Thr Ser 130 135 140 Ala Ala Gln Leu Arg Met Met Leu Glu Glu Thr Asn Pro Arg Leu Ile 145 150 155 160 Ala Ala Ser Ala Asn Cys Leu Asp Leu Ala Val Glu Ala Ala Ile Gly 165 170 175 Leu Thr Asp Leu Arg Arg Leu Val Val Phe Asp Tyr Arg Ala Glu Thr 180 185 190 Asp Asp His Arg Glu Lys Leu Thr Thr Ala Thr Glu Arg Leu Lys Ser 195 200 205 Ala Gly Ile Glu Val Val Val Glu Pro Leu Ala Asp Val Ile Ala Ala 210 215 220 Gly Arg Asp Leu Pro Glu Pro Val Leu Tyr Thr Asp Gly Asp Asp Gln 225 230 235 240 Arg Thr Ala Leu Ile Met Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 245 250 255 Gly Ala Met Phe Thr Glu Trp Thr Val Thr Arg Phe Trp Ser Ser Gly 260 265 270 Ala Ala Pro Asn Arg Asp Thr Pro Ile Ile Asn Val Asn Phe Leu Pro 275 280 285 Leu Asn His Leu Ala Gly Arg Val Gly Leu Leu Thr Ala Phe Ile Pro 290 295 300 Gly Gly Thr Cys Tyr Phe Val Pro Glu Ser Asp Leu Ser Thr Leu Phe 305 310 315 320 Glu Asp Trp Gln Leu Ala Arg Pro Thr His Met Gly Val Val Pro Arg 325 330 335 Val Val Asp Met Leu Phe Gln His His Gln Thr Arg Val Asp Ala Leu 340 345 350 Met Ala Glu Gly Ala Asp Ala Asp Thr Ala Asp Arg Leu Ala Lys Thr 355 360 365 Glu Leu Arg Glu Asp Val Leu Gly Gly Arg Val Val Ala Gly Met Leu 370 375 380 Ala Thr Ala Pro Leu Ser Pro Glu Met Lys Ala Phe Leu Glu Ser Ser 385 390 395 400 Leu Asp Phe His Leu Leu Asp Leu Tyr Gly Leu Thr Glu Val Gly Gly 405 410 415 Val Phe Arg Asp Gly Lys Ile Ser Arg Pro Pro Val Leu Asp Tyr Lys 420 425 430 Leu Val Asp Val Pro Glu Leu Gly Tyr Tyr Thr Thr Asp Lys Pro His 435 440 445 Pro Arg Gly Glu Leu Leu Val Lys Ser Ala Thr Ala Thr Pro Gly Tyr 450 455 460 Tyr Lys Arg Pro Asp Val Thr Ala Glu Val Phe Asp Ala Asp Gly Tyr 465 470 475 480 Tyr Arg Thr Gly Asp Val Met Ala Glu Ile Ala Pro Asp Gln Leu Val 485 490 495 Tyr Leu Asp Arg Arg Asn Asn Val Ile Lys Leu Ala Gln Gly Glu Phe 500 505 510 Val Ala Val Ala Asn Leu Glu Thr Val Tyr Val Gly Ala Pro Leu Val 515 520 525 Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala 530 535 540 Val Val Val Pro Thr Glu Glu Ala Leu Arg Val His Pro Asp Pro Val 545 550 555 560 Glu Leu Lys Asn Ser Ile Arg Glu Ser Leu Gln Arg Thr Ala Arg Ala 565 570 575 Asn His Leu His Ser Tyr Glu Leu Pro Ala Asp Phe Ile Ile Glu Thr 580 585 590 Ala Pro Phe Thr Ile Glu Ser Gly Met Leu Ala Ala Val Gly Lys Pro 595 600 605 Ile Arg Pro Lys Met Ile Glu His Tyr Gly Gln Arg Leu Glu Gln Leu 610 615 620 Tyr Val Asp Leu Ala Glu Ala Arg Val Gln Glu Leu Arg Gln Leu Arg 625 630 635 640 Asp Thr Ala Arg Gln Arg Pro Val Ile Asp Thr Val Thr Glu Ala Ala 645 650 655 Gln Ala Leu Leu Gly Met Ser Ala Asp Ala Val Arg Pro Asp His His 660 665 670 Phe Leu Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Asn 675 680 685 Leu Leu Arg Asp Leu Phe Asp Val Glu Val Pro Val Gly Val Ile Thr 690 695 700 Gly Pro Ala Ala Asp Leu Arg Lys Leu Ala Ala Tyr Ile Lys Gln Ser 705 710 715 720 Glu Arg Ala Ala Pro Ala Thr Ala Ala Ser Val His Gly Pro Asn Thr 725 730 735 Gly Val Ile Arg Ala Asp Glu Leu Ala Leu Asp Lys Phe Leu Asp Ala 740 745 750 Glu Thr Leu Arg Asn Ala Thr Gln Leu Asp Ala Pro Ser Gly Ala Val 755 760 765 Asn Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu 770 775 780 Cys Leu Glu Trp Leu Gln Arg Met Ala Gln Thr Asp Arg Gln Leu Ile 785 790 795 800 Cys Leu Val Arg Gly Ala Asp Asp Asp Glu Ala Leu Ala Arg Leu Glu 805 810 815 Ala Ala Tyr Gly Glu Thr Asp Arg Ala Leu Leu Asp Glu Phe Arg Ala 820 825 830 Leu Ala Arg Arg His Leu Arg Val Ile Ala Ala Asp Ile Ala Gln Pro 835 840 845 Arg Phe Gly Leu Ala Asp Thr Asp Trp Ala Gln Leu Ala Arg Asp Val 850 855 860 Asp Lys Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Asn Gln Leu Phe Gly Pro Asn Ile Val Gly Thr Ala Glu Val Ile Arg 885 890 895 Leu Ala Leu Thr Thr Arg Met Lys Pro Val Thr Tyr Leu Ser Thr Met 900 905 910 Ala Val Ala Met Thr Val Pro Asp Phe Asp Glu Asp Gly Asp Ile Arg 915 920 925 Thr Val Ser Pro Thr Arg His Ile Gly Pro Gly Tyr Ala Asn Gly Tyr 930 935 940 Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 945 950 955 960 Leu Ser Gly Leu Pro Val Ser Val Phe Arg Ser Asp Met Ile Leu Thr 965 970 975 His Arg Arg Tyr Thr Gly Gln Leu Asn Val Thr Asp Ala Phe Thr Arg 980 985 990 Met Leu Leu Ser Leu Val Leu Thr Gly Ile Ala Pro Arg Ser Phe Tyr 995 1000 1005 Arg Gly Gly Asp Asp Gly Ile Arg Pro Arg Ala His Tyr Glu Gly 1010 1015 1020 Leu Pro Val Asp Phe Val Thr Glu Ala Ile Thr Ser Leu Gly Leu 1025 1030 1035 Ser Ala Thr Glu Gly Phe Arg Ser Tyr Asp Val Met Asn Pro His 1040 1045 1050 Asp Asp Gly Ile Ser Val Asp Thr Phe Val Asp Trp Leu Ile Glu 1055 1060 1065 Asp Gly His Ser Ile Asp Ile Ile Asp Asn Tyr Asp Glu Trp Leu 1070 1075 1080 Ser Arg Phe Glu Ile Ala Leu Arg Gly Leu Pro Asp Glu Leu Arg 1085 1090 1095 Arg Ala Ser Val Leu Pro Leu Leu Asp Ala Tyr Arg Val Pro Gly 1100 1105 1110 Asp Pro Arg Arg Ala Ala Ala Thr Pro Asn His Val Phe Arg Lys 1115 1120 1125 Ala Val Gln Glu Asn Lys Ile Gly Gly Glu Ser Ala Asp Ile Pro 1130 1135 1140 Gln Ile Asp Arg Ala Leu Ile Ala Lys Tyr Ile Gly Asp Leu Arg 1145 1150 1155 Ala His Gly Leu Leu Arg 1160 <210> 238 <211> 1162 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides saopaulense <400> 238 Met Thr Ala Gly Ala Ala Ala Arg Ala Ala Glu Leu Phe Glu Ser Asp 1 5 10 15 Pro Gln Phe Arg Gln Ala Leu Pro Asp Pro Asp Val Met Asp Ser Leu 20 25 30 Leu Val Pro Gly Leu Arg Leu Ser Gln Val Leu His Ala Leu Leu Thr 35 40 45 Gly Tyr Ala Asp Arg Pro Val Met Gly Phe Arg Ser Arg Glu Thr Val 50 55 60 Ile Asp Pro Ala Ser Gly Arg Ala Val Asp Arg Leu Leu Pro Ala Phe 65 70 75 80 Glu Thr Ile Thr Tyr Gly Arg Leu Leu Glu Asn Ile Ser Ala Ile Leu 85 90 95 Ala Glu Trp Gln His Gly Thr Asp Ala Ile Gly Ala Gly Asp Phe Val 100 105 110 Ala Thr Ile Gly Phe Ser Ser Pro Asp Tyr Val Thr Leu Asp Leu Ala 115 120 125 Thr Leu Met Asn Gly Ser Val Ser Ile Pro Leu Gln His Asn Ala Ser 130 135 140 Ala Thr Gln Leu Arg Ala Met Leu Glu Glu Thr Asp Pro Arg Leu Ile 145 150 155 160 Ala Ala Ser Ala Asp Cys Leu Asp Leu Ala Val Glu Ala Ala Met Gly 165 170 175 Leu Ser Asn Leu Arg Arg Val Val Val Phe Asp Tyr Arg Pro Asp Thr 180 185 190 Asp Asp His Arg Glu Lys Leu Ala Ala Ala Arg Ala Arg Leu Asp Ala 195 200 205 Ala Gly Met Glu Val Val Ile Glu Pro Leu Ala Gln Val Ile Ala Lys 210 215 220 Gly Arg Glu Leu Pro Glu Pro Val Leu Tyr Thr Asp Gly Asp Asp Gln 225 230 235 240 Arg Thr Ala Leu Ile Met Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 245 250 255 Gly Ala Met Phe Thr Glu Trp Thr Val Thr Arg Phe Trp Ser Ser Gly 260 265 270 Ala Ala Pro Asn Arg Asp Thr Pro Ile Ile Asn Val Asn Phe Leu Pro 275 280 285 Leu Asn His Leu Ala Gly Arg Val Gly Leu Leu Thr Ala Phe Ile Pro 290 295 300 Gly Gly Thr Cys Tyr Phe Val Pro Glu Ser Asp Leu Ser Thr Leu Phe 305 310 315 320 Glu Asp Trp Gln Leu Thr Arg Pro Thr His Met Gly Val Val Pro Arg 325 330 335 Val Val Asp Met Leu Phe Gln His Tyr Gln Thr Arg Val Asp Ala Leu 340 345 350 Val Ala Glu Gly Ala Asp Ala Asp Thr Ala Asp Arg Leu Ala Lys Thr 355 360 365 Glu Leu Arg Glu Asp Val Leu Gly Gly Arg Val Ile Ala Gly Met Leu 370 375 380 Ala Thr Ala Pro Leu Ser Pro Glu Met Lys Thr Phe Leu Glu Ser Ser 385 390 395 400 Leu Asn Phe His Leu Leu Asp Leu Tyr Gly Leu Thr Glu Val Gly Gly 405 410 415 Val Phe Arg Asp Gly Lys Ile Ser Arg Pro Pro Val Leu Asp Tyr Lys 420 425 430 Leu Val Asp Val Pro Glu Leu Gly Tyr Tyr Thr Thr Asp Lys Pro His 435 440 445 Pro Arg Gly Glu Leu Leu Ile Lys Ser Ala Thr Ala Thr Pro Gly Tyr 450 455 460 Tyr Lys Arg Pro Asp Val Thr Ala Glu Val Phe Asp Ala Asp Gly Tyr 465 470 475 480 Tyr Arg Thr Gly Asp Val Met Ala Glu Ile Ala Pro Asp Glu Leu Val 485 490 495 Tyr Val Asp Arg Arg Asn Asn Val Ile Lys Leu Ala Gln Gly Glu Phe 500 505 510 Val Ala Val Ala Asn Leu Glu Thr Val Tyr Val Gly Ala Pro Pro Val 515 520 525 Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ala Tyr Leu Leu Ala 530 535 540 Val Val Val Pro Thr Glu Glu Ala Leu Arg Ala His Pro Asp Pro Ile 545 550 555 560 Glu Leu Lys Asn Thr Ile Arg Glu Ser Leu Gln Arg Thr Ala Arg Ala 565 570 575 Asn His Leu His Ser Tyr Glu Leu Pro Ala Asp Phe Ile Ile Glu Thr 580 585 590 Thr Pro Phe Thr Ile Glu Ser Gly Met Leu Ala Ala Val Gly Lys Pro 595 600 605 Ile Arg Pro Lys Met Ile Glu Tyr Tyr Gly Asp Arg Leu Glu Gln Leu 610 615 620 Tyr Val Asp Leu Ala Glu Ala Arg Val Gln Glu Leu Arg Gln Leu Arg 625 630 635 640 Asp Thr Ala Gln Leu Arg Pro Val Ile Glu Thr Val Thr Glu Ala Ala 645 650 655 Gln Ala Leu Leu Gly Met Ser Ala Asp Ala Val Arg Pro Gln His His 660 665 670 Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Asn 675 680 685 Leu Leu Arg Asp Leu Phe Asp Val Glu Val Pro Val Gly Val Ile Thr 690 695 700 Gly Pro Ala Ala Asp Leu Arg Lys Leu Ala Ala Tyr Ile Glu His Glu 705 710 715 720 Arg Glu Ser Ser Thr Ala Thr Ala Ala Ser Val His Gly Pro Asp Ala 725 730 735 Pro Asn Ile Ser Ala Glu Glu Leu Thr Leu Asp Lys Phe Ile Asp Ala 740 745 750 Glu Thr Leu Arg Asn Ala Ser Glu Leu Asp Met Pro Thr Gly Ala Val 755 760 765 Asn Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu 770 775 780 Cys Leu Glu Trp Leu Gln Arg Leu Ala Pro Thr Asp Gly Arg Leu Ile 785 790 795 800 Cys Leu Val Arg Gly Asp Asp Asp Asp Asp Ala Arg Ala Arg Leu Glu 805 810 815 Ala Ala Tyr Gly Glu Thr Asp Gln Ala Leu Leu Asp Glu Phe Arg Asn 820 825 830 Leu Ala Arg Arg His Leu Arg Val Ile Ala Ala Asp Ile Ala Gln Pro 835 840 845 Arg Phe Gly Val Asp Asp Ala Thr Trp Glu Gln Leu Thr His Asp Val 850 855 860 Asp Lys Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Asn Gln Leu Phe Gly Pro Asn Val Phe Gly Thr Ala Glu Val Ile Arg 885 890 895 Leu Ala Leu Thr Thr Arg Leu Lys Pro Val Thr Tyr Leu Ser Thr Met 900 905 910 Ala Val Ala Met Thr Val Pro Asp Phe Glu Glu Asp Gly Asp Ile Arg 915 920 925 Ala Val Ser Ala Val Arg Thr Val Asp Asp Gly Tyr Ala Asn Gly Tyr 930 935 940 Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp 945 950 955 960 Leu Cys Gly Leu Pro Thr Ser Val Phe Arg Ser Asp Met Ile Leu Thr 965 970 975 His Arg Arg Tyr Ser Gly Gln Leu Asn Val Thr Asp Ala Phe Thr Arg 980 985 990 Met Leu Leu Ser Leu Val Leu Thr Gly Ile Ala Pro Arg Ser Phe Tyr 995 1000 1005 Gln Gly Asp Gly Asn Gly Ser Arg Pro Arg Ala His Tyr Glu Gly 1010 1015 1020 Leu Pro Val Asp Phe Val Ala Glu Ala Ile Thr Thr Leu Gly Leu 1025 1030 1035 Ala Thr Ala Glu Gly Phe Arg Ser Tyr Asn Val Met Asn Pro His 1040 1045 1050 Asp Asp Gly Ile Ser Val Asp Thr Phe Val Asp Trp Leu Ile Asp 1055 1060 1065 Asp Gly His Ala Ile Asp Ile Ile Asp Gly Tyr Glu Glu Trp Leu 1070 1075 1080 Ser Arg Phe Glu Thr Ala Leu Arg Gly Leu Pro Asp Glu Gln Arg 1085 1090 1095 Arg Ala Ser Val Leu Ala Leu Leu Asp Ala Tyr Arg Ala Pro Gly 1100 1105 1110 His Pro Arg Arg Gly Ala Ala Ile Pro Thr Asp Val Phe Arg Lys 1115 1120 1125 Ala Val Gln Asp His Glu Ile Gly Asp His Asn Asp Ile Pro Gln 1130 1135 1140 Ile Asp Arg Ala Leu Ile Gly Lys Tyr Leu Ser Asp Leu Arg Ala 1145 1150 1155 His Gly Leu Leu 1160 <210> 239 <211> 1175 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. 06-412-2C <400> 239 Met Thr His Thr Leu Ala Val Asp Ser Arg Gln Asp Arg Glu Thr Arg 1 5 10 15 Gln Arg Ser Arg Phe Gln Glu Leu His Glu Ser Asp Gln Glu Phe Arg 20 25 30 Ala Ala Glu Pro Asp Ser Ser Val Ala Asp Ala Ala Gln Glu Leu Ala 35 40 45 Pro Asn Leu Ala Arg Val Val Ala Glu Ile Met Thr Arg Tyr Ser Asp 50 55 60 Arg Pro Ala Leu Gly Ser Arg Ala Arg Gln Ile Thr Arg Val Asp Asp 65 70 75 80 Ala Asn Val Leu His Leu Leu Pro Arg Phe Asp Thr Val Thr Tyr Gly 85 90 95 Glu Val Trp Lys Ser Ala Gly Ala Leu Ala Ser Ala Leu Thr His Asp 100 105 110 Ser Val Gly Ile Ala Pro Gly Asp Phe Phe Ala Thr Leu Gly Phe Ala 115 120 125 Ser Ala Asp Tyr Val Ile Ala Glu Leu Ala Thr Ile Arg Leu Gly Ala 130 135 140 Val Ala Val Pro Leu Gln Ala Gly Thr Ser Ala Gly Gln Leu Ser Ala 145 150 155 160 Ile Ala Asp Glu Val Glu Pro Val Val Leu Ala Ala Asp Val Asp Asn 165 170 175 Leu Ser Val Ala Val Gln Val Ala Gly Gln Cys Arg Ser Ile Arg Arg 180 185 190 Ile Val Val Leu Asp Tyr Asp Ala Glu Val Asp Val His Thr Arg Ile 195 200 205 Met Lys Ser Ala Arg Asp Asp Ala Glu Gln Ala Gly Val Val Ile Arg 210 215 220 Pro Leu Thr Glu Leu Ile Arg Asp Gly Glu Gln Leu Pro Glu Ile Pro 225 230 235 240 Leu Pro Asp Ala Glu Asp Pro Asp Arg Leu Ala Thr Leu Ile Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met His Thr Glu Arg Ile 260 265 270 Val Cys Gly Ala Trp Thr Gly Ala Trp His His Thr Gly Ala Ser Ser 275 280 285 Glu Ser Val Asp Arg Pro Ala Phe Pro Val Ile Thr Leu Asp Tyr Leu 290 295 300 Pro Met Ser His Leu Ala Gly Arg Gly Leu Val Phe Ser Ala Leu Ala 305 310 315 320 Ala Gly Gly Thr Val His Phe Ala Gly Ala Ser Asp Leu Ser Thr Leu 325 330 335 Phe Glu Asp Phe Ala Leu Ala Arg Pro Thr Met Ala Leu Leu Ile Pro 340 345 350 Arg Val Cys Glu Met Ile Arg His Asn Val Leu Ala Glu Ile Asp Arg 355 360 365 Glu Val Asp Arg Ser Ser Gly Gly Asp Glu Asp Ser Val Arg Arg Asp 370 375 380 Val Leu Glu Arg His Arg Asn Asp Arg Phe Gly Gly Arg Ile Leu Ala 385 390 395 400 Ala Met Val Gly Thr Ala Pro Ile Ala Thr Glu Val Lys Asp Phe Val 405 410 415 Thr Glu Leu Leu Asp Ile Gln Val Arg Asp Asn Tyr Gly Ser Thr Glu 420 425 430 Ala Gly Met Val Leu His Asp Gly Val Ile Ala Arg Pro Pro Val Ile 435 440 445 Glu Tyr Lys Leu Asp Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp 450 455 460 Thr Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Ser Ser Ile Ile 465 470 475 480 Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Ser 485 490 495 Glu Gly Phe Tyr Arg Thr Gly Asp Val Val Ala Glu Ile Glu Pro Asp 500 505 510 Arg Leu Ala Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ala Gln 515 520 525 Gly Glu Phe Val Ala Leu Ala Arg Leu Glu Ala Val Phe Gly Thr Ser 530 535 540 Asp Leu Val Asp Gln Ile Phe Leu Tyr Gly Asn Ser Gln Arg Ala Tyr 545 550 555 560 Leu Leu Ala Val Val Val Pro Ser His Pro Asp Thr Thr Thr Ala Ser 565 570 575 Ile Ile Glu Ser Leu Gln Glu Ile Ala Arg Thr Glu Ser Leu Asn Ser 580 585 590 Tyr Glu Ile Pro Arg Asp Val Thr Ile Glu His Gln Pro Phe Thr Gln 595 600 605 Glu Asn Gly Leu Leu Ser Gly Ala Gly Lys Gln Leu Arg Pro Lys Leu 610 615 620 Val Glu Arg Tyr Gly Ala Asp Leu Glu Arg Arg Tyr Val Asp Leu Glu 625 630 635 640 Ser Gly Gln Asn Glu Arg Ile Arg Glu Leu Arg Arg His Gly Ala Asp 645 650 655 Ala Pro Val Leu Thr Thr Val Gly Asp Ala Ala Gln Ala Leu Leu Gly 660 665 670 Cys Asp Gly Ser Asp Val Arg Pro Asp Ala His Phe Ser Asp Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Thr Leu Leu Arg Asp Ile 690 695 700 Tyr Gly Val Asp Val Pro Val Gly Val Ile Thr Gly Pro Ala Met Asp 705 710 715 720 Leu Ser Ala Leu Ala Asp Tyr Ile Thr Ser Ala Arg Asp Asn Asp Ser 725 730 735 Asp Thr Ala Thr Phe Ala Ser Val His Gly Arg Asp Ala Thr Val Ala 740 745 750 His Ala Ser Asp Leu Arg Leu Ala Ala Phe Leu Asp Glu Thr Leu Leu 755 760 765 Asp Thr Ala His His Val Ala Gly Pro Arg Thr Arg Thr Glu Thr Val 770 775 780 Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu 785 790 795 800 Trp Leu Glu Arg Met Ala Glu Val Gly Gly Thr Val Val Cys Leu Val 805 810 815 Arg Gly Arg Ser Asp Ser Asp Ala Arg Ser Arg Leu Asp Ala Ala Phe 820 825 830 Asp Ser Gly Asp Glu Lys Leu Ser Ala His Tyr Arg Ala Leu Ala Asp 835 840 845 Ser Thr Leu Glu Val Val Ala Gly Asp Leu Gly Thr Pro Arg Phe Gly 850 855 860 Leu Asp Asp Asp Glu Phe Ala Ala Leu Ala Glu Arg Val Asp Arg Ile 865 870 875 880 Val His Pro Ala Ala Leu Val Asn His Ala Leu Pro Tyr Glu His Leu 885 890 895 Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Arg Leu Ala Leu 900 905 910 Thr Asp His Val Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala 915 920 925 Val Gly Val Asp Asn Phe Arg Glu Asn Gly Asp Ile Arg Ile Asp Ser 930 935 940 Pro Ser Arg Ala Val Asp Asp Ser Tyr Ala Asn Gly Tyr Gly Asn Ser 945 950 955 960 Lys Trp Ala Gly Glu Val Leu Leu Arg Asn Ala Phe Asp Glu Phe Gly 965 970 975 Leu Pro Val Ser Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Thr 980 985 990 Trp Ser Gly Gln Leu Asn Val Pro Asp Val Phe Thr Arg Leu Ile Leu 995 1000 1005 Ser Val Val Ala Thr Gly Leu Ala Pro Arg Thr Phe Tyr Ala Thr 1010 1015 1020 Gly Thr Gly Ala Pro Thr Asp Asp Ser Gly Arg Pro Leu Ala His 1025 1030 1035 Tyr Asp Gly Leu Pro Ala Asp Phe Ser Ala Glu Ala Ile Thr Ser 1040 1045 1050 Ile Ala Gly Ala Asp Val Ser Gly Tyr Arg Thr Phe Asp Ile Leu 1055 1060 1065 Asn Pro His Asp Asp Ser Ile Ser Leu Asp Thr Phe Val Asp Trp 1070 1075 1080 Ile Arg Glu Ala Gly Arg Asp Ile Glu Ile Val Ala Asn Tyr Asp 1085 1090 1095 Glu Trp Phe Glu Arg Phe Ser Ala Ala Val Glu Ala Leu Pro Glu 1100 1105 1110 Lys Gln Arg Ser His Ser Leu Leu Pro Leu Ile Gln Ser Tyr Ala 1115 1120 1125 Gln Pro Gln Gln Pro Ser Ser Gly Ala Met Leu Pro Ala Asp Glu 1130 1135 1140 Phe Ala Ala Ala Val Gly Glu Ile Pro His Leu Gly Arg Gly Leu 1145 1150 1155 Ile Glu Lys Tyr Leu Ser Asp Leu Glu Val Leu Gly Leu Val Val 1160 1165 1170 Lys Arg 1175 <210> 240 <211> 1182 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. 1482292.6 <400> 240 Met Ala Ser Asp Ala Thr Arg Gln Leu Gly Ala Pro Ala Asp Ser Asn 1 5 10 15 Glu Glu Arg Arg Ala Arg Arg Ile Arg Glu Leu Cys Ala Ser Asp Pro 20 25 30 Gln Phe Arg Ser Ala Met Pro Ile Pro Gln Val Leu Glu Ala Ala Arg 35 40 45 Gln Pro Gly Leu Arg Leu Pro Gln Val Ile Glu Thr Leu Val Glu Gly 50 55 60 Tyr Ala Gly Arg Pro Met Phe Gly Gln Arg Ala Arg Gln Gln Val Thr 65 70 75 80 Asp Pro Gln Thr Gly Arg Thr Ser Ser Arg Leu Leu Pro Ser Phe Thr 85 90 95 Thr Leu Thr Tyr Gly Glu Leu Trp Ala Arg Ala Arg Ala Ile Ala Thr 100 105 110 Ala Trp Cys Arg Asn Thr His Tyr Arg Leu Ser Pro Gly Asp Phe Val 115 120 125 Ala Thr Val Gly Phe Ala Ser Ser Asp Tyr Val Ala Ile Asp Val Ala 130 135 140 Cys Ala Tyr Ala Gly Trp Val Ser Val Pro Leu Gln His Asn Ala Ser 145 150 155 160 Val Ala Gln Leu Arg Ser Ile Leu Ser Glu Ala Lys Pro Arg Val Leu 165 170 175 Ala Val Ser Ala Glu Tyr Leu Asp Thr Ala Val Gln Ala Ala Leu Gly 180 185 190 Gly Glu Trp Leu Arg His Leu Val Val Phe Asp Tyr Leu Pro Val Val 195 200 205 Asp Asp His Gln Glu Ser Tyr Glu Arg Ala Leu Ala Leu Leu His Ala 210 215 220 Ala Val Met Pro Val Gln Val Gln Thr Leu Asn Glu Val Ile Ser Gln 225 230 235 240 Gly Ser Ala Leu Pro Ala Glu Pro Ala Tyr Leu Gly Ala Asp Glu Ala 245 250 255 Arg Leu Ala Met Ile Leu Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 260 265 270 Gly Ala Met Tyr Thr Glu Ala Met Thr Ser Arg Leu Trp Thr Met Ser 275 280 285 Phe Pro Ala Glu Pro Asp Ala Ala Val Phe Ser Val Asn Phe Leu Pro 290 295 300 Leu His His Leu Gly Gly Arg Ile Ala Leu Leu Ala Cys Ile Arg Ala 305 310 315 320 Gly Gly Thr Thr Tyr Phe Ala Ala Gly Pro Glu Leu Ser Thr Leu Phe 325 330 335 Glu Asp Trp Ala Leu Val Arg Pro Thr Glu Leu Tyr Val Val Pro Arg 340 345 350 Val Ile Glu Met Leu Ile Gln Arg Phe Arg Thr Gly Val Asp Arg Leu 355 360 365 Arg Leu Glu Gly Ala Asp Asp Glu Thr Ala Gln Ala Gln Ala Ala Asp 370 375 380 Glu Leu Arg Gln Gln Leu Leu Gly Gly Arg Val Leu Gly Gly Phe Ile 385 390 395 400 Gly Thr Ala Pro Leu Ala Thr Glu Met Arg Thr Phe Ile Glu Ser Arg 405 410 415 Leu Gln Val His Leu Val Asp Gly Tyr Gly Leu Thr Glu Val Gly Gly 420 425 430 Ile Thr Lys Asp Gly Val Val Leu Arg Pro Pro Val Val Lys Tyr Lys 435 440 445 Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Lys Pro Tyr 450 455 460 Pro Arg Gly Glu Leu Leu Val Lys Ser Thr Thr Ser Thr Pro Gly Tyr 465 470 475 480 Tyr Asn His Pro Glu Ile Thr Ala Ala Val Phe Asp Glu Asp Gly Phe 485 490 495 Tyr Arg Thr Gly Asp Val Met Ala Glu Val Gly Pro Asp His Leu Val 500 505 510 Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe 515 520 525 Val Ala Val Ala Asn Leu Glu Ala Leu Tyr Ala Thr Ala Pro Leu Ile 530 535 540 Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ser Ser Leu Leu Ala 545 550 555 560 Val Ile Val Pro Thr Val Glu Ala Leu Ala His Phe Asp Gly Asp Leu 565 570 575 Thr Ala Leu Lys Ser Ala Leu Arg Asp Ser Leu Arg Glu Thr Ala Lys 580 585 590 Ala Ser Gln Leu Gln Pro Tyr Glu Ile Pro Val Asp Tyr Leu Ile Glu 595 600 605 Thr Glu Pro Phe Thr Thr Ala Asn Gly Leu Leu Ser Gly Val Gly Lys 610 615 620 Leu Leu Arg Pro Asn Leu Asn Asp Arg Tyr Gly Glu Arg Leu Glu Leu 625 630 635 640 Leu Tyr Ile Glu Leu Ala Ala Leu Gln Gln Asp Lys Leu Gly Ala Leu 645 650 655 His Arg Leu Ala Asp Asp Leu Pro Val Ile Glu Ile Val Ile Arg Ala 660 665 670 Val Gly Leu Leu Leu Gly Thr Asp Pro Val Asp Arg Asn Asp His Phe 675 680 685 Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Thr Leu 690 695 700 Leu Gln Glu Ile Phe Gly Val Glu Val Pro Val Gly Val Leu Ile Gly 705 710 715 720 Pro Ala Asn Ser Leu Gln Glu Leu Ala Asn Phe Ile Glu Thr Gln Arg 725 730 735 Gln Ser Ser Ser Glu Arg Ala Ser Phe Thr Arg Val His Gly Arg Ala 740 745 750 Ala Glu Tyr Leu His Ala Ser Asp Leu Thr Leu Asp Lys Phe Ile Asp 755 760 765 Thr Lys Thr Leu Asp Arg Ala Ala Ala Leu Ser Ile Pro Ala Val Gly 770 775 780 Glu Pro Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Tyr Leu Gly Arg 785 790 795 800 Phe Leu Cys Leu Glu Trp Leu Gln Arg Leu Ala Cys Ser Gly Gly Lys 805 810 815 Leu Val Cys Leu Leu Arg Ala Gly Ser Thr Asn Thr Ala Gln Val Arg 820 825 830 Leu Asn Ala Val Phe Asp Thr Gly Asp Pro Val Leu Leu Arg Arg Phe 835 840 845 His Glu Leu Ala Ala Asp His Leu Asp Val Val Val Gly Asp Met Ser 850 855 860 Glu Pro Asp Leu Gly Leu Asp Glu Ala Thr Trp Asp Arg Leu Ala Gln 865 870 875 880 Thr Val Asp Met Ile Val His Pro Gly Ala Leu Val Asn His Val Leu 885 890 895 Pro Tyr Glu Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Ala Leu 900 905 910 Ile Arg Leu Ala Ile Thr Gln Arg Met Lys Pro Val Asn Tyr Val Ser 915 920 925 Thr Val Ala Val Ser Met Ser Val Pro Asp Gly Glu Phe Ile Glu Asp 930 935 940 Gly Asp Ile Arg Val Val Ser Pro Val Arg Pro Asn Asn Gly Ser Tyr 945 950 955 960 Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 965 970 975 Asn Ala His Asp Arg Tyr Ser Leu Pro Val Asn Val Phe Arg Pro Asp 980 985 990 Met Ile Leu Ala His Ser Glu Tyr Leu Gly Gln Val Asn Val Val Asp 995 1000 1005 Ala Phe Thr Arg Leu Val Phe Ser Leu Leu Val Thr Gly Ile Ala 1010 1015 1020 Pro Gln Ser Phe Tyr Gln Lys Arg Asn Gly Glu Phe Arg Pro Arg 1025 1030 1035 Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Val Ala Glu Ser Ile 1040 1045 1050 Cys Lys Leu Ser Gly Gln Leu Arg Asp Gly Phe His Ser Phe Asp 1055 1060 1065 Val Leu Asn Pro Tyr Asp Asp Gly Ile Ser Leu Asp Val Phe Val 1070 1075 1080 Asp Trp Leu Ile Ala Ser Gly His Ser Ile Thr Arg Ile Pro Asp 1085 1090 1095 Tyr His Glu Trp Leu Thr Arg Phe Arg Thr Ala Met Thr Ala Leu 1100 1105 1110 Pro Glu Arg Gln Arg Gln Tyr Ser Val Leu Ala Leu Leu Glu Ala 1115 1120 1125 Tyr His Gln Pro Gln Ala Pro Leu Arg Gly Ala Pro Val Pro Thr 1130 1135 1140 Glu Val Phe His Ala Ala Val Arg Ala Thr Lys Val Gly Pro Asp 1145 1150 1155 Lys Asp Ile Pro His Ile Gly Arg Pro Leu Ile Asp Lys Tyr Ile 1160 1165 1170 Thr Asp Leu Arg His Leu Gly Leu Leu 1175 1180 <210> 241 <211> 1181 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus sp. PBTS 2 <400> 241 Met Thr Arg Thr Ile Ala Met Lys Ser Thr Val Ala Val Asp Ser Glu 1 5 10 15 His Asp Arg Asp Ile Arg Gln Arg Asp Arg Phe Gln His Leu His Asp 20 25 30 Ser Asp Pro Glu Phe Arg Ala Ala Glu Pro Asp Arg Ser Val Ala Asp 35 40 45 Ala Ala Arg Glu Leu Ala Pro Asn Leu Ala Arg Val Val Ala Glu Ile 50 55 60 Met Thr Arg Tyr Ala Asp Arg Pro Ala Leu Gly Arg Arg Ala Arg Thr 65 70 75 80 Ile Glu Asp Thr Asp Gly Ser Thr Thr Ala Arg Leu Leu Pro Arg Phe 85 90 95 Asp Thr Val Thr Tyr Gly Gln Ala Trp Ala Asp Ala Gly Ala Leu Ala 100 105 110 Ser Ala Leu Gly His Asp Asp Gly Gly Ile Ala Ala Gly Asp Phe Val 115 120 125 Ala Thr Leu Gly Phe Ala Gly Ile Asp Tyr Val Ile Thr Glu Leu Ala 130 135 140 Thr Ile Arg Val Gly Ala Val Ala Val Pro Leu Gln Ala Gly Ala Thr 145 150 155 160 Ala Gly Gln Leu Arg Ala Ile Val Asp Glu Val Glu Pro Val Val Leu 165 170 175 Ala Ser Asp Val Asp Asn Leu Ala Val Ala Met Glu Val Ala Gly His 180 185 190 Cys Arg Ser Ile Arg Thr Val Val Val Leu Asp Tyr Asp Asp Arg Ile 195 200 205 Asp Ala Asp Thr Arg Ala Leu Thr Ser Ala Arg Glu Gly Val His Gly 210 215 220 Ser Gly Ile Ala Val Arg Pro Leu Thr Glu Leu Val Asp Glu Gly Ser 225 230 235 240 Arg Leu Pro Gln Val Pro Leu Phe Asp Val Glu Asp Pro Glu Arg Leu 245 250 255 Ala Ala Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 260 265 270 Met His Thr Glu Gln Ile Val Ser Gly Ala Trp Thr Gly Ala Trp His 275 280 285 Arg Thr Gly Ala Ser Ser Glu Gly Val Asp Glu Pro Ala Phe Pro Val 290 295 300 Ile Thr Leu Asp Tyr Leu Pro Met Ser His Leu Ala Gly Arg Gly Leu 305 310 315 320 Val Phe Ser Thr Leu Ala Ala Gly Gly Thr Val His Phe Ala Gly Ser 325 330 335 Ser Asp Leu Ser Thr Leu Phe Glu Asp Phe Ala Leu Ala Arg Pro Thr 340 345 350 Leu Ala Leu Leu Ile Pro Arg Val Cys Glu Met Ile Arg His Thr Val 355 360 365 Leu Ala Glu Ile Asp Arg Ala Val Asp Gly Thr Asp Ala Gly Glu His 370 375 380 Glu Gln Ile Ser Arg Gly Val Leu Glu Arg Val Arg Ser Glu Gln Phe 385 390 395 400 Gly Gly Arg Ile Leu Ala Ala Met Val Gly Thr Ala Pro Ile Ala Ala 405 410 415 Glu Val Lys Asp Phe Val Thr Asp Leu Leu Asp Val Arg Val Arg Asp 420 425 430 Asn Tyr Gly Ser Thr Glu Ala Gly Met Val Leu Leu Asp Gly Ile Val 435 440 445 Ala Arg Pro Pro Val Leu Glu Tyr Lys Leu Asp Asp Val Pro Glu Leu 450 455 460 Gly Tyr Phe Ser Thr Asp Thr Pro His Pro Arg Gly Glu Leu Leu Leu 465 470 475 480 Lys Thr Thr Ser Ile Ile Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr 485 490 495 Ala Asp Val Phe Asp Ser Asp Gly Phe Tyr Arg Thr Gly Asp Val Val 500 505 510 Ala Glu Leu Glu Pro Asp Arg Leu Ala Tyr Val Asp Arg Arg Lys Asn 515 520 525 Val Leu Lys Leu Ala Gln Gly Glu Phe Val Ala Leu Ala Arg Leu Glu 530 535 540 Ala Val Phe Gly Thr Ser Glu Leu Val Asp Gln Ile Phe Leu Tyr Gly 545 550 555 560 Asn Ser Gln Arg Ser Tyr Leu Leu Ala Ile Val Val Pro Ala His Ala 565 570 575 Asn Ser Thr Ala Gly Ala Ile Met Glu Ser Leu Gln Arg Ile Ala Arg 580 585 590 Thr Glu Ser Leu Asn Ser Tyr Glu Ile Pro Arg Glu Val Val Leu Glu 595 600 605 Arg Glu Pro Phe Thr Gln Asp Asn Gly Leu Leu Ser Gly Ala Gly Lys 610 615 620 Gln Leu Arg Pro Lys Leu Val Glu Arg Tyr Gly Asp Glu Leu Glu Arg 625 630 635 640 Arg Tyr Ala Glu Leu Glu Ser Gly Gln Thr Asp Arg Leu Arg Glu Leu 645 650 655 Arg Arg Ser Gly Ala Gln Ala Pro Val Leu Ala Thr Val Gly Asp Ala 660 665 670 Ala Gln Ala Leu Leu Gly Cys Ser Gly Ala Asp Ile Arg Pro Asp Ala 675 680 685 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser 690 695 700 Thr Leu Leu Arg Asp Ile Tyr Asp Val Asp Val Pro Val Gly Val Ile 705 710 715 720 Thr Gly Pro Ala Met Asp Leu Ala Ala Leu Ala Asp Tyr Ile Thr Ser 725 730 735 Ala Ile Asp Asn Asp Ser Asp Thr Ala Thr Phe Ala Ser Val His Gly 740 745 750 Arg Asp Ala Ser Val Ala Leu Ala Ser Asp Leu Thr Leu Ser Ala Phe 755 760 765 Leu Asp Ala Ser Leu Leu Asp Ala Ala His Arg Ile Pro Gly Pro Arg 770 775 780 Pro Val Thr Asn Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly 785 790 795 800 Arg Phe Leu Cys Leu Glu Trp Leu Glu Lys Met Ala Ala Ala Gly Gly 805 810 815 Arg Val Ile Cys Leu Val Arg Gly Arg Ser Asp Ala Asp Ala Arg Gly 820 825 830 Arg Leu Asp Ala Ala Phe Asp Ser Gly Asp Ala Thr Leu Ser Asp Arg 835 840 845 Tyr Arg Ala Leu Ala Asp Ala Ala Leu Asp Val Ile Ala Gly Asp Leu 850 855 860 Gly Thr Pro Arg Phe Gly Leu Thr Asp Asp Val Trp Glu Glu Leu Ser 865 870 875 880 Arg Arg Val Asp Arg Val Val His Pro Ala Ala Leu Val Asn His Ala 885 890 895 Leu Pro Tyr Glu His Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu 900 905 910 Val Ile Arg Leu Ala Leu Thr Asp His Ile Lys Pro Val Thr Tyr Leu 915 920 925 Ser Thr Val Ala Val Ala Val Gly Val Asp Asp Phe His Glu Asn Gly 930 935 940 Asp Ile Arg Val Asp Ser Ala Gln Arg Ala Val Asp Glu Thr Tyr Ala 945 950 955 960 Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Asn 965 970 975 Ala Phe Asp Glu Tyr Ser Leu Pro Val Ser Val Phe Arg Ser Asp Met 980 985 990 Ile Leu Ala His Ser Thr Trp Ser Gly Gln Leu Asn Val Pro Asp Val 995 1000 1005 Phe Thr Arg Leu Ile Leu Ser Val Val Ala Thr Gly Leu Ala Pro 1010 1015 1020 Arg Ser Phe Tyr Ala Thr Asp Thr Gly Ala Pro Thr Asp Glu Gln 1025 1030 1035 Gly Arg Pro Leu Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Ser 1040 1045 1050 Ala Ala Ala Ile Thr Ser Ile Ala Gly Asp Asp Val Ala Gly Tyr 1055 1060 1065 Arg Thr Phe Asp Ile Leu Asn Pro His Asp Asp Asp Ile Ser Leu 1070 1075 1080 Asp Thr Phe Val Asp Trp Leu Arg Glu Ala Gly Cys Thr Ile Asp 1085 1090 1095 Ile Val Asp Asp Tyr Asp Glu Trp Phe Glu Arg Phe Ser Ala Ala 1100 1105 1110 Val Gln Glu Leu Pro Glu Lys Gln Arg Ser His Ser Leu Leu Pro 1115 1120 1125 Leu Ile His Ser Tyr Ala His Pro Gln His Pro Ser Ser Gly Ala 1130 1135 1140 Ile Leu Pro Ala Glu Glu Phe Ala Ser Ala Val Gly Asp Ile Pro 1145 1150 1155 His Leu Gly Arg Glu Leu Ile Glu Lys Tyr Leu Ala Asp Leu Val 1160 1165 1170 Ala Leu Gly Leu Val Ala Lys Ser 1175 1180 <210> 242 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium smegmatis <400> 242 Met Thr Ser Asp Val His Asp Ala Thr Asp Gly Val Thr Glu Thr Ala 1 5 10 15 Leu Asp Asp Glu Gln Ser Thr Arg Arg Ile Ala Glu Leu Tyr Ala Thr 20 25 30 Asp Pro Glu Phe Ala Ala Ala Ala Pro Leu Pro Ala Val Val Asp Ala 35 40 45 Ala His Lys Pro Gly Leu Arg Leu Ala Glu Ile Leu Gln Thr Leu Phe 50 55 60 Thr Gly Tyr Gly Asp Arg Pro Ala Leu Gly Tyr Arg Ala Arg Glu Leu 65 70 75 80 Ala Thr Asp Glu Gly Gly Arg Thr Val Thr Arg Leu Leu Pro Arg Phe 85 90 95 Asp Thr Leu Thr Tyr Ala Gln Val Trp Ser Arg Val Gln Ala Val Ala 100 105 110 Ala Ala Leu Arg His Asn Phe Ala Gln Pro Ile Tyr Pro Gly Asp Ala 115 120 125 Val Ala Thr Ile Gly Phe Ala Ser Pro Asp Tyr Leu Thr Leu Asp Leu 130 135 140 Val Cys Ala Tyr Leu Gly Leu Val Ser Val Pro Leu Gln His Asn Ala 145 150 155 160 Pro Val Ser Arg Leu Ala Pro Ile Leu Ala Glu Val Glu Pro Arg Ile 165 170 175 Leu Thr Val Ser Ala Glu Tyr Leu Asp Leu Ala Val Glu Ser Val Arg 180 185 190 Asp Val Asn Ser Val Ser Gln Leu Val Val Phe Asp His His Pro Glu 195 200 205 Val Asp Asp His Arg Asp Ala Leu Ala Arg Ala Arg Glu Gln Leu Ala 210 215 220 Gly Lys Gly Ile Ala Val Thr Thr Leu Asp Ala Ile Ala Asp Glu Gly 225 230 235 240 Ala Gly Leu Pro Ala Glu Pro Ile Tyr Thr Ala Asp His Asp Gln Arg 245 250 255 Leu Ala Met Ile Leu Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly 260 265 270 Ala Met Tyr Thr Glu Ala Met Leu Ala Arg Leu Trp Thr Met Ser Phe 275 280 285 Ile Thr Gly Asp Pro Thr Pro Val Ile Asn Val Asn Phe Met Pro Leu 290 295 300 Asn His Leu Gly Gly Arg Ile Pro Ile Ser Thr Ala Val Gln Asn Gly 305 310 315 320 Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp Met Ser Thr Leu Phe Glu 325 330 335 Asp Leu Ala Leu Val Arg Pro Thr Glu Leu Gly Leu Val Pro Arg Val 340 345 350 Ala Asp Met Leu Tyr Gln His His Leu Ala Thr Val Asp Arg Leu Val 355 360 365 Thr Gln Gly Ala Asp Glu Leu Thr Ala Glu Lys Gln Ala Gly Ala Glu 370 375 380 Leu Arg Glu Gln Val Leu Gly Gly Arg Val Ile Thr Gly Phe Val Ser 385 390 395 400 Thr Ala Pro Leu Ala Ala Glu Met Arg Ala Phe Leu Asp Ile Thr Leu 405 410 415 Gly Ala His Ile Val Asp Gly Tyr Gly Leu Thr Glu Thr Gly Ala Val 420 425 430 Thr Arg Asp Gly Val Ile Val Arg Pro Pro Val Ile Asp Tyr Lys Leu 435 440 445 Ile Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Lys Pro Tyr Pro 450 455 460 Arg Gly Glu Leu Leu Val Arg Ser Gln Thr Leu Thr Pro Gly Tyr Tyr 465 470 475 480 Lys Arg Pro Glu Val Thr Ala Ser Val Phe Asp Arg Asp Gly Tyr Tyr 485 490 495 His Thr Gly Asp Val Met Ala Glu Thr Ala Pro Asp His Leu Val Tyr 500 505 510 Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly Glu Phe Val 515 520 525 Ala Val Ala Asn Leu Glu Ala Val Phe Ser Gly Ala Ala Leu Val Arg 530 535 540 Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Ser Phe Leu Leu Ala Val 545 550 555 560 Val Val Pro Thr Pro Glu Ala Leu Glu Gln Tyr Asp Pro Ala Ala Leu 565 570 575 Lys Ala Ala Leu Ala Asp Ser Leu Gln Arg Thr Ala Arg Asp Ala Glu 580 585 590 Leu Gln Ser Tyr Glu Val Pro Ala Asp Phe Ile Val Glu Thr Glu Pro 595 600 605 Phe Ser Ala Ala Asn Gly Leu Leu Ser Gly Val Gly Lys Leu Leu Arg 610 615 620 Pro Asn Leu Lys Asp Arg Tyr Gly Gln Arg Leu Glu Gln Met Tyr Ala 625 630 635 640 Asp Ile Ala Ala Thr Gln Ala Asn Gln Leu Arg Glu Leu Arg Arg Ala 645 650 655 Ala Ala Thr Gln Pro Val Ile Asp Thr Leu Thr Gln Ala Ala Ala Thr 660 665 670 Ile Leu Gly Thr Gly Ser Glu Val Ala Ser Asp Ala His Phe Thr Asp 675 680 685 Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Leu Ser Asn Leu Leu Ser 690 695 700 Asp Phe Phe Gly Phe Glu Val Pro Val Gly Thr Ile Val Asn Pro Ala 705 710 715 720 Thr Asn Leu Ala Gln Leu Ala Gln His Ile Glu Ala Gln Arg Thr Ala 725 730 735 Gly Asp Arg Arg Pro Ser Phe Thr Thr Val His Gly Ala Asp Ala Thr 740 745 750 Glu Ile Arg Ala Ser Glu Leu Thr Leu Asp Lys Phe Ile Asp Ala Glu 755 760 765 Thr Leu Gln Ala Ala Pro Gly Leu Pro Lys Val Thr Thr Glu Pro Arg 770 775 780 Thr Val Leu Leu Ser Gly Ala Asn Gly Trp Leu Gly Arg Phe Leu Thr 785 790 795 800 Leu Gln Trp Leu Glu Arg Leu Ala Pro Val Gly Gly Thr Leu Ile Thr 805 810 815 Ile Val Arg Gly Arg Asp Asp Ala Ala Ala Arg Ala Arg Leu Thr Gln 820 825 830 Ala Tyr Asp Thr Asp Pro Glu Leu Ser Arg Arg Phe Ala Glu Leu Ala 835 840 845 Asp Arg His Leu Arg Val Val Ala Gly Asp Ile Gly Asp Pro Asn Leu 850 855 860 Gly Leu Thr Pro Glu Ile Trp His Arg Leu Ala Ala Glu Val Asp Leu 865 870 875 880 Val Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Arg Gln 885 890 895 Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Lys Leu Ala 900 905 910 Leu Thr Glu Arg Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ser Val 915 920 925 Ala Met Gly Ile Pro Asp Phe Glu Glu Asp Gly Asp Ile Arg Thr Val 930 935 940 Ser Pro Val Arg Pro Leu Asp Gly Gly Tyr Ala Asn Gly Tyr Gly Asn 945 950 955 960 Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys 965 970 975 Gly Leu Pro Val Ala Thr Phe Arg Ser Asp Met Ile Leu Ala His Pro 980 985 990 Arg Tyr Arg Gly Gln Val Asn Val Pro Asp Met Phe Thr Arg Leu Leu 995 1000 1005 Leu Ser Leu Leu Ile Thr Gly Val Ala Pro Arg Ser Phe Tyr Ile 1010 1015 1020 Gly Asp Gly Glu Arg Pro Arg Ala His Tyr Pro Gly Leu Thr Val 1025 1030 1035 Asp Phe Val Ala Glu Ala Val Thr Thr Leu Gly Ala Gln Gln Arg 1040 1045 1050 Glu Gly Tyr Val Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly 1055 1060 1065 Ile Ser Leu Asp Val Phe Val Asp Trp Leu Ile Arg Ala Gly His 1070 1075 1080 Pro Ile Asp Arg Val Asp Asp Tyr Asp Asp Trp Val Arg Arg Phe 1085 1090 1095 Glu Thr Ala Leu Thr Ala Leu Pro Glu Lys Arg Arg Ala Gln Thr 1100 1105 1110 Val Leu Pro Leu Leu His Ala Phe Arg Ala Pro Gln Ala Pro Leu 1115 1120 1125 Arg Gly Ala Pro Glu Pro Thr Glu Val Phe His Ala Ala Val Arg 1130 1135 1140 Thr Ala Lys Val Gly Pro Gly Asp Ile Pro His Leu Asp Glu Ala 1145 1150 1155 Leu Ile Asp Lys Tyr Ile Arg Asp Leu Arg Glu Phe Gly Leu Ile 1160 1165 1170 <210> 243 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides sp. H092 <400> 243 Met Thr Ala His Thr Gln Ala Asn Tyr Asp Thr Asp Ala Ala Ala Leu 1 5 10 15 Ala Thr Lys Leu Phe Glu Ser Asp Pro Gln Phe Arg Ala Ala Arg Pro 20 25 30 Asp Pro Glu Val Met Asp Ser Leu Leu Val Pro Gly Leu Arg Leu Ser 35 40 45 Gln Val Leu His Ala Leu Leu Thr Gly Tyr Ala Glu Arg Pro Val Met 50 55 60 Gly Phe Arg Ser Arg Glu Ser Val Ala Asp Pro Ala Thr Gly Arg Thr 65 70 75 80 Val Asp Arg Leu Leu Pro Ala Phe Glu Thr Val Thr Tyr Gly Gln Leu 85 90 95 Leu Asp Asn Ile Ser Ala Ile Leu Ala Glu Trp Gln His Gly Glu Asn 100 105 110 Arg Ile Gly Ala Asp Asp Phe Val Ala Thr Ile Gly Phe Ser Ser Pro 115 120 125 Asp Tyr Val Thr Leu Asp Leu Ala Thr Leu Met Asn Gly Ser Val Ser 130 135 140 Ile Pro Leu Gln His Asn Ala Ser Val Thr Gln Leu Arg Met Met Leu 145 150 155 160 Glu Glu Thr Asn Pro Arg Leu Val Ala Ala Ser Ala Asp Cys Leu Asp 165 170 175 Leu Ala Val Glu Ala Ala Leu Gly Leu Thr Asp Leu Gln Arg Val Val 180 185 190 Val Phe Asp Tyr Arg Pro Asp Thr Asp Asp His Arg Glu Lys Leu Ala 195 200 205 Ala Ala Arg Glu Arg Leu Gln Ala Ala Gly Met Arg Val Val Val Glu 210 215 220 Pro Leu Ala Glu Val Ile Ala Asn Gly Arg Arg Leu Pro Glu Pro Val 225 230 235 240 Leu Tyr Thr Ala Gly Asp Asp Gln Arg Thr Ala Leu Ile Met Tyr Thr 245 250 255 Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Phe Thr Glu Trp Thr 260 265 270 Val Thr Arg Phe Trp Ser Ser Gly Ala Ala Pro Asn Arg Asp Thr Pro 275 280 285 Ile Ile Asn Val Asn Phe Leu Pro Leu Asn His Leu Ala Gly Arg Val 290 295 300 Gly Leu Leu Thr Ala Phe Ile Pro Gly Gly Thr Cys Tyr Phe Val Pro 305 310 315 320 Glu Ser Asp Leu Ser Thr Leu Phe Glu Asp Trp Gln Leu Ala Arg Pro 325 330 335 Thr His Met Gly Val Val Pro Arg Val Val Asp Met Leu Phe Gln His 340 345 350 Tyr Gln Thr Arg Val Asp Ala Leu Ile Ala Glu Gly Ala Glu Ala Lys 355 360 365 Ser Ala Asp Arg Thr Ala Lys Ala Glu Leu Arg Glu Asp Val Leu Gly 370 375 380 Gly Arg Val Val Ala Gly Met Leu Ala Thr Ala Pro Leu Ser Pro Glu 385 390 395 400 Met Lys Thr Phe Leu Glu Ser Ser Leu Asn Phe His Leu Leu Asp Leu 405 410 415 Tyr Gly Leu Thr Glu Val Gly Gly Val Phe Arg Asp Gly Lys Ile Ser 420 425 430 Arg Pro Pro Val Leu Asp Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly 435 440 445 Tyr Tyr Thr Thr Asp Lys Pro His Pro Arg Gly Glu Leu Leu Val Lys 450 455 460 Ser Ala Thr Ala Thr Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala 465 470 475 480 Glu Val Phe Asp Ala Asp Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala 485 490 495 Glu Ile Ala Pro Asp Glu Leu Val Tyr Val Asp Arg Arg Asn Asn Val 500 505 510 Ile Lys Leu Ala Gln Gly Glu Phe Val Ala Val Ala Asn Leu Glu Thr 515 520 525 Val Tyr Val Gly Ala Pro Leu Val Arg Gln Ile Phe Val Tyr Gly Asn 530 535 540 Ser Glu Arg Ala Tyr Leu Leu Ala Val Ile Val Pro Thr Glu Glu Ala 545 550 555 560 Leu Arg Ala His Pro Asp Pro Val Asp Leu Lys Asn Ser Ile Arg Glu 565 570 575 Ser Leu Gln Arg Thr Ala Arg Val Ser His Leu His Ser Tyr Glu Leu 580 585 590 Pro Ala Asp Phe Ile Ile Glu Thr Thr Pro Phe Ser Ile Glu Ser Gly 595 600 605 Met Leu Ala Ala Val Gly Lys Pro Ile Arg Pro Lys Met Ile Glu His 610 615 620 Tyr Gly Asp Arg Leu Glu Gln Leu Tyr Ala Asp Leu Ala Glu Ala Arg 625 630 635 640 Val Gln Glu Leu Arg Gln Leu Arg Asp Thr Ala Arg Gln Arg Pro Val 645 650 655 Ile Glu Thr Val Thr Glu Ala Ala Gln Ala Leu Leu Gly Met Ser Ser 660 665 670 Asp Ala Val Arg Pro Asp His His Phe Ile Asp Leu Gly Gly Asp Ser 675 680 685 Leu Ser Ala Leu Thr Phe Ser Asn Leu Leu Arg Asp Leu Phe Asp Val 690 695 700 Glu Val Pro Val Gly Val Ile Thr Gly Pro Ala Ala Asp Leu Arg Lys 705 710 715 720 Leu Ala Ala Tyr Val Glu Gly Ala Arg Glu Ser Gly Ala Ala Thr Ala 725 730 735 Ala Ser Val His Gly Ser Asp Val Thr Val Ile Asn Ala Asn Glu Leu 740 745 750 Thr Leu Asp Lys Phe Val Asp Ala Glu Thr Leu Ser Ser Ala Ala Glu 755 760 765 Leu Glu Arg Phe Ser Gly Ala Val Gly Thr Val Leu Leu Thr Gly Ala 770 775 780 Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Gln Arg Leu 785 790 795 800 Ala Gln Ser Gly Gly Gln Leu Ile Cys Leu Val Arg Gly Asp Asp Asp 805 810 815 Asp Asp Ala Leu Ala Arg Leu Glu Ala Ala Tyr Gly His Thr Asp Gln 820 825 830 Ala Leu Leu Asp Glu Phe Arg Ala Leu Ala Arg Arg His Leu Arg Val 835 840 845 Ile Ala Ala Asp Ile Thr Gln Pro Arg Leu Gly Ile Asp Asp Ala Thr 850 855 860 Trp Glu Gln Leu Ala Arg Glu Val Asp Lys Ile Val His Pro Ala Ala 865 870 875 880 Leu Val Asn His Val Leu Pro Tyr Asn Gln Leu Phe Gly Pro Asn Val 885 890 895 Leu Gly Thr Ala Glu Val Ile Arg Leu Ala Leu Thr Thr Arg Ile Lys 900 905 910 Pro Val Thr Tyr Leu Ser Thr Met Ala Val Ala Met Ala Val Pro Asp 915 920 925 Phe Asp Glu Asp Gly Asp Ile Arg Thr Val Ser Pro Ile Arg His Ile 930 935 940 Gly Pro Gly Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Gly Glu 945 950 955 960 Val Leu Leu Arg Glu Ala Tyr Asp Leu Cys Gly Leu Pro Val Ser Val 965 970 975 Phe Arg Ser Asp Met Ile Leu Thr His Arg Gln Tyr Ser Gly Gln Leu 980 985 990 Asn Val Thr Asp Ala Phe Thr Arg Met Leu Leu Ser Leu Val Leu Thr 995 1000 1005 Gly Ile Ala Pro Arg Ser Phe Tyr Gln Gly Asp Gly Asp Gly Ser 1010 1015 1020 Arg Pro Arg Ala His Tyr Glu Gly Leu Pro Val Asp Phe Val Thr 1025 1030 1035 Glu Ala Ile Thr Thr Leu Gly Leu Ala Asn Ser Glu Gly Phe Arg 1040 1045 1050 Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly Ile Ser Val Asp 1055 1060 1065 Thr Phe Val Asp Trp Leu Val Glu Asp Gly His Thr Ile Asp Ile 1070 1075 1080 Ile Asp Asp Tyr Asp Glu Trp Leu Ser Arg Phe Glu Thr Ala Leu 1085 1090 1095 Arg Gly Leu Pro Asp Asp Gln Arg Arg Ser Ser Val Leu Pro Leu 1100 1105 1110 Leu Asp Ala Tyr Arg Ala Pro Gly His Pro Arg Arg Gly Ala Asp 1115 1120 1125 Thr Pro Thr Asp Gln Phe Arg Lys Ala Val Gln Asn Tyr Lys Ile 1130 1135 1140 Gly Ser Asp Asp Asp Ser Ala Asp Ile Pro His Ile Asp His Ala 1145 1150 1155 Leu Ile Thr Lys Tyr Ile Ser Asp Leu Arg Ala His Gly Leu Leu 1160 1165 1170 <210> 244 <211> 1164 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium colombiense <400> 244 Met Asp Ala His Asp Glu Glu Phe Arg Thr Thr Lys Pro Asp Ser Ala 1 5 10 15 Leu Gln Leu Ala Ala Arg Glu Pro Gly Leu Arg Leu Pro Gln Ile Leu 20 25 30 Glu Ile Phe Ala Glu Gly Tyr Ala Asp Arg Pro Ala Leu Gly Trp Arg 35 40 45 Ala Arg Ser Leu Thr Thr Asp Gln Ala Thr Gly Arg Thr Ser Ala Gln 50 55 60 Leu Leu Pro Arg Phe Asp Thr Leu Thr Tyr Arg Glu Leu Trp Ala Asn 65 70 75 80 Val Arg Ala Ile Ala Gly Ala Trp Arg His Asp Ala Thr Asn Pro Val 85 90 95 Ala Pro Gly Asp Val Val Ala Thr Val Gly Phe Ala Ser Ala Glu Tyr 100 105 110 Leu Thr Ile Asp Leu Val Cys Ala Tyr Leu Gly Leu Val Ala Val Pro 115 120 125 Leu Gln His Asn Thr Thr Ala Ser Arg Leu Arg Pro Ile Val Glu Glu 130 135 140 Val Glu Pro Ser Thr Leu Ala Ala Gly Val Gly Tyr Leu Asp Leu Ala 145 150 155 160 Val Gln Ala Ala Leu Gly Ser Ser Ser Leu Arg Arg Val Val Val Phe 165 170 175 Asp Tyr Arg Pro Glu Val Asp Glu Gln Arg Glu Ala Val Gln Arg Ala 180 185 190 Gln Ala Lys Leu Ala Gly Ala Gly Ala Ala Val Thr Ile Glu Thr Leu 195 200 205 Asp Asp Val Ile Glu Arg Gly Arg Thr Leu Pro Pro Glu Pro Met Phe 210 215 220 Thr Gly Asp Thr Asp Glu Arg Leu Ala Met Ile Met Tyr Thr Ser Gly 225 230 235 240 Ser Thr Gly Leu Pro Lys Gly Ala Met Tyr Thr Glu Arg Met Leu Cys 245 250 255 Arg Leu Trp Thr Asn Glu Leu Met Pro Asp Phe Thr Asp Thr Pro Val 260 265 270 Ile Asn Val Asn Phe Met Pro Leu Asn His Leu Gly Gly Arg Ile Pro 275 280 285 Leu Ser Thr Ala Phe Gln Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu 290 295 300 Ser Asp Leu Ser Thr Leu Phe Asp Asp Trp Asn Leu Val Arg Pro Thr 305 310 315 320 Glu Met Gly Leu Val Pro Arg Val Ala Glu Met Leu Tyr Gln Arg Tyr 325 330 335 Gln Ser Ala Val Asp Arg Phe Glu Ile Ala Gly Ala Asp Thr Ala Ala 340 345 350 Ala Gln Ala Gln Ala Gln Thr Glu Leu Arg Glu Gln Val Leu Gly Gly 355 360 365 Arg Ile Val Thr Ala Phe Cys Gly Thr Ala Pro Leu Ala Ala Glu Met 370 375 380 Arg Ser Phe Ile Glu Thr Cys Leu Asp Val His Val Leu Asp Gly Tyr 385 390 395 400 Gly Leu Thr Glu Val Gly Met Val Thr Lys Asp Gly Arg Ile Asn Gln 405 410 415 Pro Pro Val Leu Gly Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr 420 425 430 Phe Leu Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser 435 440 445 Leu Thr Ala Met Pro Gly Tyr Phe Lys Arg Pro Asp Val Thr Thr Lys 450 455 460 Ala Phe Asp Pro Glu Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu 465 470 475 480 Leu Glu Pro Gly Arg Leu Ala Tyr Val Asp Arg Arg Asn Asn Val Leu 485 490 495 Lys Leu Ala Gln Gly Glu Phe Val Ala Val Ala Arg Leu Glu Ala Val 500 505 510 Phe Ser Ser Ala Ala Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser 515 520 525 Glu Arg Pro Tyr Leu Leu Ala Val Val Val Pro Thr Asp Asp Ala Ala 530 535 540 Glu Arg Phe Ala Gly Asp Ala Asp Gly Leu Lys Ala Ala Leu Ala Glu 545 550 555 560 Ser Leu Arg Gln Ser Ala Lys Leu Ala Glu Leu Gln Ser Tyr Glu Val 565 570 575 Pro Val Asp Phe Val Val Glu Thr Glu Pro Phe Ser Glu Asp Asn Gly 580 585 590 Leu Leu Ser Gly Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu His 595 600 605 Tyr Gly Ala Arg Leu Glu Gln Leu Tyr Ala Glu Leu Ala Glu Asn Arg 610 615 620 Val Thr Glu Leu Arg Ala Leu Arg Glu Gly Ala Ala Asp His Pro Val 625 630 635 640 Ile Phe Thr Leu Ser Arg Ala Ala Glu Ala Leu Leu Gly Leu Ala Gly 645 650 655 Gly Pro Pro Ala Pro Asp Ala Leu Phe Ile Glu Leu Gly Gly Asp Ser 660 665 670 Leu Ser Ala Leu Thr Phe Ser Asn Leu Leu Arg Asp Ile Phe Asp Val 675 680 685 Glu Val Pro Val Gly Met Ile Thr Gly Pro Ala Thr Asp Leu Gly Gln 690 695 700 Leu Ala Glu Tyr Val Glu Ser Glu Arg Val Ser Gly Ser Arg Arg Pro 705 710 715 720 Thr Phe Ala Thr Val His Gly Arg Ser Ala Thr Gln Val Arg Ala Ala 725 730 735 Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Thr Thr Leu Ala Glu Ala 740 745 750 Pro Ala Leu Pro Arg Ala Thr Gly Thr Pro His Ala Val Leu Leu Thr 755 760 765 Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu Ile Leu Glu Trp Leu Glu 770 775 780 Arg Leu Ala Glu Thr Gly Gly Lys Leu Ile Ser Val Ile Arg Ala Ala 785 790 795 800 Asp Thr Ala Ala Ala Thr Lys Arg Leu Glu Ala Val Phe Asp Ser Gly 805 810 815 Asp Pro Gln Leu Leu Gln Arg Phe Arg Arg Leu Ala Ala Glu His Leu 820 825 830 Glu Ile Ile Val Gly Asp Ile Gly Glu Pro Asn Leu Gly Leu Glu Gln 835 840 845 Gly Thr Trp Glu Arg Leu Ala Gln Ser Val Asp Leu Ile Val His Pro 850 855 860 Ala Ala Leu Val Asn His Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro 865 870 875 880 Asn Val Val Gly Thr Ala Glu Leu Ile Arg Leu Ala Ile Thr Thr Arg 885 890 895 Ile Lys Pro Val Thr Tyr Met Ser Thr Val Ala Val Ala Leu Ser Val 900 905 910 Asp Pro Ala Ala Phe Ala Glu Asp Gly Asp Ile Arg Thr Val Ser Ala 915 920 925 Leu Arg Pro Val Asp Asp Ser Tyr Ala Asn Gly Tyr Ala Asn Ser Lys 930 935 940 Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu 945 950 955 960 Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Arg Tyr 965 970 975 Ala Gly Gln Leu Asn Val Pro Asp Ala Phe Thr Arg Leu Val Phe Ser 980 985 990 Leu Leu Thr Thr Gly Ile Ala Pro Ala Ser Phe Tyr Gln Thr Asp Pro 995 1000 1005 Gln Gly Asn Arg Pro Val Ala His Tyr Asp Gly Leu Pro Ala Asp 1010 1015 1020 Phe Val Ala Glu Ala Val Thr Thr Leu Gly Glu Gln Ile Ala Ser 1025 1030 1035 Ala Ala Glu Asp Ser Gly Ala Tyr Arg Ser Phe Asp Val Met Asn 1040 1045 1050 Pro His Asp Asp Gly Ile Ser Leu Asp Val Phe Val Asp Trp Leu 1055 1060 1065 Ile Ala Ala Gly His Asp Ile Arg Arg Ile Asp Asp Tyr Asp Glu 1070 1075 1080 Trp Leu Gly Arg Phe Thr Thr Ala Leu Arg Ala Leu Pro Asp Thr 1085 1090 1095 Gln Arg Gln His Ser Val Leu Pro Leu Leu Asp Ala Tyr Arg Lys 1100 1105 1110 Pro Glu Thr Pro Leu Arg Gly Ala Pro Ala Pro Thr Asp Val Phe 1115 1120 1125 Arg Ser Ala Val Arg Ser Ala Lys Ile Gly Ala Asp Glu Asp Ile 1130 1135 1140 Pro His Leu Ser Ala Ala Leu Ile Asp Lys Tyr Val Ala Asp Leu 1145 1150 1155 Arg Leu Leu Gly Leu Val 1160 <210> 245 <211> 1188 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. TKK-01-0059 <400> 245 Met Ala Gly Asp Ala Lys His Thr Lys Val Ser Ser Arg Gly Pro Ala 1 5 10 15 Arg Glu Arg Val Ala Asp Arg Ile Arg Glu Leu Ala Ala Thr Asp Glu 20 25 30 Gln Phe Arg Asn Ala Glu Pro Asp Pro Ala Leu Gln Arg Ala Ala Arg 35 40 45 Gln Pro Gly Leu Arg Leu Pro Gln Ile Leu Glu Leu Phe Val Glu Gly 50 55 60 Tyr Ala Asp Arg Pro Ala Val Gly Trp Arg Ala Arg Thr Leu His Thr 65 70 75 80 Asp Pro Ala Thr Gly Arg Thr Thr Thr Arg Leu Leu Pro Arg Phe Asp 85 90 95 Thr Met Thr Tyr Arg Glu Leu Trp Asp Asp Val Arg Ala Ile Ala Ala 100 105 110 Ala Trp Arg His Asp Ala Ala Asn Pro Val Ser Pro Gly Asp Phe Val 115 120 125 Ala Thr Val Gly Phe Ala Ser Ala Glu Tyr Leu Thr Leu Asp Leu Val 130 135 140 Cys Gly Tyr Leu Gly Leu Val Ala Val Pro Leu Gln His Asn Thr Thr 145 150 155 160 Ala Ser Arg Leu Arg Pro Ile Val Asp Glu Val Glu Pro Ser Ile Leu 165 170 175 Ala Ala Gly Val Gly Tyr Leu Asp Leu Ala Val Glu Ala Ala Ala Gly 180 185 190 Ser Pro Ser Leu Arg Arg Leu Val Val Phe Asp Tyr Gln Pro Glu Val 195 200 205 Asp Glu Gln Arg Glu Ala Leu Gln Arg Ala Glu Ala Arg Leu Ala Ala 210 215 220 Ala Gly Ala Ala Val Thr Ile Glu Thr Leu Asp Glu Ile Ile Glu Arg 225 230 235 240 Gly Arg Ala Leu Pro Pro Glu Pro Met Tyr Thr Gly Asp Thr Asp Gln 245 250 255 Arg Leu Ala Met Ile Met Tyr Thr Ser Gly Ser Thr Gly Leu Pro Lys 260 265 270 Gly Ala Met Tyr Thr Glu Gln Met Leu Ala Lys Val Trp Thr Asn Glu 275 280 285 Leu Met Pro Asp Phe Ala Asp Thr Pro Val Phe Asn Val Asn Phe Met 290 295 300 Pro Leu Asn His Leu Gly Gly Arg Ile Pro Leu Ser Thr Ala Phe Gln 305 310 315 320 Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp Leu Ser Thr Leu 325 330 335 Phe Asp Asp Trp Asn Leu Val Arg Pro Thr Glu Met Gly Leu Val Pro 340 345 350 Arg Val Ala Glu Met Leu Tyr Gln Arg Tyr Gln Ser Ala Val Asp Arg 355 360 365 Leu Val Ala Ser Gly Ala Asp Ala Gly Ser Ala Glu Ser Arg Ala Arg 370 375 380 Asp Glu Leu Arg Glu Gln Val Leu Gly Gly Arg Ile Val Thr Ala Phe 385 390 395 400 Cys Gly Thr Ala Pro Leu Ala Ala Glu Met Arg Ala Phe Val Glu Thr 405 410 415 Cys Leu Asp Val His Val Leu Asp Gly Tyr Gly Leu Thr Glu Val Gly 420 425 430 Met Val Thr Lys Asp Gly Arg Met Thr Arg Pro Pro Val Leu Asp Tyr 435 440 445 Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe His Thr Asp Lys Pro 450 455 460 Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Leu Thr Ala Thr Pro Gly 465 470 475 480 Tyr Phe Lys Arg Pro Asp Val Thr Ala Asn Ala Phe Asp Pro Asp Gly 485 490 495 Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu Leu Glu Pro Asp Arg Leu 500 505 510 Ala Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly Glu 515 520 525 Phe Val Ala Val Ala Arg Leu Glu Ala Val Phe Ala Ser Ala Pro Leu 530 535 540 Ile Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Pro Tyr Leu Leu 545 550 555 560 Ala Val Val Val Pro Thr Ala Asp Ala Ala Glu Arg Phe Gly Gly Asp 565 570 575 Pro Glu Gly Leu Lys Ala Ala Leu Ala Glu Ser Leu Arg Gln Ser Ala 580 585 590 Gln Leu Ala Glu Leu Gln Ser Tyr Glu Val Pro Val Asp Phe Ile Val 595 600 605 Glu Thr Glu Pro Phe Ser Glu Asp Asn Gly Leu Leu Ser Gly Val Gly 610 615 620 Lys Leu Leu Arg Pro Lys Leu Lys Glu Arg Tyr Ala Asp Gly Leu Glu 625 630 635 640 Gln Leu Tyr Ala Glu Leu Ala Glu Asn Arg Val Thr Glu Leu Arg Ala 645 650 655 Leu Arg Glu Gly Ala Asp Lys His Pro Val Ile Phe Thr Leu Thr Arg 660 665 670 Ala Ala Glu Ala Leu Leu Gly Val Ala Gly Gly Pro Pro Glu Pro Asp 675 680 685 Ala Leu Phe Ile Glu Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe 690 695 700 Ser Asn Leu Leu Arg Asp Ile Phe Asp Val Asp Val Pro Val Gly Met 705 710 715 720 Ile Thr Gly Pro Ala Thr Asp Leu Gly Gln Leu Ala Glu Tyr Val Glu 725 730 735 Ser Glu Arg Lys Ser Gly Ser Arg Arg Pro Thr Phe Ala Thr Val His 740 745 750 Gly Arg Gly Ala Ala Glu Val Arg Ala Ala Glu Leu Thr Leu Asp Lys 755 760 765 Phe Ile Asp Ala Lys Thr Leu Ala Val Ala Pro Thr Leu Pro Arg Ala 770 775 780 Thr Gly Thr Pro His Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu 785 790 795 800 Gly Arg Phe Leu Ala Leu Glu Trp Leu Glu Arg Leu Ala Glu Thr Gly 805 810 815 Gly Lys Leu Val Ser Ile Ile Arg Ala Thr Asp Thr Ala Thr Ala Val 820 825 830 Lys Arg Leu Glu Ala Val Phe Asp Ser Gly Asp Pro Gln Leu Leu Glu 835 840 845 Arg Phe Arg Thr Leu Ala Ala Glu His Leu Glu Val Ile Val Gly Asp 850 855 860 Ile Gly Glu Pro Asn Leu Gly Leu Asp Gln Ala Thr Trp Gln Arg Leu 865 870 875 880 Ala Gln Ser Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His 885 890 895 Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala 900 905 910 Glu Leu Ile Arg Leu Ala Val Thr Thr Arg Ile Lys Pro Val Thr Tyr 915 920 925 Leu Ser Thr Val Ala Val Ala Met Thr Val Asp Pro Gly Glu Phe Ala 930 935 940 Glu Asp Gly Asp Ile Arg Ala Val Ser Ala Val Arg Pro Ile Asp Asp 945 950 955 960 Gly Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Gly Glu Val Leu 965 970 975 Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg 980 985 990 Ser Asp Met Ile Leu Ala His Ser Arg Tyr Ala Gly Gln Leu Asn Val 995 1000 1005 Pro Asp Ala Phe Thr Arg Leu Met Phe Ser Leu Leu Thr Thr Gly 1010 1015 1020 Ile Ala Pro Ser Ser Phe Tyr Arg Thr Asp Glu His Gly Asn Arg 1025 1030 1035 Ala Val Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Val Ala Glu 1040 1045 1050 Ala Val Thr Thr Leu Gly Glu Gln Met Ala Ala Glu Glu Ser Gly 1055 1060 1065 Glu Tyr Arg Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly Val 1070 1075 1080 Ser Leu Asp Val Phe Val Asp Trp Leu Ile Ala Ala Gly His Asp 1085 1090 1095 Ile Arg Arg Ile Glu Asp Tyr Asp Glu Trp Leu Gly Arg Phe Thr 1100 1105 1110 Thr Ala Leu Arg Val Leu Pro Asp Lys Gln Arg Gln His Ser Val 1115 1120 1125 Leu Pro Leu Leu Asp Ala Tyr Arg Glu Pro Ala Thr Pro Leu Arg 1130 1135 1140 Gly Ala Pro Ala Pro Thr Asp Val Phe Arg His Ala Val Arg Thr 1145 1150 1155 Ala Lys Ile Gly Glu Asp Glu Asp Ile Pro His Leu Ser Ala Ala 1160 1165 1170 Leu Ile Asp Lys Tyr Val Ala Asp Leu Arg Leu Leu Gly Leu Val 1175 1180 1185 <210> 246 <211> 1189 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium ahvazicum <400> 246 Met Thr Ile Asp Ala Lys Arg Asp Asn Gly Thr Ser Ala Ser Val Thr 1 5 10 15 Thr Thr Pro Arg Glu Arg Val Ala Glu Arg Ile Arg Arg Val Val Ala 20 25 30 Thr Asp Glu Gln Tyr Gln Tyr Ala Arg Pro Asp Leu Ala Leu Gln Ala 35 40 45 Ala Ala Arg Arg Pro Gly Leu Arg Leu Pro Gln Ile Leu Glu Thr Phe 50 55 60 Val Glu Gly Tyr Gly Asp Arg Pro Ala Leu Gly Trp Arg Ala Arg Glu 65 70 75 80 Leu Ser Thr Asp Pro Thr Thr Gly Arg Thr Thr Thr Arg Leu Leu Pro 85 90 95 Arg Phe Asp Thr Ile Ser Tyr Arg Asp Leu Trp Ala Asn Val Arg Ala 100 105 110 Val Ala Thr Ala Trp Arg Arg Asp Glu Ala Thr Pro Val Ala Pro Gly 115 120 125 Asp Val Val Ala Thr Leu Gly Phe Ala Ser Pro Glu Tyr Leu Thr Leu 130 135 140 Asp Leu Val Thr Gly Tyr Leu Gly Leu Val Ala Val Pro Leu Gln His 145 150 155 160 Asn Ala Thr Ala Ser Arg Leu Gln Arg Ile Val Ala Glu Ile Glu Pro 165 170 175 Gln Val Leu Ala Ala Gly Ala Glu Tyr Leu Asp Leu Ala Val Glu Ala 180 185 190 Ala Leu Gly Ser Thr Ser Leu Arg Arg Leu Val Val Phe Asp Tyr Gln 195 200 205 Thr Asp Ile Asp Asp Gln Arg Glu Asn Leu Glu Arg Ala Gln Ala Lys 210 215 220 Leu Ala Glu Ala Gly Met Ala Val Thr Val Glu Ile Phe Asp Glu Leu 225 230 235 240 Val Glu Arg Gly Arg Ala Leu Pro Pro Glu Pro Phe Tyr Thr Gly Glu 245 250 255 Thr Asp Glu Arg Leu Ala Met Ile Met Tyr Thr Ser Gly Ser Thr Gly 260 265 270 Leu Pro Lys Gly Ala Met Tyr Thr Glu Arg Met Ile Leu Arg Leu Trp 275 280 285 Thr Asn Glu Leu Tyr Pro Glu Phe Ala Asp Val Pro Val Phe Asn Val 290 295 300 Asn Phe Met Pro Leu Asn His Val Gly Gly Arg Ile Pro Leu Ser Ser 305 310 315 320 Ser Phe Gln Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp Leu 325 330 335 Ser Thr Leu Phe Asp Asp Trp Asn Leu Val Arg Pro Thr Glu Met Gly 340 345 350 Met Val Pro Arg Val Val Glu Met Leu Tyr Gln Arg Tyr Gln Ser Ala 355 360 365 Val Glu Arg Leu Ile Gly Gln Gly Ala Glu Pro Glu Asp Ala Asp Ala 370 375 380 Ala Ala Lys Ala Glu Leu Arg Glu Gln Leu Leu Gly Gly Arg Val Ile 385 390 395 400 Thr Ala Phe Ser Thr Thr Ala Pro Leu Ala Ala Glu Met Lys Thr Phe 405 410 415 Ile Glu Ser Cys Leu Asp Thr His Val Leu Asp Gly Tyr Gly Leu Thr 420 425 430 Glu Val Gly Met Val Phe Lys Asp Gly Val Val Ser Arg Pro Pro Ile 435 440 445 Leu Asp Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe His Thr 450 455 460 Asp Lys Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Gln Thr Ala 465 470 475 480 Phe Gly Gly Tyr Phe Lys Arg Pro Asp Val Thr Ala Asn Ala Phe Asp 485 490 495 Pro Asp Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu Ile Gly Pro 500 505 510 Asp Arg Leu Val Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala 515 520 525 Gln Gly Glu Phe Val Ala Val Ala Arg Leu Glu Ala Val Phe Ser Ser 530 535 540 Ala Ala Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Pro 545 550 555 560 Tyr Leu Val Ala Val Val Val Pro Thr Arg Glu Ala Glu Gln Arg Phe 565 570 575 Ala Gly Asp Pro Asp Gly Leu Lys Ala Ala Leu Ser Glu Ser Leu Arg 580 585 590 Arg Thr Ala Lys Leu Ala Glu Leu Gln Ser Tyr Glu Val Pro Ala Asp 595 600 605 Phe Leu Val Asp Ser Glu Pro Phe Ser Glu Asp Asn Gly Leu Leu Ser 610 615 620 Gly Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu His Tyr Gly Ala 625 630 635 640 Arg Leu Glu Asp Leu Tyr Ala Glu Leu Ala Ala Thr Arg Thr Ala Glu 645 650 655 Leu Arg Ala Leu Arg Glu Gly Ala Ala Asp Arg Pro Val Ile Asp Thr 660 665 670 Leu Thr Arg Ala Ala Gln Ala Leu Leu Gly Leu Pro Gly Gly Ser Pro 675 680 685 Gln Pro His Thr Gln Phe Leu Glu Leu Gly Gly Asp Ser Leu Ser Ala 690 695 700 Leu Thr Phe Ser Asn Leu Leu Gln Asp Ile Phe Asp Val Gln Val Pro 705 710 715 720 Val Gly Gln Ile Ile Ser Pro Ala Ser Asp Leu Gly Gln Leu Ala Glu 725 730 735 Tyr Val Glu Ser Glu Arg Glu Ser Gly Ala Lys Arg Pro Thr Phe Ser 740 745 750 Thr Val His Gly Arg Gly Ala Ser Glu Val Arg Ala Ser Glu Leu Thr 755 760 765 Leu Asp Lys Phe Ile Asp Ala Ala Thr Leu Asn Ala Ala Pro Lys Leu 770 775 780 Pro His Ala Thr Gly Thr Pro His Thr Val Leu Leu Thr Gly Ala Asn 785 790 795 800 Gly Tyr Leu Gly Arg Phe Leu Thr Leu Glu Trp Leu Glu Arg Leu Ala 805 810 815 Asp Arg Gly Gly Lys Leu Ile Thr Ile Ile Arg Gly Thr Asp Ser Glu 820 825 830 Ala Ala Ala Lys Arg Leu Glu Ala Val Phe Asp Gly Gly Asp Pro Gly 835 840 845 Leu Leu Gln Arg Tyr Arg Thr Leu Ala Ala Asp His Leu Glu Val Ile 850 855 860 Val Gly Asp Ile Ala Glu Pro Asn Leu Gly Leu Asp Gln Ala Thr Trp 865 870 875 880 Gln Arg Leu Ala Glu Asp Val Glu Met Ile Val His Pro Ala Ala Leu 885 890 895 Val Asn His Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro Asn Val Val 900 905 910 Gly Thr Ala Glu Leu Ile Arg Leu Ala Ile Thr Ile Arg Ile Lys Pro 915 920 925 Val Thr Tyr Met Ser Thr Val Ala Val Ala Met Ser Val Asp Pro Ser 930 935 940 Val Phe Ala Glu Asp Gly Asp Ile Arg Ala Val Ser Pro Val Arg Pro 945 950 955 960 Val Asp Asp Ser Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Gly Gly 965 970 975 Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Ala Thr 980 985 990 Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Gln Tyr Ala Gly Gln 995 1000 1005 Leu Asn Val Pro Asp Ala Phe Thr Arg Leu Ile Phe Ser Leu Leu 1010 1015 1020 Val Thr Gly Ile Ala Pro Ser Ser Phe Tyr Gln Thr Asp Pro Gln 1025 1030 1035 Gly Asn Arg Ala Val Ala His Tyr Asp Gly Leu Pro Ala Asp Phe 1040 1045 1050 Val Ala Glu Ser Val Thr Thr Leu Gly Glu Gln Thr Ala Val Ala 1055 1060 1065 Gly Gly Tyr Arg Ser Phe Asp Val Met Asn Pro His Asp Asp Gly 1070 1075 1080 Ile Ser Leu Asp Val Phe Val Asp Trp Leu Ile Ala Gly Gly Asn 1085 1090 1095 Asp Ile Arg Arg Ile Asp Asp His Asp Glu Trp Phe Gly Arg Phe 1100 1105 1110 Glu Thr Ala Leu Arg Ala Leu Pro Asp Lys Gln Arg Gln His Ser 1115 1120 1125 Val Leu Ala Leu Leu Asp Val Tyr Arg Lys Pro Glu Ala Pro Leu 1130 1135 1140 Arg Gly Ala Pro Ala Pro Thr Asp Val Phe Arg Gly Ala Val Arg 1145 1150 1155 Ala Ala Lys Ile Gly Ala Asp Lys Asp Ile Pro His Leu Ser Glu 1160 1165 1170 Gly Leu Ile Glu Lys Tyr Val Ala Asp Leu Arg Leu Leu Gly Leu 1175 1180 1185 Val <210> 247 <211> 1169 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium florentinum <400> 247 Met Asp Glu Asp Pro Asp Glu Arg Met Ser Arg Arg Val Ala Glu Tyr 1 5 10 15 Phe Asp Asn Asp Pro Gln Phe Arg Ala Ala Ala Pro Leu Pro Gly Val 20 25 30 Ile Glu Ala Val Gly Thr Pro Gly Leu Arg Leu Thr Glu Val Leu Glu 35 40 45 Thr Ile Val Glu Gly Tyr Ala Asp Arg Pro Ala Leu Gly Glu Arg Ala 50 55 60 Arg Gly Leu Val Thr Asp Ala Ala Gly Arg Thr Ser Val Arg Arg His 65 70 75 80 Pro Arg Phe Asp Thr Ile Ser Tyr Arg Glu Val Trp Asp Arg Val Arg 85 90 95 Ala Ile Ala Ser Ala Trp Arg Asn Asp Pro Glu Asn Pro Val Val Pro 100 105 110 Gly Asp Val Val Ala Thr Ile Gly Phe Ser Ser Ala Asp Tyr Leu Val 115 120 125 Val Asp Leu Val Cys Ala Tyr Leu Gly Leu Val Thr Val Pro Leu Gln 130 135 140 His Asn Ala Pro Val Ala Arg Leu Arg Pro Ile Ile Glu Glu Cys Glu 145 150 155 160 Pro Lys Ile Val Ala Val Ser Ala Glu Tyr Leu Asp Leu Ala Ala Glu 165 170 175 Ser Leu Leu Thr Ser Thr Ser Leu Arg Gln Val Met Val Phe Asp Tyr 180 185 190 Gln Ala Gly Ala Asp Glu Gln Arg Glu Asn Phe Glu Gln Thr Arg Val 195 200 205 Arg Leu Gln Gly Ser Asp Ala Ala Val Val Val Thr Thr Val Asp Asp 210 215 220 Val Val Glu Arg Gly Arg Glu Leu Pro Ala Val Ala Pro Phe Thr Glu 225 230 235 240 Asp Ser Asn Glu Arg Leu Ala Met Ile Met Tyr Thr Ser Gly Ser Thr 245 250 255 Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Arg Thr Ile Thr Thr Leu 260 265 270 Trp Ala Ser Met Leu Phe Leu Thr Pro Gly Leu Pro Val Ile Asn Val 275 280 285 Asn Phe Met Pro Leu Asn His Leu Gly Gly Arg Leu Pro Leu Ala Ser 290 295 300 Ala Phe Leu Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp Leu 305 310 315 320 Ser Thr Leu Phe Glu Asp Trp Ala Leu Val Arg Pro Thr Glu Val Gly 325 330 335 Val Val Pro Arg Val Val Glu Met Leu Tyr Gln His Tyr Arg Gly Val 340 345 350 Val Asp Arg Gly Ile Ala Glu Gly Ala Asp Pro Ala Thr Ala Glu Gln 355 360 365 Asp Ala Leu Thr Glu Leu Arg Glu His Val Leu Gly Gly Arg Val Met 370 375 380 Gly Gly Phe Val Gly Ser Ala Pro Leu Ala Ala Glu Met Lys Ala Phe 385 390 395 400 Leu Asp Ser Met Leu Gly Val His Val Thr Asp Gly Tyr Gly Leu Thr 405 410 415 Glu Thr Gly Met Leu Thr Arg Asp Gly Ile Ile Ser Arg Gln Arg Val 420 425 430 Ile Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Leu Thr 435 440 445 Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Thr Asp Thr Met 450 455 460 Thr Pro Gly Tyr Tyr Lys Arg Pro Glu Ile Thr Ala Glu Val Phe Asp 465 470 475 480 Glu Asp Gly Phe Tyr Lys Thr Gly Asp Val Met Ala Glu Ile Gly Pro 485 490 495 Asp His Leu Ile Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu Ala 500 505 510 Gln Gly Glu Phe Val Ala Val Ala Asn Leu Glu Ser Ile Tyr Ala Gly 515 520 525 Ala Pro Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg Pro 530 535 540 Ser Leu Leu Ala Val Ile Val Pro Thr Pro Glu Ala Leu Ala Glu Tyr 545 550 555 560 Gly Asn Ser Leu Ala Leu Lys Ser Ala Ile His Gln Ser Leu Gln Gln 565 570 575 Thr Ala Ala Ala Ala Gln Leu Gln Ser Tyr Glu Met Pro Val Asp Phe 580 585 590 Ile Leu Glu Thr Lys Pro Phe Thr Asp Glu Asn Gly Leu Leu Ser Gly 595 600 605 Leu Gly Lys Gln Leu Arg Pro Arg Leu Lys Gly His Tyr Gly Glu Ala 610 615 620 Leu Glu Gln Leu Tyr Thr Glu Ile Ala Ala Ala Gln Val Asp Glu Val 625 630 635 640 Arg Val Leu Arg Glu Thr Ala Thr Asp Arg Pro Val Val Glu Thr Leu 645 650 655 Thr Ala Ala Cys Arg Ala Leu Leu Gly Ile Ser Asp Ala Asp Pro Glu 660 665 670 Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe 675 680 685 Ser Arg Leu Leu Ala Glu Ile Phe His Val Glu Val Pro Val Ser Val 690 695 700 Ile Thr Ser Pro Ala Asn Asp Ile Ala Thr Ile Ala Asp Tyr Ile Asp 705 710 715 720 Ala Gln Arg Gly Thr Arg Val Gln Arg Pro Thr Phe Gly Thr Val His 725 730 735 Gly Gln Gly Ala Thr Ala Val Ala Thr Gly Glu Leu Thr Leu Asp Lys 740 745 750 Phe Ile Asp Ala Gln Thr Leu Ser Ala Ala Pro Ser Leu Pro His Ala 755 760 765 Thr Gly Ala Pro His Thr Val Leu Leu Thr Gly Ala Asn Gly Trp Leu 770 775 780 Gly Arg Phe Leu Thr Leu Glu Trp Leu Glu Arg Leu Ala Val Arg Gly 785 790 795 800 Gly Gln Leu Val Thr Ile Val Arg Gly Arg Asp Ala Asp Asp Ala Arg 805 810 815 Thr Arg Leu Glu Asn Ala Phe Asp Ser Gly Asp Pro Glu Leu Leu Ser 820 825 830 Arg Phe Arg Glu Leu Ala Ala Met His Leu Glu Val Leu Pro Gly Asp 835 840 845 Ile Gly Asp Gln Asp Leu Gly Leu Asp Pro Ala Thr Trp Gln Arg Leu 850 855 860 Ala Asp Thr Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala 885 890 895 Glu Leu Ile Arg Leu Ala Ile Thr Thr Gln Ile Lys Pro Val Thr Tyr 900 905 910 Leu Ser Thr Ile Ala Val Ala Met Thr Val Ala Pro Gly Gln Phe Gln 915 920 925 Glu Asp Gly Asp Ile Arg Arg Val Ser Pro Thr Arg Pro Leu Asn Asp 930 935 940 Asp Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Glu Ala Asn Glu Leu Cys Gly Leu Pro Val Ala Val Phe Arg 965 970 975 Ser Asp Met Ile Leu Ala His Thr Arg Tyr Arg Gly Gln Leu Asn Val 980 985 990 Pro Asp Met Phe Thr Arg Leu Ile Phe Ser Leu Leu Val Thr Gly Ile 995 1000 1005 Ala Pro His Ser Phe Tyr Glu Arg Asp Pro Ala Cys Ser Arg Ala 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Asp Phe Ile Ala Glu Ala 1025 1030 1035 Ile Thr Thr Ile Gly Ser Arg Val Thr Ala Gly Tyr Ser Ser Phe 1040 1045 1050 Asp Val Met Asn Pro Tyr Asp Asp Gly Val Ser Leu Asp Val Phe 1055 1060 1065 Val Asp Trp Leu Ile Arg Ala Gly Asn Lys Ile Gln Arg Ile Val 1070 1075 1080 Asp Tyr Asp Glu Trp Leu Ala Arg Phe Gln Thr Ala Leu Thr Gly 1085 1090 1095 Leu Pro Glu Arg Gln Arg Gln Gln Ser Val Leu Pro Leu Leu His 1100 1105 1110 Ala Phe Arg Lys Pro Glu Lys Ala Ile Arg Gly Ala Ala Ala Pro 1115 1120 1125 Ala Glu Ala Phe His Ala Ala Val Arg Ala Asp Lys Ile Gly Pro 1130 1135 1140 Ala Lys Asp Ile Pro His Ile Ser Ala Glu Leu Ile Asp Lys Tyr 1145 1150 1155 Ala Asp Asp Leu Arg Gln Leu Ser Leu Leu Gly 1160 1165 <210> 248 <211> 1172 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium europaeum <400> 248 Met Ala Asp Arg Ile Arg His Leu Asp Ala Val Asp Glu Gln Phe Arg 1 5 10 15 Thr Thr Lys Pro Asp Ala Ser Val Gln Gln Thr Ala Arg Glu Pro Gly 20 25 30 Leu Arg Leu Pro Glu Ile Leu Arg Thr Phe Val Glu Gly Tyr Ala Asp 35 40 45 Arg Ala Ala Leu Gly Trp Arg Ala Arg Ser Leu Val Thr Asp Ser Ala 50 55 60 Thr Gly Arg Thr Thr Ala Gln Leu Leu Pro Arg Phe Asp Thr Leu Thr 65 70 75 80 Tyr Arg Glu Leu Trp Ala Asn Val Gly Ala Ile Ala Ser Ala Trp Arg 85 90 95 Gly Asp Ala Thr Asn Pro Val Ala Pro Gly Asp Phe Val Ala Thr Val 100 105 110 Gly Phe Ala Ser Ala Glu Tyr Leu Thr Leu Asp Leu Val Cys Gly Tyr 115 120 125 Leu Gly Leu Val Ala Val Pro Leu Gln His Asn Ala Ala Ala Ser Arg 130 135 140 Leu Arg Pro Ile Val Thr Glu Val Glu Pro Arg Val Leu Ala Ala Gly 145 150 155 160 Ala Gly Tyr Leu Asp Leu Ala Val Glu Ala Ala Leu Gly Ser Ala Ser 165 170 175 Leu Arg Arg Leu Val Val Phe Asp Tyr Ser Pro Arg Ile Asp Asp Gln 180 185 190 Arg Glu Ala Val Glu Arg Ala Arg Ala Thr Leu Ser Ala Ala Gly Met 195 200 205 Thr Val Thr Val Glu Thr Phe Asp Glu Leu Ile Gly Arg Gly Arg Thr 210 215 220 Leu Pro Leu Glu Pro Ala Tyr Thr Gly Gly Thr Asp Glu Arg Leu Ala 225 230 235 240 Met Ile Met Tyr Thr Ser Gly Ser Thr Gly Leu Pro Lys Gly Ala Met 245 250 255 Tyr Thr Glu Arg Met Leu Cys Lys Leu Trp Thr Asn Glu Leu Met Pro 260 265 270 Glu Phe Ala Asp Thr Pro Val Leu Asn Val Asn Phe Met Pro Leu Asn 275 280 285 His Leu Gly Gly Arg Ile Pro Leu Ser Thr Ala Phe Gln Ala Gly Gly 290 295 300 Thr Ser Tyr Phe Val Pro Glu Ser Asp Leu Ser Thr Leu Phe Asp Asp 305 310 315 320 Trp Asn Leu Val Arg Pro Thr Glu Met Gly Leu Val Pro Arg Val Ala 325 330 335 Glu Met Leu Tyr Gln Arg Tyr Gln Ser Ala Val Asp Arg Arg Val Ser 340 345 350 Arg Gly Val Asp Pro Glu Ser Ala Ala Ala Glu Ala Arg Thr Glu Leu 355 360 365 Arg Glu Gln Val Leu Gly Gly Arg Ile Val Thr Ala Phe Cys Gly Thr 370 375 380 Ala Pro Leu Ala Ala Glu Met Arg Ser Phe Val Glu Thr Cys Leu Gly 385 390 395 400 Val His Val Leu Asp Gly Tyr Gly Leu Thr Glu Val Gly Met Val Thr 405 410 415 Lys Asp Gly Arg Ile Ala Arg Pro Pro Val Leu Asp Tyr Lys Leu Val 420 425 430 Asp Val Pro Glu Leu Gly Tyr Phe Leu Thr Asp Lys Pro Phe Pro Arg 435 440 445 Gly Glu Leu Leu Val Lys Ser Leu Thr Ala Thr Pro Gly Tyr Phe Lys 450 455 460 Arg Pro Asp Val Thr Ala Asn Ala Phe Asp Ala Gln Gly Tyr Tyr Arg 465 470 475 480 Thr Gly Asp Val Met Ala Glu Leu Glu Pro Asp Arg Leu Ala Tyr Val 485 490 495 Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly Glu Phe Val Ala 500 505 510 Val Ala Arg Leu Glu Ala Val Phe Ser Ser Ala Ala Leu Ile Arg Gln 515 520 525 Ile Phe Val Tyr Gly Asn Ser Glu Arg Pro Tyr Leu Leu Ala Val Ile 530 535 540 Val Pro Thr Ala Asp Ala Leu Glu Arg Phe Ala Gly Asp Pro Gly Gly 545 550 555 560 Leu Arg Ala Ala Leu Gly Glu Ser Leu Arg Gln Ser Gly Lys Leu Ala 565 570 575 Glu Leu Gln Ser Tyr Glu Val Pro Val Asp Phe Leu Val Glu Ala Asp 580 585 590 Pro Phe Ser Glu Asp Asn Gly Leu Leu Ser Gly Val Gly Lys Leu Leu 595 600 605 Arg Pro Lys Leu Lys Glu His Tyr Gly Glu Arg Leu Glu Arg Leu Tyr 610 615 620 Ala Asp Leu Ala Ala Asn Arg Ala Thr Glu Leu Arg Ala Leu Arg Asp 625 630 635 640 Gly Ala Ala Asp Arg Pro Val Ile Asp Thr Leu Val Ser Ala Ala Glu 645 650 655 Ala Leu Leu Gly Leu Ala Gly Gly Pro Pro Asp Pro Gly Ala Leu Phe 660 665 670 Ile Glu Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser Asn Leu 675 680 685 Leu Gln Asp Ile Phe Asp Val Glu Val Pro Val Gly Met Ile Thr Gly 690 695 700 Pro Ala Thr Thr Leu Ser Gln Leu Ala Glu Tyr Val Ala Ala Glu Arg 705 710 715 720 Arg Ser Gly Ser Arg Arg Pro Thr Phe Ala Thr Val His Gly Arg Asp 725 730 735 Ala Thr Glu Val Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp 740 745 750 Ala Lys Thr Leu Ala Ala Ala Ala Gly Leu Pro Cys Ala Thr Gly Thr 755 760 765 Ser His Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe 770 775 780 Leu Cys Leu Glu Trp Leu Glu Arg Leu Ala Glu Thr Gly Gly Lys Leu 785 790 795 800 Val Cys Ile Val Arg Gly Ala Asp Ala Ala Ala Ala Ala Glu Arg Leu 805 810 815 Glu Gly Val Tyr Arg Ser Gly Asp Pro Arg Leu Leu Glu Arg Phe Arg 820 825 830 Glu Leu Ala Ala Asp His Leu Glu Val Ile Ala Gly Asp Ile Gly Glu 835 840 845 Pro Asn Leu Gly Leu Asp Pro Ala Thr Trp Asp Ser Leu Ala Arg Gly 850 855 860 Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His Val Leu Pro 865 870 875 880 Tyr Asp Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile 885 890 895 Arg Leu Ala Ile Thr Glu Arg Val Lys Pro Val Asn Tyr Leu Ser Thr 900 905 910 Val Ala Val Ala Met Ser Val Ala Glu Phe Ala Glu Asp Gly Asp Ile 915 920 925 Arg Ala Ile Ser Ala Val Arg Pro Ile Asp Asn Gly Tyr Ala Asn Gly 930 935 940 Tyr Ala Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His 945 950 955 960 Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu 965 970 975 Ala His Ser Arg Tyr Ala Gly Gln Leu Asn Val Pro Asp Ala Phe Thr 980 985 990 Arg Leu Ile Phe Ser Leu Leu Val Thr Gly Ile Ala Pro Ala Ser Phe 995 1000 1005 Tyr Glu Ala Thr Asp Thr Gly Gly Arg Ala Val Ala His Tyr Asp 1010 1015 1020 Gly Leu Pro Ala Asp Phe Val Ala Glu Ala Val Thr Ala Leu Gly 1025 1030 1035 Glu Gln Ile Ala Thr Val Ala Asp Asp Ala Ala Ala Thr Gly Thr 1040 1045 1050 Phe Arg Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly Ile Ser 1055 1060 1065 Leu Asp Val Phe Val Asp Trp Leu Val Ala Asp Gly His Asp Ile 1070 1075 1080 Arg Arg Ile Glu Asp Tyr Asp Glu Trp Leu Gly Arg Phe Gly Thr 1085 1090 1095 Ala Leu Arg Ala Leu Pro Asp Arg Gln Arg Gln Leu Ser Ala Leu 1100 1105 1110 Pro Leu Leu Asp Ala Tyr Arg Lys Pro Glu Arg Pro Leu Arg Gly 1115 1120 1125 Ala Pro Ala Pro Thr Asp Ala Phe Arg Gly Ala Val Arg Thr Ala 1130 1135 1140 Lys Leu Gly Ala Asp His Asp Ile Pro His Leu Ser Ala Asp Leu 1145 1150 1155 Ile Ala Lys Tyr Val Leu Asp Leu Arg Leu Leu Gly Leu Leu 1160 1165 1170 <210> 249 <211> 1178 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. E1319 <400> 249 Met Gly Pro His Arg Ala Arg Val Ala Asp Arg Ile Arg Arg Leu Asp 1 5 10 15 Ala Gly Asp Glu Gln Phe Arg Arg Ala Lys Pro Asp Leu Asp Val Gln 20 25 30 Arg Ala Ala Arg Glu Pro Gly Gln Arg Leu Pro Gln Ile Leu Gln Thr 35 40 45 Phe Val Glu Gly Tyr Ala Asp Arg Pro Ala Leu Gly Trp Arg Ala Arg 50 55 60 Glu Leu Thr Thr Asp Pro Ala Thr Gly Arg Thr Gly Ser Arg Leu Leu 65 70 75 80 Pro Arg Phe Asp Thr Val Thr Tyr Arg Glu Leu Trp Asp Asn Val Ala 85 90 95 Ala Ile Ala Ala Ala Trp Arg Asn Asp Ala Ala Asn Pro Val Ala Pro 100 105 110 Gly Asp Phe Leu Ala Thr Val Gly Phe Ala Ser Ala Glu Tyr Leu Thr 115 120 125 Leu Asp Leu Val Cys Ala Tyr Leu Gly Leu Val Ala Val Pro Leu Gln 130 135 140 His Asn Ala Thr Ala Thr Arg Leu Gln Pro Ile Val Ala Glu Val Glu 145 150 155 160 Pro Arg Val Leu Ala Ala Ser Ala Gly Tyr Leu Asp Leu Ala Val Asp 165 170 175 Ala Ala Val Gly Ser Ala Ser Leu Gln Arg Leu Val Val Phe Asp Tyr 180 185 190 Arg Pro Glu Ile Asp Asp His Arg Asp Ala Leu Glu Arg Ala Arg Ala 195 200 205 Lys Leu Ser Ala Ala Ala Met Ala Val Thr Ile Glu Thr Leu Asp Glu 210 215 220 Val Leu Ala Arg Gly Arg Thr Leu Pro Pro Glu Pro Ile Tyr Thr Gly 225 230 235 240 Asp Ser Asp Glu Arg Leu Ala Met Ile Met Tyr Thr Ser Gly Ser Thr 245 250 255 Gly Leu Pro Lys Gly Ala Met Tyr Thr Glu Arg Thr Leu Cys Lys Leu 260 265 270 Trp Thr Leu Glu Met Leu Pro Asp Leu Ala Asp Val Pro Val Leu Asn 275 280 285 Val Asn Phe Met Pro Leu Asn His Leu Gly Gly Arg Ile Pro Leu Ala 290 295 300 Thr Ser Phe Gln Ser Gly Gly Thr Ser Tyr Phe Val Pro Glu Ser Asp 305 310 315 320 Leu Ser Thr Leu Phe Asp Asp Trp Asn Leu Val Arg Pro Thr Glu Met 325 330 335 Gly Leu Val Pro Arg Val Ala Glu Met Leu Tyr Gln Arg Tyr Gln Ser 340 345 350 Ala Val Asp Arg Arg Leu Val Asp Gly Ala Asp Ala Ala Asp Ala Glu 355 360 365 Glu Gln Ala Arg Ala Glu Leu Arg Asp Gln Val Leu Gly Gly Arg Val 370 375 380 Val Thr Ala Phe Cys Gly Thr Ala Pro Leu Thr Ala Glu Met Arg Asn 385 390 395 400 Phe Val Glu Thr Ser Leu Gly Val His Ile Leu Asp Gly Tyr Gly Leu 405 410 415 Thr Glu Leu Gly Met Val Thr Lys Asp Gly Trp Ile Ala Arg Pro Pro 420 425 430 Val Leu Asp Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg 435 440 445 Thr Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Leu Thr 450 455 460 Ala Thr Pro Gly Tyr Phe Lys Arg Pro Asp Val Thr Ala Ala Ala Phe 465 470 475 480 Asp Glu Asp Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu Leu Glu 485 490 495 Pro Asp Arg Leu Ala Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu 500 505 510 Ser Gln Gly Glu Phe Val Ala Val Ala Arg Leu Glu Ala Val Phe Ala 515 520 525 Ala Ala Ala Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg 530 535 540 Pro Tyr Leu Leu Ala Val Ile Val Pro Thr Asp Asp Ala Val Arg Arg 545 550 555 560 Phe Ala Gly Asp Pro Asp Gly Leu Lys Ala Val Leu Ala Glu Ser Leu 565 570 575 Arg His Ala Ala Arg Leu Ala Glu Leu Gln Ser Tyr Glu Val Pro Ile 580 585 590 Asp Phe Leu Val Glu Ser Glu Pro Phe Thr Glu Asp Asn Gly Leu Leu 595 600 605 Ser Gly Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu Arg Tyr Ala 610 615 620 Asp Glu Leu Glu Gln Arg Tyr Ala Glu Leu Ala Thr Asn Arg Ala Thr 625 630 635 640 Glu Leu Arg Ala Leu Arg Asp Gly Ala Glu Asp Arg Pro Val Ile Asp 645 650 655 Thr Val Ala Arg Ala Ala Glu Ala Leu Leu Gly Leu Pro Asp Gly Pro 660 665 670 Pro Ala Pro Glu Ala Ser Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser 675 680 685 Ala Leu Asn Phe Ser Asn Leu Leu Arg Asp Ile Phe Asp Val Glu Val 690 695 700 Pro Val Gly Thr Leu Ile Gly Pro Thr Thr Asp Leu Arg Gln Ile Ala 705 710 715 720 Ala Leu Ile Glu Ala Gly Arg Glu Ser Gly Asn Leu Arg Pro Thr Leu 725 730 735 Ala Ser Val His Gly Arg Asp Ala Thr Ser Ala Arg Ala Ala Asp Leu 740 745 750 Thr Leu Asp Lys Phe Ile Asp Ala Gln Thr Leu Ala Ala Ala Pro Thr 755 760 765 Leu Pro His Leu Thr Gly Ala Pro Thr Thr Val Leu Leu Thr Gly Ala 770 775 780 Asn Gly Tyr Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Glu Arg Leu 785 790 795 800 Ala Val Ser Gly Gly Arg Leu Ile Cys Val Val Arg Gly Ala Asp Ala 805 810 815 Ala Ala Ala Thr Ala Arg Leu Glu Asp Ala Tyr Arg Ser Gly Asp Pro 820 825 830 Gln Leu Leu Arg Arg Phe Arg Glu Leu Ala Ala Glu His Leu Glu Val 835 840 845 Leu Ala Gly Asp Ile Gly Glu Pro Asn Leu Gly Leu Gly Gln Asp His 850 855 860 Trp His Arg Leu Thr Glu Thr Val Asp Leu Ile Val His Pro Ala Ala 865 870 875 880 Leu Val Asn His Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro Asn Val 885 890 895 Val Gly Thr Ala Glu Val Ile Arg Leu Ala Leu Thr Ala Arg Ile Lys 900 905 910 Ala Val Thr Tyr Leu Ser Thr Val Ala Val Ala Leu Ser Ile Asp Pro 915 920 925 Ala Glu Phe Ala Glu Asp Gly Asp Ile Arg Val Val Ser Ala Glu Arg 930 935 940 Pro Ile Asp Thr Ser Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala 945 950 955 960 Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val 965 970 975 Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Ser His His Ala Gly 980 985 990 Gln Leu Asn Val Pro Asp Ala Phe Thr Arg Leu Leu Ile Ser Leu Leu 995 1000 1005 Leu Thr Gly Ile Ala Pro Ala Ser Phe Tyr Glu Val Pro Ala Gly 1010 1015 1020 Gly Gly Arg Ala Asn Ala His Tyr Asp Gly Leu Pro Ala Asp Phe 1025 1030 1035 Val Ala Glu Ala Val Thr Thr Leu Gly Glu Arg Leu Ala Ser Thr 1040 1045 1050 Pro Ala Ala Tyr Gly Gly Tyr Arg Ser Phe Asp Val Met Asn Pro 1055 1060 1065 His Asp Asp Gly Ile Ser Leu Asp Val Val Val Asp Trp Leu Ile 1070 1075 1080 Gly Ala Gly Arg Asp Ile Arg Arg Ile Asp Asp Tyr Gln Glu Trp 1085 1090 1095 Leu Gly Arg Phe Ser Thr Ala Leu Arg Ala Leu Pro Asp Lys Gln 1100 1105 1110 Arg Ala Gln Ser Val Leu Pro Leu Leu Asp Val Tyr Arg Ser Pro 1115 1120 1125 Gln Glu Ala Leu Arg Gly Ala Pro Ala Pro Thr Glu Val Phe Arg 1130 1135 1140 Thr Ala Val Gln Ser Ala Lys Ile Gly Ala Asp Gln Asp Ile Pro 1145 1150 1155 His Leu Ser Ala Lys Leu Ile Glu Lys Tyr Val Ser Asp Leu Ala 1160 1165 1170 Leu Leu Gly Leu Ala 1175 <210> 250 <211> 1165 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium arosiense ATCC BAA-1401 (DSM 45069) <400> 250 Met Asp Ala Arg Asp Glu Gln Phe Arg Thr Thr Lys Pro Glu Pro Ala 1 5 10 15 Leu Gln Ser Ala Ala Arg Glu Thr Gly Leu Arg Leu Pro Gln Ile Leu 20 25 30 Glu Ile Phe Ala Gln Gly Tyr Ala Glu Arg Pro Ala Leu Gly Trp Arg 35 40 45 Ala Arg Ser Leu Thr Thr Asp Pro Asp Thr Gly Arg Thr Ala Thr Gln 50 55 60 Leu Leu Pro Arg Phe Asp Thr Met Thr Tyr Arg Glu Leu Trp Ala Asp 65 70 75 80 Val Arg Ala Ile Ala Ala Ala Trp Arg His Ala Pro Thr Asn Pro Val 85 90 95 Ala Pro Gly Asp Phe Val Ala Thr Val Gly Phe Ala Ser Ala Glu Tyr 100 105 110 Leu Thr Ile Asp Leu Ala Cys Gly Tyr Leu Gly Leu Val Ala Val Pro 115 120 125 Leu Gln His Asn Thr Thr Ala Ala Arg Leu Lys Pro Ile Val Asp Glu 130 135 140 Ala Glu Pro Ser Val Leu Ala Ala Gly Val Gly Tyr Leu Asp Leu Ala 145 150 155 160 Ile Asp Ala Ala Leu Asn Ser Ser Ser Leu Arg Arg Val Val Val Phe 165 170 175 Asp Tyr Gln Pro Glu Val Asp Asp Gln Arg Glu Ala Val Glu Arg Ala 180 185 190 Gln Ala Lys Leu Ser Gly Ala Gly Ile Ala Val Thr Ile Glu Thr Leu 195 200 205 Ala Glu Val Ile Glu Arg Gly Arg Ser Leu Pro Pro Glu Pro Met Phe 210 215 220 Thr Gly Asp Thr Asp Glu Arg Leu Ala Met Ile Met Tyr Thr Ser Gly 225 230 235 240 Ser Thr Gly Leu Pro Lys Gly Ala Met Tyr Thr Glu Arg Met Leu Cys 245 250 255 Lys Leu Trp Thr Thr Glu Leu Met Pro Asp Phe Pro Asp Thr Pro Val 260 265 270 Ile Asn Val Asn Phe Met Pro Leu Asn His Leu Gly Gly Arg Ile Pro 275 280 285 Leu Ser Thr Ala Phe Gln Ala Gly Gly Thr Ser Tyr Phe Val Pro Glu 290 295 300 Ser Asp Leu Ser Thr Leu Phe Asp Asp Trp Asn Leu Val Arg Pro Thr 305 310 315 320 Glu Met Gly Leu Val Pro Arg Val Ala Glu Met Leu Tyr Gln Arg Tyr 325 330 335 Gln Ser Ala Val Asp Arg Leu Asp Ala Ser Gly Ala Glu Ser Pro Glu 340 345 350 Ala Gln Ala Gln Ala Glu Leu Arg Glu Gln Val Leu Gly Gly Arg Val 355 360 365 Val Thr Ala Phe Cys Gly Thr Ala Pro Leu Ala Ala Glu Met Arg Ala 370 375 380 Phe Ile Glu Thr Cys Leu Asp Val His Val Leu Asp Gly Tyr Gly Leu 385 390 395 400 Thr Glu Val Gly Met Val Thr Lys Asp Gly Trp Ile Thr Gln Pro Pro 405 410 415 Val Leu Asp Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe Arg 420 425 430 Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Leu Thr 435 440 445 Gly Thr Pro Gly Tyr Phe Lys Arg Pro Asp Val Thr Ala Asn Ala Phe 450 455 460 Asp Ala Asp Gly Tyr Tyr Arg Thr Gly Asp Val Met Ala Glu Leu Ala 465 470 475 480 Pro Gly Arg Leu Ala Tyr Val Asp Arg Arg Asn Asn Val Leu Lys Leu 485 490 495 Ala Gln Gly Glu Phe Val Ala Val Ala Arg Leu Glu Ala Val Phe Ser 500 505 510 Ser Ala Ala Leu Val Arg Gln Ile Phe Val Tyr Gly Asn Ser Glu Arg 515 520 525 Pro Tyr Leu Leu Ala Val Val Val Pro Thr Asp Asp Ala Ala Arg Arg 530 535 540 Phe Ala Gly Asp Ala Asp Gly Leu Lys Ala Ala Leu Gly Glu Ser Leu 545 550 555 560 Arg Gln Thr Ala Lys Leu Ala Glu Leu Gln Ser Tyr Glu Val Pro Val 565 570 575 Asp Phe Leu Val Glu Thr Glu Arg Phe Ser Glu Asp Asn Gly Leu Leu 580 585 590 Ser Gly Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Glu Arg Tyr Gly 595 600 605 Thr Arg Leu Glu Glu Leu Tyr Ala Glu Leu Ala Glu Asn Arg Val Thr 610 615 620 Glu Leu Arg Ala Leu Arg Glu Gly Ala Ala Asp Arg Pro Val Ile Val 625 630 635 640 Thr Leu Thr Arg Ala Ala Glu Ala Leu Leu Gly Leu Ala Gly Gly Pro 645 650 655 Pro Ser Pro Asp Ala Leu Phe Ile Asp Leu Gly Gly Asp Ser Leu Ser 660 665 670 Ala Leu Thr Phe Ser Asn Leu Leu Arg Asp Ile Phe Asp Val Glu Val 675 680 685 Pro Val Gly Met Ile Thr Gly Pro Ala Ala Asp Leu Gly Gln Leu Ala 690 695 700 Lys Tyr Val Glu Ala Glu Arg Glu Ser Ala Ser Arg Arg Pro Thr Phe 705 710 715 720 Ala Thr Val His Gly Arg Gly Ala Thr Gln Val Arg Ala Ala Asp Leu 725 730 735 Thr Leu Asp Lys Phe Ile Asp Ala Thr Thr Leu Ala Asp Ala Trp Ala 740 745 750 Leu Pro Arg Ala Thr Gly Thr Pro His Thr Val Leu Leu Thr Gly Ala 755 760 765 Asn Gly Tyr Leu Gly Arg Phe Leu Leu Leu Glu Trp Leu Glu Arg Val 770 775 780 Ala Gln Thr Gly Gly Arg Ile Ile Ser Ile Ile Arg Ala Ala Asp Thr 785 790 795 800 Ala Ala Ala Ala Lys Arg Leu Glu Ser Val Phe Asp Ser Gly Asp Pro 805 810 815 Gln Leu Leu Glu Arg Phe Arg Ala Leu Ala Ala Asp His Leu Glu Val 820 825 830 Ile Ile Gly Asp Ile Gly Glu Pro Lys Leu Gly Leu Ser Gln Ala Asn 835 840 845 Trp Glu Arg Leu Ala Gln Ser Val Asp Leu Ile Val His Pro Ala Ala 850 855 860 Leu Val Asn His Val Leu Pro Tyr Asp Gln Leu Phe Gly Pro Asn Val 865 870 875 880 Val Gly Thr Ala Glu Leu Ile Arg Leu Ala Leu Thr Thr Arg Ile Lys 885 890 895 Pro Val Thr Tyr Met Ser Thr Val Ala Val Ala Leu Ser Val Asp Pro 900 905 910 Ala Thr Phe Ala Glu Asp Gly Asp Ile Arg Thr Val Ser Ala Leu Arg 915 920 925 Pro Val Asp Asp Ser Tyr Ala Asn Gly Tyr Ala Asn Ser Lys Trp Ala 930 935 940 Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys Gly Leu Pro Val 945 950 955 960 Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Ser Arg Tyr Ala Gly 965 970 975 Gln Leu Asn Val Pro Asp Ala Phe Thr Arg Leu Leu Phe Ser Leu Leu 980 985 990 Ile Thr Gly Ile Ala Pro Ala Ser Phe Tyr Gln Thr Asp Pro His Gly 995 1000 1005 Asn Arg Ala Val Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Val 1010 1015 1020 Ala Glu Ala Val Ala Thr Leu Gly Glu Gln Ile Ala Thr Ala Ala 1025 1030 1035 Gly Ala Ser Gly Ile Tyr Arg Ser Phe Asp Val Met Asn Pro His 1040 1045 1050 Asp Asp Gly Val Ser Leu Asp Val Phe Val Asp Trp Leu Ile Ala 1055 1060 1065 Ala Gly His Asp Ile Gly Arg Ile Asp Asp Tyr Asp Glu Trp Leu 1070 1075 1080 Ser Arg Phe Thr Thr Ala Ile Arg Ala Leu Pro Glu Arg Gln Arg 1085 1090 1095 Ala His Ser Val Leu Pro Leu Leu Asp Ala Tyr Arg Lys Pro Glu 1100 1105 1110 Thr Pro Leu Arg Gly Ala Pro Ala Pro Thr Asp Val Phe Arg Gly 1115 1120 1125 Ala Val Gln Asp Ala Lys Ile Gly Ala Glu Gln Asp Ile Pro His 1130 1135 1140 Leu Ser Ala Ala Leu Ile Asp Lys Tyr Val Ala Asp Leu Ser Leu 1145 1150 1155 Leu Gly Leu Tyr Asn Gly Ala 1160 1165 <210> 251 <211> 1163 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium litorale <400> 251 Met Pro Thr Asp Thr Arg Glu Ala Arg Phe Glu Gln Arg Val Ala Asp 1 5 10 15 Leu Ala Ala Asn Asp Ala Gln Phe Ala Ala Ala Thr Pro Asp Pro Asp 20 25 30 Ile Thr Ala Ala Ala Asp Gln Pro Gly Leu Arg Leu Pro Ala Ile Ile 35 40 45 Lys Thr Val Phe Asp Gly Tyr Ala Asp Arg Pro Ala Val Gly Gln Arg 50 55 60 Thr Val Arg Phe Thr Glu Asp Pro Val Thr Gly Arg Thr Thr Ala Glu 65 70 75 80 Leu Leu Pro Ala Phe Glu Thr Ile Thr Tyr Gln Gln Leu Trp Gln Arg 85 90 95 Val Gln Ala Val Ala Gly Ala Trp Ala Asp Asn Pro Val Arg Pro Gly 100 105 110 Asp Arg Val Ala Val Leu Gly Phe Thr Ser Val Asp Tyr Thr Thr Ile 115 120 125 Asp Leu Ala Leu Val Leu Leu Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ser Ala Val Asp Ser Leu Ser Pro Ile Ile Ala Glu Thr Glu Pro 145 150 155 160 Ala Leu Ile Ala Ser Ser Ile Asp Tyr Val Ala Asp Ala Val Glu Leu 165 170 175 Ala Leu Arg Gly Pro Glu Pro Lys Arg Leu Val Val Phe Asp Tyr Arg 180 185 190 Pro Glu Ile Asp Asp Gln Arg Asp Ala Leu Ala Ala Ala Arg Thr Arg 195 200 205 Leu Ala Gly Thr Ala Val Ser Val Thr Thr Leu Ala Asp Asp Ile Ala 210 215 220 Gly Ala Pro Ser Thr Pro Thr Val Leu Arg Asp Thr Asp Glu Asp Asp 225 230 235 240 Pro Leu Thr Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys 245 250 255 Gly Ala Met Tyr Pro Ala His Lys Val Ala Asp Met Trp Arg Ala Ala 260 265 270 Ala Ala His Trp Asp Glu Lys His Gly Ala Phe Pro Ala Ile Val Leu 275 280 285 Ser Phe Met Pro Met Ser His Val Met Gly Arg Gly Ala Leu Tyr Gly 290 295 300 Ala Leu Ser Thr Gly Gly Thr Val Tyr Phe Ala Ala Arg Pro Asp Leu 305 310 315 320 Ser Thr Phe Leu Glu Asp Leu Ala Leu Thr Arg Pro Thr Gln Leu Asn 325 330 335 Leu Val Pro Arg Val Trp Asp Met Ile His Gln Glu Val Gln Ser Glu 340 345 350 Leu Asp Arg Arg Ala Gly Thr Glu Arg Ala Gln Val Leu Ala Glu Lys 355 360 365 Arg Ser Ser Leu Leu Gly Gly Arg Phe Val Asn Ala Met Thr Gly Ser 370 375 380 Ala Pro Ile Ala Pro Glu Leu Lys Ala Trp Val Glu Asp Phe Leu Asp 385 390 395 400 Met His Leu Val Glu Gly Tyr Gly Ser Thr Glu Ala Gly Ala Val Phe 405 410 415 Val Asp Gly Leu Val Arg Arg Pro Pro Val Thr Asp Tyr Lys Leu Val 420 425 430 Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Leu Pro His Pro Arg 435 440 445 Gly Glu Leu Leu Val Lys Ser Thr Gln Leu Phe Pro Gly Tyr Tyr Lys 450 455 460 Arg Pro Glu Val Thr Ala Glu Met Phe Asp Ala Glu Gly Phe Tyr Arg 465 470 475 480 Thr Gly Asp Ile Val Ala Glu Leu Gly Pro Asp Gln Leu Gln Tyr Val 485 490 495 Asp Arg Arg Asn Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Thr 500 505 510 Val Ser Lys Leu Glu Ala Ala Phe Gly Arg Ser Pro Leu Val His Gln 515 520 525 Ile Tyr Leu Tyr Gly Asn Ser Ala Arg Pro Tyr Leu Leu Ala Val Val 530 535 540 Val Pro Thr Ala Glu Ala Leu Ala Asp His Asp Thr Thr Glu Leu Lys 545 550 555 560 Ala Leu Ile Gly Glu Ser Leu Gln Asp Val Ala Arg Thr Ala Gly Leu 565 570 575 Gln Ser Tyr Glu Ile Pro Arg Asp Phe Leu Ile Glu Ala Thr Pro Phe 580 585 590 Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala Trp Pro 595 600 605 Arg Leu Lys Glu Arg Tyr Gly Pro Ala Leu Glu Gln Leu Tyr Val Asp 610 615 620 Leu Ala Glu Gly Gln Ala Asp Glu Leu Arg Ala Leu Arg Gln Ser Gly 625 630 635 640 Ser Asp Ala Pro Ala Leu Glu Thr Val Thr Arg Ala Ala Gly Ala Leu 645 650 655 Leu Gly Ala Ala Ala Ala Asp Leu Gln Pro Asp Ala His Phe Thr Asp 660 665 670 Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ala Asn Leu Leu Gln 675 680 685 Glu Ile Phe Asp Val Glu Val Pro Val Gly Val Ile Val Ser Pro Ala 690 695 700 Asn Asp Leu Ala Gly Ile Ala Ala Tyr Val Glu Thr Gln Arg Thr Ser 705 710 715 720 Gly Ser Lys Arg Pro Thr Phe Ala Thr Val His Gly Ala Gly Ala Thr 725 730 735 Glu Ala His Ala Arg Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala 740 745 750 Thr Leu Ala Ala Ala Ala Thr Leu Pro Gly Pro Thr Gly Glu Ile Arg 755 760 765 Thr Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala 770 775 780 Leu Glu Trp Leu Glu Arg Met Ser Met Val Asp Gly Lys Val Ile Cys 785 790 795 800 Leu Val Arg Ala Arg Ser Asn Glu Asp Ala Arg Gln Arg Leu Asp Ser 805 810 815 Thr Phe Asp Ser Gly Asp Pro Lys Leu Leu Ala His Tyr Gln Gln Leu 820 825 830 Ala Ala Ala His Leu Glu Val Ile Ala Gly Asp Lys Gly Glu Glu Asn 835 840 845 Leu Gly Leu Asp Pro Ala Thr Trp Gln Arg Leu Ala Asp Thr Val Asp 850 855 860 Leu Ile Val Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Arg 865 870 875 880 Glu Leu Phe Gly Pro Asn Ala Val Gly Thr Ala Glu Leu Ile Arg Ile 885 890 895 Ala Leu Thr Thr Lys Leu Lys Pro Phe Val Tyr Val Ser Thr Ile Gly 900 905 910 Val Gly Ala Gly Ile Ala Ala Gly Gln Phe Val Glu Asp Ala Asp Ile 915 920 925 Arg Thr Ile Ser Ala Thr Arg Ala Val Asp Asp Ser Tyr Ala Asn Gly 930 935 940 Tyr Ser Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala Asn 945 950 955 960 Asp Leu Cys Gly Leu Pro Val Ser Val Phe Arg Cys Asp Met Ile Leu 965 970 975 Ala Asp Thr Thr Tyr Gly Gly Gln Leu Asn Leu Pro Asp Met Phe Thr 980 985 990 Arg Met Met Leu Ser Leu Val Ala Thr Gly Ile Ala Pro Ala Ser Phe 995 1000 1005 Tyr Glu Leu Ala Ala Asp Gly Ser Arg Gln Arg Ala His Tyr Asp 1010 1015 1020 Gly Leu Pro Val Glu Phe Ile Ala Glu Ala Ile Ser Thr Leu Gly 1025 1030 1035 Ala Gln Val Asp Glu Gly Phe Glu Thr Tyr His Val Met Asn Pro 1040 1045 1050 Tyr Asp Asp Gly Ile Gly Leu Asp Glu Phe Val Asp Trp Leu Val 1055 1060 1065 Glu Ala Gly Tyr Pro Ile Gln Arg Ile Asp Asp Tyr Ala Gly Trp 1070 1075 1080 Leu Gln Arg Phe Glu Thr Ala Met Arg Ser Leu Pro Asp Arg Gln 1085 1090 1095 Arg Gln Tyr Ser Leu Leu Pro Leu Leu His Asn Tyr Gln Arg Pro 1100 1105 1110 Glu His Pro Ile Asn Gly Ser Ile Ala Pro Thr Asp Arg Phe Arg 1115 1120 1125 Ala Ala Val Gln Asp Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro 1130 1135 1140 His Val Ser Pro Glu Val Ile Val Lys Tyr Ala Thr Asp Leu Thr 1145 1150 1155 Leu Leu Gly Leu Leu 1160 <210> 252 <211> 1178 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. JS623 <400> 252 Met Phe Thr Asp Ser Arg Glu Asp Arg Leu Ala Arg Arg Val Ala Asp 1 5 10 15 Leu Tyr Ser Thr Asp Ile Gln Phe Val Asp Ala Arg Pro Ile Glu Ala 20 25 30 Leu Ser Ala Ala Ile Glu Gln Pro Gly Leu Arg Leu Pro Arg Ile Met 35 40 45 Ser Thr Val Met Gly Ala Tyr Ala Glu Arg Pro Ala Val Gly Glu Arg 50 55 60 Gly Val Asn Leu Thr Thr Asp Pro Ala Thr Gly Arg Thr Ser Leu Glu 65 70 75 80 Leu Leu Pro Cys Phe Gln Thr Ile Thr Tyr Arg Glu Leu Trp Asp Arg 85 90 95 Val Gly Ala Val Ala Ser Gly Leu Thr Gln Gly Pro Gly Pro Val Gln 100 105 110 Pro Gly Asp Arg Ala Cys Val Leu Gly Phe Ala Ser Ala Asp Tyr Ala 115 120 125 Thr Ile Asp Met Ala Leu Val Leu Leu Gly Ala Val Ser Val Pro Leu 130 135 140 Gln Thr Arg Ala Pro Val Ser Gln Leu Arg Pro Ile Val Thr Glu Thr 145 150 155 160 Glu Pro Arg Val Phe Gly Ser Ser Ile Gly Asp Leu Ala Asn Ala Val 165 170 175 Glu Leu Val Leu Thr Gly Tyr Thr Pro Ala Arg Leu Val Val Phe Asp 180 185 190 Tyr His Pro Asp Val Asp Asp Gln Arg Glu Ala Phe Asp Ala Ala Lys 195 200 205 Thr Arg Leu Ala Glu Ala Gly Ser Pro Val Leu Val Glu Thr Leu Ala 210 215 220 Ala Leu Leu Asp Arg Gly Ala Ser Leu Pro Ala Ala Pro Glu Phe Val 225 230 235 240 Pro Asp Asp Asp Glu Asp Pro Leu Thr Leu Leu Ile Tyr Thr Ser Gly 245 250 255 Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr Pro Glu Arg Leu Val Ala 260 265 270 Asn Phe Trp Arg Arg Ser Arg Trp Asn Trp Gly Ser Ser Val Glu Pro 275 280 285 Leu Ile Thr Leu Ser Phe Met Pro Met Ser His Val Met Gly Arg Gly 290 295 300 Ile Leu Tyr Gly Thr Leu Gly Gln Gly Gly Thr Ala Tyr Phe Thr Ala 305 310 315 320 Arg Ser Asp Leu Ser Thr Leu Phe Glu Asp Leu Ala Leu Val Arg Pro 325 330 335 Thr Glu Leu Asn Phe Val Pro Arg Ile Trp Asp Met Leu Phe Thr Glu 340 345 350 Phe Gln Ser Glu Val Asp Arg Arg Ser Val Asp Gly Val Asp Arg Ala 355 360 365 Val Leu Glu Ala Asp Val Met Ala Glu Gln Ala Gln Asn Leu Leu Gly 370 375 380 Gly Arg Phe Val Ser Ala Met Thr Gly Ser Ala Pro Ile Ser Ala Glu 385 390 395 400 Asn Lys Glu Phe Val Glu Ala Leu Leu Asp Leu His Leu Val Glu Gly 405 410 415 Tyr Gly Ser Thr Glu Ala Gly Ile Ile Tyr Ile Asp Gly Gln Val Arg 420 425 430 Arg Pro Ala Val Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly 435 440 445 Tyr Phe His Thr Asp Gln Pro Phe Pro Arg Gly Glu Leu Leu Val Lys 450 455 460 Thr Gln Asp Leu Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Val Thr Ala 465 470 475 480 Asp Val Phe Asp Pro Asp Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala 485 490 495 Glu Val Asp Pro Asp Gln Leu Val Tyr Leu Asp Arg Arg Asn Asn Val 500 505 510 Leu Lys Leu Ser Gln Gly Glu Phe Val Thr Val Ser Lys Leu Glu Ala 515 520 525 Val Phe Gly Asp Ser Pro Leu Val Arg Gln Ile Tyr Val Tyr Gly Asn 530 535 540 Ser Ala Arg Ser Tyr Val Leu Ala Val Val Val Pro Thr Asp Asp Thr 545 550 555 560 Leu Asn Arg Thr Gly Gly Asp Val Glu Ser Leu Lys Ser Ala Ile Ser 565 570 575 Glu Ser Leu Gln Asn Ile Ala Lys Asp Val Gly Leu Gln Ser Tyr Glu 580 585 590 Ile Pro Arg Asp Phe Ile Ile Glu Thr Thr Pro Phe Thr Leu Glu Asn 595 600 605 Gly Leu Leu Thr Gly Ile Arg Lys Leu Ala Arg Pro Lys Leu Lys Val 610 615 620 His Tyr Gly Asp Arg Leu Glu Gln Leu Tyr Thr Glu Leu Ala Asp Ser 625 630 635 640 Gln Ala Asn Glu Leu Arg Ala Leu Arg Gln Asn Gly Ala Asp Arg Pro 645 650 655 Val Leu Glu Thr Val Ile Arg Ala Ala Gly Ala Val Leu Gly Ala Ala 660 665 670 Ala Ser Asp Leu Glu Pro Asp Ala His Phe Ser Asp Leu Gly Gly Asp 675 680 685 Ser Leu Ser Ala Leu Thr Phe Gly Asn Leu Leu Arg Glu Ile Phe Asp 690 695 700 Ile Asp Val Pro Val Gly Val Ile Val Ser Pro Ala Ser Asp Leu Arg 705 710 715 720 Ser Ile Ala Gly Tyr Ile Glu Ala Glu Arg Arg Pro Gly Ala Lys Arg 725 730 735 Pro Thr Phe Ala Ser Val His Asp Arg Ser Asn Lys Pro Ile Thr Glu 740 745 750 Val Leu Ala Ser Asp Leu Thr Leu Asp Lys Phe Ile Asp Ala Lys Thr 755 760 765 Leu Ala Ala Ala Ser Thr Leu Pro Ser Pro Ser Ala Glu Val Arg Thr 770 775 780 Val Leu Leu Thr Gly Ala Thr Gly Phe Leu Gly Arg Tyr Leu Ala Leu 785 790 795 800 Glu Trp Leu Glu Arg Met Asn Leu Val Gly Gly Lys Leu Ile Cys Leu 805 810 815 Val Arg Ala Lys Asp Asp Val Ala Ala Arg Asp Arg Leu Asp Lys Thr 820 825 830 Phe Asp Ser Gly Asp Pro Glu Leu Leu Arg His Tyr Arg Glu Leu Ala 835 840 845 Ala Gly His Leu Glu Val Ile Ala Gly Asp Lys Gly Glu Glu Asn Leu 850 855 860 Gly Leu Asp Gln Gln Thr Trp Gln Arg Leu Ala Asp Ile Val Asp Leu 865 870 875 880 Ile Val Asp Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Glu 885 890 895 Leu Phe Gly Pro Asn Ala Leu Gly Thr Ala Glu Leu Ile Arg Ile Ala 900 905 910 Leu Thr Thr Lys Gln Lys Pro Tyr Thr Tyr Val Ser Thr Ile Gly Val 915 920 925 Gly Asp Gln Ile Glu Pro Ser Ser Phe Thr Glu Asp Ala Asp Val Arg 930 935 940 Val Met Ser Pro Thr Arg Ala Ile Asn Glu Gly Tyr Ala Asn Gly Tyr 945 950 955 960 Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala Asn Asp 965 970 975 Leu Cys Gly Leu Pro Val Ala Val Phe Arg Cys Asp Met Ile Leu Ala 980 985 990 Asp Thr Ala Tyr Ala Gly Gln Leu Asn Val Pro Asp Met Phe Thr Arg 995 1000 1005 Leu Leu Leu Ser Val Val Ala Thr Gly Ile Gly Pro Gly Ser Phe 1010 1015 1020 Tyr Glu Leu Asp Ala Asp Gly Asn Arg Gln Arg Ala His Phe Asp 1025 1030 1035 Gly Leu Pro Val Gly Phe Ile Ala Asp Ala Ile Ser Thr Leu Gly 1040 1045 1050 Ala Gln Val Val Asp Gly Tyr Glu Thr Tyr His Val Met Asn Pro 1055 1060 1065 Tyr Asp Asp Gly Ile Gly Leu Asp Glu Tyr Val Asp Trp Leu Thr 1070 1075 1080 Asp Ala Gly Tyr Pro Ile Gln Arg Ile Ser Gly Tyr Asp Ala Trp 1085 1090 1095 Leu Gln Arg Phe Asp Thr Ala Leu Arg Ala Leu Pro Asp Lys Gln 1100 1105 1110 Arg Gln Ala Ser Leu Leu Pro Leu Leu His Asn Tyr Gln Arg Pro 1115 1120 1125 Glu Lys Pro Ile Arg Gly Ser Met Ala Pro Thr Asp Arg Phe Arg 1130 1135 1140 Ala Ala Val Gln Asp Ala Lys Ile Gly Pro Asp Lys Asp Ile Pro 1145 1150 1155 His Val Thr Ala Pro Met Ile Val Lys Tyr Ile Thr Asp Leu Gln 1160 1165 1170 Leu Leu Gly Leu Leu 1175 <210> 253 <211> 1404 <212> PRT <213> Artificial Sequence <220> <223> Candida albicans SC5314 <400> 253 Met Thr Asp Phe Trp Leu Asn Tyr Leu Asp Asn Pro Thr Leu Ser Val 1 5 10 15 Leu Pro His Asp Phe Leu Lys Pro Ala Asn Asn Lys Ser Val Glu Gly 20 25 30 Thr Tyr Thr Phe Asn Ile Asp Asn Gly Ser Thr Asp Phe Lys Phe Gly 35 40 45 Leu Ala Val Phe Ala Ala Leu Val Tyr Arg Leu Thr Gly Asp Glu Asp 50 55 60 Ile Val Ile Ala Thr Asp Glu Ser Ala Asn Thr Pro Glu Phe Ile Val 65 70 75 80 Arg Leu Asn Leu Thr Pro Glu Leu Thr Phe Gln Glu Leu Val Ser Lys 85 90 95 Ile Thr Lys Glu Tyr Glu Asn Ser Ile Ser Gln Ile Asn Tyr Lys Ala 100 105 110 Leu Ser Glu Val Ser His Arg Ile Lys Glu Ala Lys Gly Leu Asp Glu 115 120 125 Asn Pro Gly Leu Phe Arg Leu Ser Tyr Gln His Ala His Ser Asn Gln 130 135 140 Gln Leu Asn Thr Thr Val Glu Gly Ser Ile Arg Asp Leu Ala Ile Tyr 145 150 155 160 Thr Asp Gly Thr Lys Phe Thr Ile Tyr Tyr Asn Ala Leu Leu Tyr Ser 165 170 175 His Glu Arg Ile Val Ile Phe Gly Glu Gln Phe Ala Gln Tyr Leu Thr 180 185 190 Thr Val Ser Asn Asp Thr Asn Thr Val Ile Thr Lys Val Asn Leu Ile 195 200 205 Thr Asp Phe Gln Lys Lys Asn Leu Pro Asp Pro Thr Ile Asp Leu Asp 210 215 220 Trp Ser Gly Tyr Arg Gly Ala Ile Gln Asp Ile Phe Met Asp Asn Ala 225 230 235 240 Asn Lys His Pro Asp Arg Thr Cys Val Val Glu Thr Glu Ser Phe Leu 245 250 255 Asp Ser Asn Ser Lys Thr Arg Ser Phe Thr Tyr Gln Gln Ile Asn Gln 260 265 270 Ala Ser Asn Val Val Gly Asn Tyr Leu Lys Glu Thr Gly Ile Lys Lys 275 280 285 Gly Asp Ile Val Met Ile Tyr Ala Tyr Arg Gly Val Asp Leu Met Ile 290 295 300 Ala Val Met Gly Val Leu Lys Ala Gly Ala Thr Phe Ser Val Ile Asp 305 310 315 320 Pro Ala Tyr Pro Pro Ala Arg Gln Asn Ile Tyr Leu Ser Val Ala Lys 325 330 335 Pro Lys Gly Leu Ile Gly Leu Glu Lys Ala Gly Thr Leu Asp Gln Leu 340 345 350 Val Val Asp Tyr Ile Ser Asn Glu Leu Asp Val Ile Ser Thr Ile Pro 355 360 365 Gln Leu Lys Val Gln Asp Asp Gly Thr Leu Val Gly Gly Lys His Glu 370 375 380 Gly Ala Asp Asn Asp Cys Leu Asn Asp Tyr Gln Lys Phe Lys Asp Gln 385 390 395 400 Pro Ala Gly Val Ile Val Gly Pro Asp Ser Asn Pro Thr Leu Ser Phe 405 410 415 Thr Ser Gly Ser Glu Gly Ile Pro Lys Gly Val Leu Gly Arg His Tyr 420 425 430 Ser Leu Ala Tyr Tyr Phe Pro Trp Met Ala Lys Arg Phe Gly Leu Ser 435 440 445 Glu Lys Asp Lys Phe Thr Met Leu Ser Gly Ile Ala His Asp Pro Ile 450 455 460 Gln Arg Asp Met Phe Thr Pro Leu Phe Leu Gly Ala Gln Leu Leu Val 465 470 475 480 Pro Thr Ala Asp Asp Ile Gly Thr Pro Gly Lys Leu Ala Asp Trp Met 485 490 495 Ala Lys Tyr Gly Ala Thr Val Thr His Leu Thr Pro Ala Met Gly Gln 500 505 510 Leu Leu Ser Ala Gln Ala Thr Thr Ala Ile Pro Ser Leu His His Ala 515 520 525 Phe Phe Val Gly Asp Ile Leu Thr Lys Arg Asp Cys Leu Arg Leu Gln 530 535 540 Ser Leu Ala Glu Asn Val Phe Ile Val Asn Met Tyr Gly Thr Thr Glu 545 550 555 560 Thr Gln Arg Ser Val Ser Tyr Phe Glu Ile Lys Ser Arg Lys Ala Asp 565 570 575 Pro Thr Tyr Leu Lys Asn Leu Lys Asp Val Met Pro Ala Gly Thr Gly 580 585 590 Met His Asn Val Gln Leu Leu Val Val Asn Arg Asn Asp Arg Ser Gln 595 600 605 Thr Cys Gly Val Gly Glu Val Gly Glu Ile Tyr Val Arg Ala Ala Gly 610 615 620 Leu Ala Glu Gly Tyr Arg Gly Leu Pro Asp Leu Asn Ala Ala Lys Phe 625 630 635 640 Ile Thr Asn Trp Tyr Val Asn Pro Asp Lys Trp Ile Glu Gln Asp Glu 645 650 655 Ala Asn Lys Lys Ser Ser Glu Thr Trp Arg Glu His Gly Trp Leu Lys 660 665 670 Pro Arg Asp Arg Met Tyr Arg Ser Gly Asp Leu Gly Arg Tyr Leu Pro 675 680 685 Asp Gly Asn Val Glu Cys Cys Gly Arg Ala Asp Asp Gln Val Lys Ile 690 695 700 Arg Gly Phe Arg Ile Glu Leu Gly Glu Ile Asp Thr His Leu Ser Gln 705 710 715 720 His Pro Leu Val Arg Glu Asn Val Thr Leu Val Arg Arg Asp Lys Asn 725 730 735 Glu Glu Pro Thr Leu Ile Ser Tyr Ile Val Pro Lys Asp Ser Pro Glu 740 745 750 Leu Lys Thr Phe Lys Ala Asp Val Asp Asp Ser Ile Glu Glu Ala Asn 755 760 765 Asp Pro Ile Val Lys Gly Leu Val Ala Tyr Arg Glu Leu Ile Lys Asp 770 775 780 Ile Lys Gly Tyr Leu Lys Lys Lys Leu Ala Ser Tyr Ala Ile Pro Thr 785 790 795 800 Ile Ile Val Pro Leu Val Lys Leu Pro Leu Asn Pro Asn Gly Lys Val 805 810 815 Asp Lys Pro Lys Leu Pro Phe Pro Asp Thr Ala Gln Leu Ala Ala Val 820 825 830 Ala Lys Leu Ser Val Ser Ser His Asp Ala Gln Ala Ala Glu Glu Glu 835 840 845 Asn Leu Thr Lys Leu Glu Glu Gln Ile Arg Asp Leu Trp Leu Asp Val 850 855 860 Leu Pro Asn Arg Pro Ala Thr Ile Ser Lys Asp Asp Ser Phe Phe Asp 865 870 875 880 Leu Gly Gly His Ser Ile Leu Gly Thr Arg Met Ile Phe Glu Leu Arg 885 890 895 Lys Lys Leu Asn Val Glu Ile Pro Leu Gly Val Ile Phe Lys Asn Pro 900 905 910 Thr Val Glu Gln Phe Ala Lys Glu Val Glu Lys Val Ile Lys Gly Gly 915 920 925 Gln Asp Phe Gln Leu Ala Asp Glu Gly Lys Thr Ile Gln Glu Glu Asn 930 935 940 Lys Asp Val Ala Asp Ser Gln Ser Glu Asn Leu Asn Tyr Ala Glu Asp 945 950 955 960 Ala Lys Glu Leu Ser Lys Ser Ala Leu Leu Glu Ser Tyr Ser Ser Leu 965 970 975 Lys Gln Leu Pro Ser Gly Ser Ile Asn Val Phe Val Thr Gly Ala Thr 980 985 990 Gly Phe Leu Gly Ser Phe Ile Val Arg Asp Leu Leu Thr Ala Arg Asn 995 1000 1005 Lys Asn Leu Asp Ile Lys Val Tyr Ala His Val Arg Ala Ser Ser 1010 1015 1020 Lys Glu Ala Gly Leu Gln Arg Leu Arg Gln Thr Gly Ile Thr Tyr 1025 1030 1035 Gly Ile Trp Asp Glu Asn Trp Ala Glu Lys Ile Glu Ile Val Leu 1040 1045 1050 Gly Asp Leu Ser Lys Glu Lys Phe Gly Leu Asp Asn Ser Gln Trp 1055 1060 1065 Leu Asp Leu Thr Asn Asn Ile Asp Val Ile Ile His Asn Gly Ala 1070 1075 1080 Phe Val His Trp Val Tyr Pro Tyr Ser Gln Leu Arg Asp Ala Asn 1085 1090 1095 Val Ile Gly Thr Ile Asn Val Leu Asn Met Ala Gly Glu Gly Lys 1100 1105 1110 Ala Lys Phe Phe Ser Phe Val Ser Ser Thr Ser Ala Leu Asp Thr 1115 1120 1125 Asp Tyr Phe Val Asn Leu Ser Asp Glu Leu Leu Ala Gln Gly Lys 1130 1135 1140 Asn Gly Ile Ser Glu Ala Asp Asp Leu Gln Gly Ser Ala Lys Gly 1145 1150 1155 Leu Gly Asn Gly Tyr Gly Gln Ser Lys Trp Ala Ala Glu Tyr Ile 1160 1165 1170 Ile Arg Arg Ala Gly Glu Arg Gly Leu Lys Gly Cys Ile Thr Arg 1175 1180 1185 Pro Gly Tyr Val Thr Gly Phe Ser Lys Thr Gly Ala Ser Asn Thr 1190 1195 1200 Asp Asp Phe Leu Leu Arg Met Leu Lys Gly Ser Ala Glu Leu Gly 1205 1210 1215 Leu Tyr Pro Asp Ile Thr Asn Asn Val Asn Met Val Pro Val Asp 1220 1225 1230 His Val Ala Arg Val Val Thr Ala Thr Ala Leu Asn Pro Pro Ser 1235 1240 1245 Ser Glu Glu Leu Thr Val Ala His Val Thr Gly His Pro Arg Ile 1250 1255 1260 Arg Phe Asn Asp Phe Leu Gly Cys Leu Lys Ala Tyr Gly Tyr Glu 1265 1270 1275 Ile Asn Pro Ala Asp Tyr Pro Val Trp Thr Ser Ala Leu Glu Lys 1280 1285 1290 Phe Val Ile Glu Glu Ser Lys Glu Ser Ala Leu Phe Pro Leu Leu 1295 1300 1305 His Phe Val Leu Asp Asn Leu Pro Gln Asp Thr Lys Ala Pro Glu 1310 1315 1320 Leu Asp Asp Ser Asn Val Ala Lys Ser Leu Lys Gln Asp Ser Lys 1325 1330 1335 Tyr Thr Gly Glu Asp Phe Ser Ala Gly Lys Gly Val Asp Leu Asp 1340 1345 1350 Gln Thr Gly Val Tyr Ile Ser Tyr Leu Ile Lys Ile Gly Phe Leu 1355 1360 1365 Pro Lys Pro Thr Gly Thr Gly Glu Lys Lys Leu Pro Glu Val Glu 1370 1375 1380 Ile Ser Asp Glu Ser Leu Lys Leu Ile Ser Gly Gly Ala Gly Ala 1385 1390 1395 Arg Gly Ser Ala Ala Lys 1400 <210> 254 <211> 1168 <212> PRT <213> Artificial Sequence <220> <223> Mycobacterium sp. JS623 <400> 254 Met Ser Thr Val Ser Arg Glu Glu Arg Leu Ala Arg Arg Ile Ser Asp 1 5 10 15 Leu Tyr Ala Thr Asp Gln Gln Phe Ala Asp Ala Arg Pro Ser Glu Ala 20 25 30 Val Ala His Ala Ile Glu Ser Pro Ala Leu Arg Leu Pro Gln Ile Ile 35 40 45 Gln Thr Val Ile Asp Gly Tyr Ala Glu Arg Pro Ala Leu Gly Gln Arg 50 55 60 Ala Val Glu Phe Val Thr Asp Pro Thr Thr Gly Arg Thr Ser Ala Ala 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Arg Glu Leu Ser Glu Arg 85 90 95 Val Asp Ala Val Ala Thr Ala Leu Thr Gln Asn Pro Val Arg Pro Gly 100 105 110 Asp Arg Val Ala Ile Leu Gly Phe Thr Ser Ile Asp Tyr Thr Thr Val 115 120 125 Asp Met Ala Leu Leu Arg Ala Gly Ala Val Ser Val Pro Leu Gln Thr 130 135 140 Ser Ala Pro Val Ala Gln Leu Arg Pro Ile Ala Ala Glu Thr Glu Pro 145 150 155 160 Val Ala Ile Leu Ser Ser Val Asp Phe Leu Asp Asp Ala Val Glu Leu 165 170 175 Met Leu Thr Gly His Leu Pro Glu Arg Leu Val Val Phe Asp Tyr His 180 185 190 Ala Glu Val Asp Asp His Arg Glu Ala Leu Ala Ser Ala Thr Ala Arg 195 200 205 Leu Ala Glu Thr Pro Val Val Val Glu Thr Leu Ala Glu Val Leu Ala 210 215 220 Arg Gly Asn Ala Leu Pro Ala His Pro Ala Phe Asp Ala Gly Asp Asp 225 230 235 240 Asn Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys 245 250 255 Gly Ala Met Tyr Leu Ala Lys Ala Val Ala Asn Ser Trp Arg Arg Ser 260 265 270 Ser Met Ala Met Trp Gly Asn Glu Gly Ala Thr Pro Ser Ile Thr Leu 275 280 285 Asn Phe Met Pro Met Ser His Met Met Gly Arg Gly Ile Leu Tyr Ala 290 295 300 Thr Leu Gly Ala Gly Gly Thr Ala Tyr Phe Val Ala Arg Ser Asp Leu 305 310 315 320 Ser Thr Phe Phe Asp Asp Leu Ser Leu Val Arg Pro Thr Gln Leu Ser 325 330 335 Phe Val Pro Arg Ile Trp Asp Met Val Phe Ala Glu Tyr Gln Ser Glu 340 345 350 Val Asp Arg Arg Ser Ala Asp Gly Gly Asp Arg Trp Ala Val Glu Ala 355 360 365 Asp Val Leu Ala Asp Leu Arg Gln Asn Leu Leu Gly Gly Arg Phe Ile 370 375 380 Ser Ala Met Thr Gly Ser Ala Pro Ile Ser Ser Glu Met Arg Thr Phe 385 390 395 400 Val Glu Ser Leu Leu Asp Ile His Leu Thr Asp Gly Tyr Gly Ser Thr 405 410 415 Glu Ala Gly Ala Val Phe Val Asp Gly Gln Val Gln Arg Pro Pro Val 420 425 430 Ile Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe Ser Thr 435 440 445 Asp Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Glu Thr Met 450 455 460 Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Ile Thr Ala Asp Val Phe Asp 465 470 475 480 Ala Asp Gly Tyr Tyr Arg Thr Gly Asp Val Val Ala Glu Leu Gly Pro 485 490 495 Asp Gln Leu Gln Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ser 500 505 510 Gln Gly Glu Phe Val Thr Val Ala Lys Leu Glu Ala Val Phe Val Asp 515 520 525 Ser Pro Leu Ile Arg Gln Ile Phe Val Tyr Gly Asn Ser Ala Arg Ser 530 535 540 Tyr Leu Leu Ala Val Ile Val Pro Thr Glu Glu Ala Leu Ala Arg His 545 550 555 560 Asp Ala Ala Glu Leu Lys Gln Leu Ile Thr Glu Ser Leu Gln Asp Val 565 570 575 Ala Lys Ala Thr Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile 580 585 590 Ile Glu Thr Thr Pro Phe Thr Leu Glu Asn Gly Leu Leu Thr Gly Ile 595 600 605 Arg Lys Leu Ala Arg Pro Lys Leu Lys Glu Phe Tyr Gly Glu Arg Leu 610 615 620 Glu Gln Leu Tyr Thr Asp Leu Ala Asp Ser Gln Ala Asn Glu Leu Arg 625 630 635 640 Glu Leu Arg Gln His Gly Ala Asp Arg Pro Val Leu Glu Thr Ile Ser 645 650 655 Arg Ala Ala Gly Ala Leu Leu Gly Ala Ala Ala Ser Glu Leu Gln Pro 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Ala Asn Leu Leu His Glu Ile Phe Glu Ile Asp Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Asn Asp Leu Ala Ala Leu Ala Ala Tyr Ile 705 710 715 720 Glu Ala Glu Arg Gln Pro Gly Ser Lys Arg Pro Thr Phe Ala Ser Val 725 730 735 His Gly Arg Asp Ala Thr Glu Val Tyr Ala Asn Asp Leu Thr Leu Asp 740 745 750 Lys Phe Ile Asp Ala Lys Thr Leu Ala Ala Ala Ser Ser Leu Pro Gly 755 760 765 Pro Ser Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Met Val 785 790 795 800 Asp Gly Lys Val Ile Ala Leu Val Arg Ala Lys Asp Asp Asp Ala Ala 805 810 815 Arg Glu Arg Leu Asp Lys Thr Phe Asp Ser Gly Asp Pro Glu Leu Leu 820 825 830 Arg His Tyr His Glu Leu Ala Ala Asp His Leu Glu Val Ile Ala Gly 835 840 845 Asp Lys Gly Glu Ala Asn Leu Gly Leu Asp Gln Gln Thr Trp Gln Arg 850 855 860 Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro Ala Ala Leu Val Asn 865 870 875 880 His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Ala Leu Gly Thr 885 890 895 Ala Glu Leu Ile Arg Ile Ala Leu Thr Thr Lys Gln Lys Pro Phe Val 900 905 910 Tyr Val Ser Thr Ile Gly Val Gly Ala Gly Ile Glu Pro Gly Gln Phe 915 920 925 Thr Glu Asp Gly Asp Val Arg Val Tyr Ser Ala Thr Arg Lys Val Asp 930 935 940 Asp Thr Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val 945 950 955 960 Leu Leu Arg Glu Ala His Asp Leu Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Leu Met Leu Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Asp Ser Phe Tyr Glu Val Asp Ala Asn Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Ile Ala Glu Ala 1025 1030 1035 Ile Ser Thr Leu Gly Ala Gln Val Val Asp Gly Phe Glu Thr Tyr 1040 1045 1050 His Val Met Asn Pro Tyr Asp Asp Gly Ile Gly Leu Asp Glu Tyr 1055 1060 1065 Val Asp Trp Leu Ile Glu Ala Gly Phe Pro Val Glu Arg Val Gly 1070 1075 1080 Asp Tyr Thr Thr Trp Leu Gln Arg Phe Asp Thr Ala Val Arg Ala 1085 1090 1095 Leu Pro Glu Arg Gln Arg Gln Ala Ser Leu Leu Pro Leu Leu His 1100 1105 1110 Asn Tyr Gln Arg Pro Glu Thr Pro Ile Arg Gly Ser Ile Ala Pro 1115 1120 1125 Thr Asp Arg Phe Arg Ala Ala Val Gln Asp Ala Lys Ile Gly Pro 1130 1135 1140 Asp Lys Asp Ile Pro His Val Thr Arg Asp Val Ile Val Lys Tyr 1145 1150 1155 Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 <210> 255 <211> 1150 <212> PRT <213> Artificial Sequence <220> <223> Nocardia brasiliensis ATCC 700358 <400> 255 Met Phe Ala Glu Asp Glu Gln Val Lys Ala Ala Val Pro Asp Gln Glu 1 5 10 15 Val Val Glu Ala Ile Arg Ala Pro Gly Leu Arg Leu Ala Gln Ile Met 20 25 30 Ala Thr Val Met Glu Arg Tyr Ala Asp Arg Pro Ala Val Gly Gln Arg 35 40 45 Ala Ser Glu Pro Val Thr Glu Ser Gly Arg Thr Thr Phe Arg Leu Leu 50 55 60 Pro Glu Phe Glu Thr Leu Thr Tyr Arg Glu Leu Trp Ala Arg Val Arg 65 70 75 80 Ala Val Ala Ala Ala Trp His Gly Asp Ala Glu Arg Pro Leu Arg Ala 85 90 95 Gly Asp Phe Val Ala Leu Leu Gly Phe Ala Gly Ile Asp Tyr Gly Thr 100 105 110 Leu Asp Leu Ala Asn Ile His Leu Gly Leu Val Thr Val Pro Leu Gln 115 120 125 Ser Gly Ala Thr Ala Pro Gln Leu Ala Ala Ile Leu Ala Glu Thr Thr 130 135 140 Pro Arg Val Leu Ala Ala Thr Pro Asp His Leu Asp Ile Ala Val Glu 145 150 155 160 Leu Leu Thr Gly Gly Ala Ser Pro Glu Arg Leu Val Val Phe Asp Tyr 165 170 175 Arg Pro Ala Asp Asp Asp His Arg Ala Ala Leu Glu Ser Ala Arg Arg 180 185 190 Arg Leu Ser Asp Ala Gly Ser Ala Val Val Val Glu Thr Leu Asp Ala 195 200 205 Val Arg Ala Arg Gly Ser Glu Leu Pro Ala Ala Pro Leu Phe Val Pro 210 215 220 Ala Ala Asp Glu Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 225 230 235 240 Thr Gly Thr Pro Lys Gly Ala Met Tyr Thr Glu Arg Leu Asn Arg Thr 245 250 255 Thr Trp Leu Ser Gly Ala Lys Gly Val Gly Leu Thr Leu Gly Tyr Met 260 265 270 Pro Met Ser His Ile Ala Gly Arg Ala Ser Phe Ala Gly Val Leu Ala 275 280 285 Arg Gly Gly Thr Val Tyr Phe Thr Ala Arg Ser Asp Met Ser Thr Leu 290 295 300 Phe Glu Asp Leu Ala Leu Val Arg Pro Thr Glu Met Phe Phe Val Pro 305 310 315 320 Arg Val Cys Asp Met Ile Phe Gln Arg Tyr Gln Ala Glu Leu Ser Arg 325 330 335 Arg Ala Pro Ala Ala Ala Ala Ser Pro Glu Leu Glu Gln Glu Leu Lys 340 345 350 Thr Glu Leu Arg Leu Ser Ala Val Gly Asp Arg Leu Leu Gly Ala Ile 355 360 365 Ala Gly Ser Ala Pro Leu Ser Ala Glu Met Arg Glu Phe Met Glu Ser 370 375 380 Leu Leu Asp Leu Glu Leu His Asp Gly Tyr Gly Ser Thr Glu Ala Gly 385 390 395 400 Ile Gly Val Leu Gln Asp Asn Ile Val Gln Arg Pro Pro Val Ile Asp 405 410 415 Tyr Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Gln 420 425 430 Pro His Pro Arg Gly Glu Leu Leu Leu Lys Thr Glu Gly Met Ile Pro 435 440 445 Gly Tyr Phe Arg Arg Pro Glu Val Thr Ala Glu Ile Phe Asp Glu Asp 450 455 460 Gly Phe Tyr Arg Thr Gly Asp Ile Val Ala Glu Leu Glu Pro Asp Arg 465 470 475 480 Leu Ile Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly 485 490 495 Glu Phe Val Thr Val Ala His Leu Glu Ala Val Phe Ala Thr Ser Pro 500 505 510 Leu Ile Arg Gln Ile Tyr Ile Tyr Gly Asn Ser Glu Arg Ser Phe Leu 515 520 525 Leu Ala Val Ile Val Pro Thr Ala Asp Ala Leu Ala Asp Gly Val Thr 530 535 540 Asp Ala Leu Asn Thr Ala Leu Thr Glu Ser Leu Arg Gln Leu Ala Lys 545 550 555 560 Glu Ala Gly Leu Gln Ser Tyr Glu Leu Pro Arg Glu Phe Leu Val Glu 565 570 575 Thr Glu Pro Phe Thr Val Glu Asn Gly Leu Leu Ser Gly Ile Ala Lys 580 585 590 Leu Leu Arg Pro Lys Leu Lys Glu His Tyr Gly Glu Arg Leu Glu Gln 595 600 605 Leu Tyr Arg Asp Ile Glu Ala Asn Arg Asn Asp Glu Leu Ile Glu Leu 610 615 620 Arg Arg Thr Ala Ala Glu Leu Pro Val Leu Glu Thr Val Thr Arg Ala 625 630 635 640 Ala Arg Ser Met Leu Gly Leu Ala Ala Ser Glu Leu Arg Pro Asp Ala 645 650 655 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser 660 665 670 Thr Leu Leu Gln Asp Met Leu Glu Val Glu Val Pro Val Gly Val Ile 675 680 685 Val Ser Pro Ala Asn Ser Leu Ala Asp Leu Ala Lys Tyr Ile Glu Ala 690 695 700 Glu Arg His Ser Gly Val Arg Arg Pro Ser Leu Ile Ser Val His Gly 705 710 715 720 Pro Gly Thr Glu Ile Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile 725 730 735 Asp Glu Arg Thr Leu Ala Ala Ala Lys Ala Val Pro Ala Ala Pro Ala 740 745 750 Gln Ala Gln Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg 755 760 765 Phe Leu Cys Leu Glu Trp Leu Gln Arg Leu Asp Gln Thr Gly Gly Thr 770 775 780 Leu Val Cys Ile Val Arg Gly Thr Asp Ala Ala Ala Ala Arg Lys Arg 785 790 795 800 Leu Asp Ala Val Phe Asp Ser Gly Asp Pro Glu Leu Leu Asp His Tyr 805 810 815 Arg Lys Leu Ala Ala Glu His Leu Glu Val Leu Ala Gly Asp Ile Gly 820 825 830 Asp Pro Asn Leu Gly Leu Asp Glu Ala Thr Trp Gln Arg Leu Ala Ala 835 840 845 Thr Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His Val Leu 850 855 860 Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile 865 870 875 880 Ile Arg Leu Ala Ile Thr Glu Arg Arg Lys Pro Val Thr Tyr Leu Ser 885 890 895 Thr Val Ala Val Ala Ala Gln Val Asp Pro Ala Gly Phe Asp Glu Glu 900 905 910 Arg Asp Ile Arg Glu Met Ser Ala Val Arg Ser Ile Asp Ala Gly Tyr 915 920 925 Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg 930 935 940 Glu Ala His Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp 945 950 955 960 Met Ile Leu Ala His Ser Lys Tyr Val Gly Gln Leu Asn Val Pro Asp 965 970 975 Val Phe Thr Arg Leu Ile Leu Ser Leu Ala Leu Thr Gly Ile Ala Pro 980 985 990 Tyr Ser Phe Tyr Gly Thr Asp Ser Ala Gly Gln Arg Arg Arg Ala His 995 1000 1005 Tyr Asp Gly Leu Pro Ala Asp Phe Val Ala Glu Ala Ile Thr Thr 1010 1015 1020 Leu Gly Ala Arg Ala Glu Ser Gly Phe His Thr Tyr Asp Val Trp 1025 1030 1035 Asn Pro Tyr Asp Asp Gly Ile Ser Leu Asp Glu Phe Val Asp Trp 1040 1045 1050 Leu Gly Asp Phe Gly Val Pro Ile Gln Arg Ile Asp Asp Tyr Asp 1055 1060 1065 Glu Trp Phe Arg Arg Phe Glu Thr Ala Ile Arg Ala Leu Pro Glu 1070 1075 1080 Lys Gln Arg Asp Ala Ser Leu Leu Pro Leu Leu Asp Ala His Arg 1085 1090 1095 Arg Pro Leu Arg Ala Val Arg Gly Ser Leu Leu Pro Ala Lys Asn 1100 1105 1110 Phe Gln Ala Ala Val Gln Ser Ala Arg Ile Gly Pro Asp Gln Asp 1115 1120 1125 Ile Pro His Leu Ser Pro Gln Leu Ile Asp Lys Tyr Val Thr Asp 1130 1135 1140 Leu Arg His Leu Gly Leu Leu 1145 1150 <210> 256 <211> 1188 <212> PRT <213> Artificial Sequence <220> <223> Segniliparus rugosus ATCC BAA-974 <400> 256 Met Thr Glu Ser Gln Ser Tyr Glu Thr Arg Gln Ala Arg Pro Ala Gly 1 5 10 15 Gln Ser Leu Ala Glu Arg Val Ala Arg Leu Val Ala Ile Asp Pro Gln 20 25 30 Ala Ala Ala Ala Val Pro Asp Lys Ala Val Ala Glu Arg Ala Thr Gln 35 40 45 Gln Gly Leu Arg Leu Ala Gln Arg Ile Glu Ala Phe Leu Ser Gly Tyr 50 55 60 Gly Asp Arg Pro Ala Leu Ala Gln Arg Ala Phe Glu Ile Thr Lys Asp 65 70 75 80 Pro Ile Thr Gly Arg Ala Val Ala Thr Leu Leu Pro Lys Phe Glu Thr 85 90 95 Val Ser Tyr Arg Glu Leu Leu Glu Arg Ser His Ala Ile Ala Ser Glu 100 105 110 Leu Ala Asn His Ala Glu Ala Pro Val Lys Ala Gly Glu Phe Ile Ala 115 120 125 Thr Ile Gly Phe Thr Ser Thr Asp Tyr Thr Ser Leu Asp Ile Ala Gly 130 135 140 Val Leu Leu Gly Leu Thr Ser Val Pro Leu Gln Thr Gly Ala Thr Thr 145 150 155 160 Asp Thr Leu Lys Ala Ile Ala Glu Glu Thr Ala Pro Ala Val Phe Gly 165 170 175 Ala Ser Val Glu His Leu Asp Asn Ala Val Thr Thr Ala Leu Ala Thr 180 185 190 Pro Ser Val Arg Arg Leu Leu Val Phe Asp Tyr Arg Gln Gly Val Asp 195 200 205 Glu Asp Arg Glu Ala Val Glu Ala Ala Arg Ser Arg Leu Ala Glu Ala 210 215 220 Gly Ser Ala Val Leu Val Asp Thr Leu Asp Glu Val Ile Ala Arg Gly 225 230 235 240 Arg Ala Leu Pro Arg Val Ala Leu Pro Pro Ala Thr Asp Ala Gly Asp 245 250 255 Asp Ser Leu Ser Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro 260 265 270 Lys Gly Ala Met Tyr Pro Glu Arg Asn Val Ala Gln Phe Trp Gly Gly 275 280 285 Ile Trp His Asn Ala Phe Asp Asp Gly Asp Ser Ala Pro Asp Val Pro 290 295 300 Asp Ile Met Val Asn Phe Met Pro Leu Ser His Val Ala Gly Arg Ile 305 310 315 320 Gly Leu Met Gly Thr Leu Ser Ser Gly Gly Thr Thr Tyr Phe Ile Ala 325 330 335 Lys Ser Asp Leu Ser Thr Phe Phe Glu Asp Tyr Ser Leu Ala Arg Pro 340 345 350 Thr Lys Leu Phe Phe Val Pro Arg Ile Cys Glu Met Ile Tyr Gln His 355 360 365 Tyr Gln Ser Glu Leu Asp Arg Ile Gly Ala Ala Asp Gly Ser Pro Gln 370 375 380 Ala Glu Ala Ile Lys Thr Glu Leu Arg Glu Lys Leu Leu Gly Gly Arg 385 390 395 400 Val Leu Thr Ala Gly Ser Gly Ser Ala Pro Met Ser Pro Glu Leu Thr 405 410 415 Ala Phe Ile Glu Ser Val Leu Gln Val His Leu Val Asp Gly Tyr Gly 420 425 430 Ser Thr Glu Ala Gly Pro Val Trp Arg Asp Arg Lys Leu Val Lys Pro 435 440 445 Pro Val Thr Glu His Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe 450 455 460 Ser Thr Asp Ser Pro Tyr Pro Arg Gly Glu Leu Ala Ile Lys Thr Gln 465 470 475 480 Thr Ile Leu Pro Gly Tyr Tyr Lys Arg Pro Glu Thr Thr Ala Glu Val 485 490 495 Phe Asp Glu Asp Gly Phe Tyr Leu Thr Gly Asp Val Val Ala Glu Val 500 505 510 Ala Pro Glu Glu Phe Val Tyr Val Asp Arg Arg Lys Asn Val Leu Lys 515 520 525 Leu Ser Gln Gly Glu Phe Val Ala Leu Ser Lys Leu Glu Ala Ala Tyr 530 535 540 Gly Thr Ser Pro Leu Val Arg Gln Ile Ser Val Tyr Gly Ser Ser Gln 545 550 555 560 Arg Ser Tyr Leu Leu Ala Val Val Val Pro Thr Pro Glu Ala Leu Ala 565 570 575 Lys Tyr Gly Asp Gly Glu Ala Val Lys Ser Ala Leu Gly Asp Ser Leu 580 585 590 Gln Lys Ile Ala Arg Glu Glu Gly Leu Gln Ser Tyr Glu Val Pro Arg 595 600 605 Asp Phe Ile Ile Glu Thr Asp Pro Phe Thr Ile Glu Asn Gly Ile Leu 610 615 620 Ser Asp Ala Gly Lys Thr Leu Arg Pro Lys Val Lys Ala Arg Tyr Gly 625 630 635 640 Glu Arg Leu Glu Ala Leu Tyr Ala Gln Leu Ala Glu Thr Gln Ala Gly 645 650 655 Glu Leu Arg Ser Ile Arg Val Gly Ala Gly Glu Arg Pro Val Ile Glu 660 665 670 Thr Val Gln Arg Ala Ala Ala Ala Leu Leu Gly Ala Ser Ala Ala Glu 675 680 685 Val Asp Pro Glu Ala His Phe Ser Asp Leu Gly Gly Asp Ser Leu Ser 690 695 700 Ala Leu Thr Tyr Ser Asn Phe Leu His Glu Ile Phe Gln Val Glu Val 705 710 715 720 Pro Val Ser Val Ile Val Ser Ala Ala Asn Asn Leu Arg Ser Val Ala 725 730 735 Ala His Ile Glu Lys Glu Arg Ser Ser Gly Ser Asp Arg Pro Thr Phe 740 745 750 Ala Ser Val His Gly Ala Gly Ala Thr Thr Ile Arg Ala Ser Asp Leu 755 760 765 Lys Leu Glu Lys Phe Leu Asp Ala Gln Thr Leu Ala Ala Ala Pro Ser 770 775 780 Leu Pro Arg Pro Ala Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ser 785 790 795 800 Asn Gly Trp Leu Gly Arg Phe Leu Ala Leu Ala Trp Leu Glu Arg Leu 805 810 815 Val Pro Gln Gly Gly Lys Val Val Val Ile Val Arg Gly Lys Asp Asp 820 825 830 Lys Ala Ala Lys Ala Arg Leu Asp Ser Val Phe Glu Ser Gly Asp Pro 835 840 845 Ala Leu Leu Ala His Tyr Glu Asp Leu Ala Asp Lys Gly Leu Glu Val 850 855 860 Leu Ala Gly Asp Phe Ser Asp Ala Asp Leu Gly Leu Arg Lys Ala Asp 865 870 875 880 Trp Asp Arg Leu Ala Asp Glu Val Asp Leu Ile Val His Ser Gly Ala 885 890 895 Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro Asn Val 900 905 910 Val Gly Thr Ala Glu Val Ala Lys Leu Ala Leu Thr Lys Arg Leu Lys 915 920 925 Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala Val Gly Val Glu Pro 930 935 940 Ser Ala Phe Glu Glu Asp Gly Asp Ile Arg Asp Val Ser Ala Val Arg 945 950 955 960 Ser Ile Asp Glu Gly Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala 965 970 975 Gly Glu Val Leu Leu Arg Glu Ala Tyr Glu His Ala Gly Leu Pro Val 980 985 990 Arg Val Phe Arg Ser Asp Met Ile Leu Ala His Arg Lys Tyr Thr Gly 995 1000 1005 Gln Leu Asn Val Pro Asp Gln Phe Thr Arg Leu Ile Leu Ser Leu 1010 1015 1020 Leu Ala Thr Gly Ile Ala Pro Lys Ser Phe Tyr Gln Leu Asp Ala 1025 1030 1035 Thr Gly Gly Arg Gln Arg Ala His Tyr Asp Gly Ile Pro Val Asp 1040 1045 1050 Phe Thr Ala Glu Ala Ile Thr Thr Leu Gly Leu Ala Gly Ser Asp 1055 1060 1065 Gly Tyr His Ser Phe Asp Val Phe Asn Pro His His Asp Gly Val 1070 1075 1080 Gly Leu Asp Glu Phe Val Asp Trp Leu Val Glu Ala Gly His Pro 1085 1090 1095 Ile Ser Arg Val Asp Asp Tyr Ala Glu Trp Leu Ser Arg Phe Glu 1100 1105 1110 Thr Ser Leu Arg Gly Leu Pro Glu Ala Gln Arg Gln His Ser Val 1115 1120 1125 Leu Pro Leu Leu His Ala Phe Ala Gln Pro Ala Pro Ala Ile Asp 1130 1135 1140 Gly Ser Pro Phe Gln Thr Lys Asn Phe Gln Ser Ser Val Gln Glu 1145 1150 1155 Ala Lys Val Gly Ala Glu His Asp Ile Pro His Leu Asp Lys Ala 1160 1165 1170 Leu Ile Val Lys Tyr Ala Glu Asp Ile Lys Gln Leu Gly Leu Leu 1175 1180 1185 <210> 257 <211> 1185 <212> PRT <213> Artificial Sequence <220> <223> Nocardia sp. Y48 <400> 257 Met Thr Thr Gly Ser Trp Ser Glu Thr Ser Glu Val His Gly Val Ser 1 5 10 15 Gly Pro Arg Glu Glu Arg Arg Ala Ala Gln Leu Arg Ala Gln Asp Glu 20 25 30 Gln Val Arg Ala Ala Ala Pro Leu Asp Ala Val Asn Glu Ala Thr Ser 35 40 45 Ser Pro Gly Gln Arg Leu Thr Gln Val Val Ala Ala Ile Met Ala Gly 50 55 60 Tyr Ala Asp Arg Pro Ala Leu Gly Glu Arg Ala Arg Glu Leu Val Thr 65 70 75 80 Asp Pro Gly Thr Gly Arg Thr Ser Ile Arg Leu Leu Pro Trp Phe Asp 85 90 95 Thr Ile Ser Tyr Arg Glu Leu Trp Thr Arg Val Gly Ala Ile Ala Ser 100 105 110 Asp Trp His His His Pro Asp His Pro Leu Ala Ala Gly Glu Phe Val 115 120 125 Gly Ile Leu Gly Phe Thr Ser Cys Asp Tyr Thr Thr Leu Asp Leu Val 130 135 140 Cys Leu His Leu Gly Ala Val Cys Val Pro Leu Gln Ser Ser Ser Pro 145 150 155 160 Ala Ser Gln Leu Arg Pro Ile Ile Ala Glu Thr Gly Pro Ser Ile Leu 165 170 175 Ala Thr Ser Ala Glu Arg Leu Asp Thr Ala Val Glu Leu Ala Leu Gly 180 185 190 Ser Pro Thr Val Arg Arg Leu Val Val Phe Asp Ser His Pro Glu Val 195 200 205 Asp Glu Gln Arg Glu Ala Leu Glu Ser Ala Arg Gln Arg Leu Thr Glu 210 215 220 Ala Gly His Pro Ala Val Val Asp Ser Leu Ala Ala Val Leu Glu Arg 225 230 235 240 Gly Arg Ala Leu Pro Pro Ala Pro Leu Phe Thr Pro Gly Pro Asp Glu 245 250 255 Asp Pro Leu Thr Met Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro 260 265 270 Lys Gly Ala Met Tyr Pro Glu Arg Leu Val His Ser Leu Trp Asp Gly 275 280 285 Leu Trp Arg Asp Lys Asn Ala Leu Pro Val Ile Gly Ile Asn Tyr Met 290 295 300 Pro Met Ser His Leu Ala Gly Arg Ile Ser Leu Leu Arg Ala Leu Ser 305 310 315 320 Ser Gly Gly Thr Ser Tyr Phe Ala Ala Lys Ser Asp Leu Ser Thr Leu 325 330 335 Phe Glu Asp Ile Ala Leu Ile Arg Pro Thr Glu Leu Asn Leu Val Pro 340 345 350 Arg Val Cys Asp Met Leu Phe Gln Arg Tyr Gln Ser Glu Leu Asp Arg 355 360 365 Arg Ala Pro Gly Thr Ser Asp Leu Asp Ala Val Asp Ala Gln Val Lys 370 375 380 Gln Glu Leu Arg Glu Gly Phe Leu Gly Gly Arg Val Val Arg Ala Met 385 390 395 400 Cys Ser Thr Ala Pro Leu Ser Ala Glu Met Ala Ala Phe Val Glu Ser 405 410 415 Cys Leu Asp Leu Glu Leu His Asp Gly Tyr Gly Ser Thr Glu Ala Gly 420 425 430 Gly Val Val Ile Asp Lys His Val Leu Arg Pro Pro Val Leu Asp Tyr 435 440 445 Lys Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Thr Pro 450 455 460 His Pro Arg Gly Glu Leu Leu Ile Lys Thr Arg Thr Ile Ile Pro Gly 465 470 475 480 Tyr Phe Lys Arg Pro Asp Ala Thr Ala Glu Ile Phe Asp Ala Asp Gly 485 490 495 Tyr Tyr Gln Thr Gly Asp Ile Met Ala Glu Ile Gly Pro Asp Gln Leu 500 505 510 Val Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ser Gln Gly Glu 515 520 525 Phe Val Ala Val Ser Arg Leu Glu Ala Val Phe Ala Thr Ser Pro Leu 530 535 540 Val Arg Gln Val Phe Val Tyr Gly Ser Ser Ala Arg Ala Tyr Leu Leu 545 550 555 560 Ala Val Val Val Pro Thr Glu Glu Ala Leu Arg Arg Thr Val Thr Asp 565 570 575 Asn Ala Ala Leu Lys Ser Ser Ile Ser Glu Ser Leu Gln Arg Ile Ala 580 585 590 Arg Glu Ala Glu Leu Asn Ser Tyr Glu Ile Pro Arg Asp Leu Leu Ile 595 600 605 Glu Thr Asp Pro Phe Ser Thr Glu Asn Gly Leu Leu Ser Asp Ala Arg 610 615 620 Lys Leu Leu Arg Pro Arg Leu Lys Glu His Tyr Gly Glu Arg Leu Glu 625 630 635 640 Gln Leu Tyr Ala Glu Leu Ala Lys Gly Gln Val Asp Glu Leu His Ala 645 650 655 Leu Arg Val Thr Gly Arg Asp Arg Pro Val Leu Glu Thr Val Thr Arg 660 665 670 Ala Ala Gln Ala Leu Leu Gly Cys Ala Ser Thr Asp Leu Ser Pro Asp 675 680 685 Ala His Phe Thr Glu Leu Gly Gly Asp Ser Leu Ser Ala Leu Ser Leu 690 695 700 Ser Asn Leu Leu Gln Glu Ile Phe Thr Val Glu Val Pro Val Gly Val 705 710 715 720 Val Ile Ser Pro Ala Asn Asp Leu Arg Gln Leu Ala Asn Tyr Val Glu 725 730 735 Thr Glu Leu Ser Ser Gly Ala Lys Arg Pro Thr Phe Ala Thr Val His 740 745 750 Gly Gln Gly Ser Leu Glu Val Arg Ala Ala Asp Leu Thr Leu Asp Lys 755 760 765 Phe Ile Asp Ser Ala Thr Leu Ala Gly Ala Lys Asp Leu Pro Gly Pro 770 775 780 Ser Gly Thr Ala Arg Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu 785 790 795 800 Gly Arg Phe Leu Cys Leu Glu Trp Leu Arg Arg Leu Ser Gln Asp Gly 805 810 815 Gly Lys Leu Val Cys Ile Val Arg Gly Ser Ser Ala Glu Ala Ala Arg 820 825 830 Arg Arg Leu Glu Gln Ala Phe Asp Ser Gly Asp Ala Glu Leu Leu Arg 835 840 845 Leu Phe Arg Glu Leu Ala Ala Glu His Leu Glu Val Leu Ala Gly Asp 850 855 860 Ile Gly Glu Pro Asp Leu Gly Leu Asp Glu Gln Thr Trp His Arg Leu 865 870 875 880 Ala Asp Ser Val Asp Leu Ile Val His Pro Ala Ala Leu Val Asn His 885 890 895 Val Leu Pro Tyr Gln Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala 900 905 910 Gly Leu Ile Arg Met Ala Ile Thr Lys Arg Leu Lys Pro Phe Val Tyr 915 920 925 Leu Ser Thr Val Gly Val Leu Ser Ala Gln Ile Ala Pro Ser Ala Leu 930 935 940 Arg Glu Asp Leu Asp Ile Arg Asp Thr Ser Pro Val Arg Arg Leu Asp 945 950 955 960 Gln Ser Tyr Ala Ser Gly Tyr Gly Thr Ser Lys Trp Ala Gly Glu Val 965 970 975 Leu Leu Arg Glu Ala His Glu Ala Phe Gly Leu Pro Ala Val Val Phe 980 985 990 Arg Ser Asp Met Ile Leu Ala His Ser Arg Tyr Thr Gly Gln Leu Asn 995 1000 1005 Val Pro Asp Met Phe Thr Arg Leu Leu Leu Ser Leu Val Leu Thr 1010 1015 1020 Gly Ile Ala Pro Lys Ser Phe Tyr Arg Thr Gly Ser Asp Gly Gly 1025 1030 1035 Arg Gln Arg Ala His Tyr Asp Gly Leu Pro Ala Glu Phe Thr Ala 1040 1045 1050 Glu Ala Ile Thr Glu Leu Gly Ala Arg Ala Ala Ala Gly Tyr Arg 1055 1060 1065 Thr Phe Asn Val Leu Asn Pro His Asp Asp Gly Ile Ser Leu Asp 1070 1075 1080 Val Leu Val Asp Trp Leu Ala Glu Thr Gly His Pro Ile Gln Arg 1085 1090 1095 Ile Glu Asp Tyr Gln Glu Trp Phe Ala Arg Phe Asp Thr Ala Leu 1100 1105 1110 Arg Ala Leu Pro Glu Lys Gln Arg Gln His Cys Leu Leu Pro Leu 1115 1120 1125 Met His Ala Phe Glu Gln Pro Gly Val Pro Val Ala Gly Ser Val 1130 1135 1140 Ile Pro Ala Asp Glu Phe Arg Ala Ala Val Arg Thr Ala Lys Ile 1145 1150 1155 Gly Pro Asp Lys Asp Ile Pro His Leu Ser Ala Ser Leu Ile Thr 1160 1165 1170 Lys Tyr Val Arg Asp Leu Glu Gln Leu Gly Leu Val 1175 1180 1185 <210> 258 <211> 1164 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium vanbaalenii PYR-1 <400> 258 Met Glu Arg Lys Ala Glu Val Leu Ala Ala Arg Arg Val Glu Asp Leu 1 5 10 15 Ile Glu Arg Asp Ala Gln Val Arg Ala Ala Ile Pro Asp Pro Val Val 20 25 30 Thr Ala Glu Leu Glu Arg Ala Asp Gly Ser Leu Ala Gln Thr Val Ala 35 40 45 Arg Val Met Ala Gly Tyr Ala Asp Arg Pro Ala Leu Gly Gln Arg Ala 50 55 60 Val Glu Phe Val Pro Asp Glu Asn Gly Cys Arg Arg Thr Arg Leu Leu 65 70 75 80 Pro Trp Phe Asp Thr Ile Thr Phe Gly Glu Leu Trp Gln Arg Val Gly 85 90 95 Thr Val Ala Ala Val Trp Gln Ser Arg Ala Glu Arg Ser Val Arg Ala 100 105 110 Gly Asp Phe Val Ala Val Leu Gly Ser Thr Gly Ile Asp Tyr Thr Val 115 120 125 Val Asp Leu Ala Cys Thr Tyr Ser Gly Ala Val Pro Val Pro Leu Gln 130 135 140 Ala Gly Ala Ser Pro Thr Gln Leu Ala Pro Ile Val Arg Glu Val Glu 145 150 155 160 Pro Lys Val Leu Ala Thr Asp Val Gly Gln Leu Glu Val Ala Val Asp 165 170 175 Leu Ala Ser Ala Gly Asp Ser Val Arg Ser Leu Leu Ile Phe Gly Leu 180 185 190 Tyr Ala Glu Asp Asp Glu His Cys Ala Ala Val Glu Ser Ala Arg Arg 195 200 205 Arg Leu Ala Asp Thr Pro Val Val Val Glu Thr Ile Val Glu Leu Leu 210 215 220 Ala Ser Gly Gln Asp Arg Pro Ala Ala Ser Leu His Ala Ser Ala Asp 225 230 235 240 Pro Asp Glu Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr 245 250 255 Pro Lys Gly Ala Met Tyr Thr Gln Arg Leu Leu Thr Asn Ala Trp Cys 260 265 270 Ala Ala Gly Ala Ser Pro Met Pro Ser Ile Ala Leu Ser Tyr Leu Pro 275 280 285 Met Ser His Thr Met Ala Arg Gln Leu Leu Leu Thr Gly Leu Ala Arg 290 295 300 Gly Gly Thr Val Tyr Phe Ala Ala Arg Asn Asp Met Ser Thr Leu Phe 305 310 315 320 Asp Asp Phe Ala Leu Ala Arg Pro Thr Leu Leu Gly Phe Val Pro Arg 325 330 335 Val Cys Asp Met Val Leu Gln Arg Phe Gln Ser Glu Met Ala Arg Arg 340 345 350 Val Gly Ala Asp Asp Glu Pro Thr Val Val Glu Gln Glu Val Lys Thr 355 360 365 Glu Leu Arg Glu Gln Phe Leu Gly Gly Arg Phe Leu Val Ala Ser Ile 370 375 380 Gly Ser Ala Pro Leu Ser Ala Asp Met Arg Glu Phe Met Gln Ser Val 385 390 395 400 Leu Gly Ile Ala Leu Ile Asp Ala Tyr Gly Ser Thr Glu Thr Gly Gly 405 410 415 Val Leu Met Asn Asn Lys Val Val Arg Thr Ala Ile Leu Asp Tyr Lys 420 425 430 Leu Val Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp Arg Pro His 435 440 445 Pro Arg Gly Glu Leu Leu Ile Lys Ser Arg Thr Leu Ile Pro Gly Tyr 450 455 460 Tyr Lys Arg Pro Glu Leu Asn Ser Gln Phe Phe Asp Ala Glu Gly Phe 465 470 475 480 Tyr Arg Thr Gly Asp Val Met Ala Gln Thr Gly Phe Asp Glu Leu Val 485 490 495 Tyr Val Asp Arg Arg Asn Ser Val Leu Lys Leu Ser Gln Gly Glu Phe 500 505 510 Val Ala Val Ser Lys Leu Glu Ala Ile Phe Val Gly Ser Pro Leu Val 515 520 525 Glu Gln Ile Tyr Val Tyr Gly Ser Ser Glu Arg Ala Tyr Leu Leu Ala 530 535 540 Val Ile Val Pro Val Ala Glu Ala Ile Ala Thr His Ala Gly Thr Ala 545 550 555 560 Glu Leu Lys Ala Ala Ile Ser Glu Ser Leu Arg Gln Ile Ala Lys Asp 565 570 575 Ala Glu Leu Ser Ser Tyr Glu Val Pro Arg Asp Phe Leu Leu Glu Ser 580 585 590 Glu Pro Phe Thr Val Asp Asn Gly Leu Leu Ala Gly Leu Ser Lys Leu 595 600 605 Leu Arg Pro Ser Leu Lys Glu Arg Tyr Gly Glu Arg Leu Glu Ala Leu 610 615 620 Tyr Arg Val Ala Glu Ala Ala Gln Thr Gln Glu Leu Ala Ala Leu Arg 625 630 635 640 Gln Gln Ala Gly Met Leu Pro Val Leu Glu Thr Val Ser Arg Ala Ala 645 650 655 Gln Ala Val Leu Gly Val Ser Ala Ala Glu Leu Arg Pro Asp Ala His 660 665 670 Phe Thr Asp Leu Gly Gly Asp Ser Leu Ala Ala Leu Ser Phe Ser Thr 675 680 685 Leu Leu Gln Glu Leu Leu Gly Val Gln Val Pro Val Gly Val Ile Ala 690 695 700 Ser Ser Ala Asn Asp Leu Arg Arg Ile Ala Asn Tyr Ala Val Ala Glu 705 710 715 720 Arg Ser Ala Gly Ser Leu Arg Pro Thr Ser Thr Gly Val His Gly Thr 725 730 735 Gly Ser Gln Leu Arg Ala Ile Asp Leu Arg Leu Asp Lys Phe Ile Asp 740 745 750 Pro Ser Thr Leu Ala Ala Ala Thr Thr Leu Pro Arg Ala Gly Glu Pro 755 760 765 Arg Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly Arg Phe Leu 770 775 780 Cys Leu Glu Trp Leu Gln Arg Leu His His Ser Gly Gly Thr Leu Ile 785 790 795 800 Cys Val Val Arg Gly Ile Asp Ala Val Ala Ala Arg Glu Arg Leu Asp 805 810 815 Glu Val Phe Asp Ser Gly Asp Pro Glu Leu Leu His Arg Tyr Arg Glu 820 825 830 Leu Ala Glu Gly Thr Leu Glu Val Leu Cys Gly Asp Ile Ser Glu Pro 835 840 845 Gly Leu Gly Leu Ser Glu Arg Asp Trp Arg Arg Leu Ala Asp Thr Val 850 855 860 Glu Leu Ile Val His Ala Ala Ala Leu Val Asn His Val Leu Pro Tyr 865 870 875 880 Gly Gln Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Arg 885 890 895 Leu Ala Met Thr Thr Arg Ile Lys Pro Val Thr Tyr Leu Ser Thr Val 900 905 910 Ala Val Ala Ala Gln Val Ala Pro Glu Gln Phe Thr Glu Asp Gly Asp 915 920 925 Ile Arg Glu Ile Ser Ala Val Arg Ser Leu Asp Glu Gly Tyr Ala Asp 930 935 940 Gly Tyr Gly Thr Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala 945 950 955 960 Tyr Asp Leu Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile 965 970 975 Leu Ala His Ser Arg Phe Ala Gly Gln Leu Asn Val Ser Asp Met Phe 980 985 990 Thr Arg Leu Val Leu Ser Val Leu Ala Thr Gly Val Ala Pro Lys Ser 995 1000 1005 Phe Tyr Glu Thr Asp Arg Met Gly Asn Arg Gln Arg Ala His Tyr 1010 1015 1020 Asp Gly Leu Pro Val Asp Phe Thr Ala Gln Ala Ile Thr Val Leu 1025 1030 1035 Gly Ser Gln Val Val Ser Gly Phe Glu Thr Phe Asp Val Leu Asn 1040 1045 1050 Pro His Asp Asp Gly Leu Ser Leu Asp Glu Phe Val Asp Trp Leu 1055 1060 1065 Ile Ala Ala Gly His Ser Ile Asp Arg Ile Asp Gly Tyr Ala Glu 1070 1075 1080 Trp Leu Ser Arg Phe Gly Thr Ala Leu Arg Val Leu Ser Glu Arg 1085 1090 1095 Gln Arg Gln His Ser Val Leu Pro Leu Leu His Ala Tyr Arg Arg 1100 1105 1110 Ala Ala Val Pro Ile Pro Gly Ala Ala Leu Pro Ala Lys Lys Phe 1115 1120 1125 Gln Ala Ala Val Gln Asp Ala Gln Leu Gly Pro Gly Arg Asp Ile 1130 1135 1140 Pro His Leu Thr Pro Asp Leu Ile Glu Lys Tyr Val Ser Asp Leu 1145 1150 1155 Lys Leu Arg Asn Leu Leu 1160 <210> 259 <211> 1166 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium fallax <400> 259 Met Ser Ser Asp Pro Arg Glu Asp Ala Val Ala Arg Arg Met Met Glu 1 5 10 15 Val Tyr Ser Gly Asp Pro Glu Val Arg Ala Ala Met Ala Val Glu Ser 20 25 30 Val Ser Ala Glu Ile Arg Arg Pro Gly Leu His Leu Ala Glu Val Val 35 40 45 Glu Thr Val Met Ser Ser Tyr Ala Glu Arg Pro Ala Leu Gly Arg Arg 50 55 60 Ala Phe Glu Tyr Thr Val Asp Pro Ala Thr Gly Arg Cys Ala Ala His 65 70 75 80 Leu Leu Pro Arg Phe Asp Thr Ile Thr Tyr Gly Glu Leu Trp Glu Arg 85 90 95 Val Arg Ala Ile Ala Gly Ala Trp His His Asp Pro Glu Ile Ala Leu 100 105 110 Val Pro Gly Asp Phe Val Ala Ile Val Gly Phe Thr Ser Ser Asp Tyr 115 120 125 Val Ala Leu Asp Leu Ala Cys Ile Tyr Leu Gly Ala Val Val Ala Pro 130 135 140 Leu Pro Ala Thr Ala Gly Ala Glu Glu Leu Arg Gly Tyr Leu Ala Glu 145 150 155 160 Ile Glu Pro Arg Ile Leu Ala Val Thr Pro Asp Leu Leu Glu Thr Ala 165 170 175 Val Ala Ala Ile Gly Asp Gly Leu Ser Lys Ser Val Arg Leu Ile Val 180 185 190 Phe Asp Arg Cys Pro Gly Asp Asp Ala Glu Arg Glu Arg Ile Glu Ser 195 200 205 Ala Ala Ser Met Leu Asp Asn Gly Lys Ile Leu Asp Thr Leu Glu Asp 210 215 220 Val Val Glu Arg Gly Ala Arg Tyr Pro Val Pro Ala Met Phe Ser His 225 230 235 240 Ser Asp Ser Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Ser Pro Lys Gly Ala Leu Tyr Thr Glu Arg Leu Cys Leu Arg 260 265 270 Ala Trp Leu Val Gly Pro Gly Ala Gly Ala Ala Ile Thr Val Asn Tyr 275 280 285 Met Pro Leu Ser His Ile Gly Gly Arg Met Thr Leu Phe Gly Val Leu 290 295 300 Ala Arg Gly Gly Thr Asn Tyr Phe Thr Ala Ala Ser Asp Leu Ser Gln 305 310 315 320 Ile Phe Asp Asp Ile Ala Leu Val Arg Pro Thr Glu Leu Thr Leu Val 325 330 335 Pro Arg Leu Cys Asp Met Ala Leu Gln Thr Tyr His Asn Glu Leu Asn 340 345 350 Arg Arg Ser Ala Glu Glu Ile Asp Val Ser Arg Leu Glu Ala Glu Val 355 360 365 Arg Glu Asn Leu Arg Asp Lys Phe Phe Gly Gly Arg Leu Leu Ile Ala 370 375 380 Gly Phe Gly Ser Ala Pro Leu Ala Gly Gln Met Arg Thr Phe Ile Glu 385 390 395 400 Ser Val Leu Glu Val Pro Leu Arg Asp Gly Tyr Gly Ser Thr Glu Ala 405 410 415 Gly Gly Gly Ile Val Leu Asp Asn Gln Val Gln Arg Pro Pro Val Ile 420 425 430 Asp Tyr Met Leu Ala Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr Asp 435 440 445 Arg Pro Tyr Pro Arg Gly Glu Leu Leu Val Lys Ser Ser Thr Gln Ile 450 455 460 Pro Gly Tyr Phe Lys Arg Pro Asp Leu Ser Ala Thr Met Ile Asp Ser 465 470 475 480 Asp Gly Tyr Tyr His Thr Gly Asp Val Met Ala Gln Ile Gly Pro Asp 485 490 495 Arg Leu Thr Tyr Ile Asp Arg Arg Ser Asn Val Val Lys Leu Ser Gln 500 505 510 Gly Glu Phe Val Thr Ile Ala Arg Val Glu Ala Val Leu Ala Thr Ala 515 520 525 Arg Trp Val Arg Gln Ile Phe Val Tyr Gly Ser Ser Glu Arg Ala Tyr 530 535 540 Leu Leu Ala Val Val Val Pro Thr Gly Ser Ala Leu Arg Glu Tyr Cys 545 550 555 560 Asp Pro Ala Glu Leu Lys Glu Ala Val Thr Lys Ser Leu Arg Thr Ala 565 570 575 Ala Ala Val Ala Asp Leu Arg Pro Tyr Glu Ile Pro Arg Asp Val Leu 580 585 590 Ile Glu Thr Glu Pro Phe Ala Val Ala Asn Ala Leu Leu Ser Gly Leu 595 600 605 Gly Lys Leu Leu Arg Pro Glu Leu Val Arg Arg Tyr Gly Ala Ser Leu 610 615 620 Gln Gln Met Tyr Ala Asp Leu Glu His Ala Glu Arg Gln Ala Leu Arg 625 630 635 640 Ser Ile Gln Ala Gln Val Arg Phe Arg Pro Val Arg Glu Ile Val Gly 645 650 655 Arg Val Ala Ser Ala Leu Leu Gly Ser Pro Ala Ala Thr Leu Arg Gly 660 665 670 Asp Val Arg Phe Val Glu Met Gly Gly Asp Ser Leu Thr Ala Val Ala 675 680 685 Leu Ser Lys Gln Leu Gly Glu Leu Tyr Gly Val Asp Val Pro Val Ala 690 695 700 Leu Val Ile Asp Pro Thr Ile Asp Leu Asp Arg Leu Ser Asp Tyr Val 705 710 715 720 Gln Arg Gln Arg Ser Ser Asn Asp Met His Gly Pro Arg Phe Glu Ser 725 730 735 Val His Gly Ser Pro Ala Asp Val Arg Ala Ala Asp Leu Val Leu Asp 740 745 750 Gln Phe Ile Ala Pro Ala Ala Leu Gly Ala Ala Glu Ser Ala Ala Pro 755 760 765 Pro Thr Ala Ala Pro His Val Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu Ser Arg Leu Gln Arg Asp 785 790 795 800 Gly Gly Thr Leu Ile Cys Leu Val Arg Gly Asp Asp Ala Glu His Ala 805 810 815 Arg Val Arg Leu Glu Ser Ala Phe Glu Ser Thr Pro Pro Leu Ala Glu 820 825 830 Gln Phe Arg Lys Leu Ser Val Asp Arg Leu Glu Val Val Ala Gly Asp 835 840 845 Val Thr Ala Arg Glu Leu Gly Leu Pro Pro Arg Ile Trp Asp Glu Leu 850 855 860 Ala Cys Arg Val Asp Ser Val Val His Ala Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Glu Asp Leu Phe Gly Pro Asn Thr Val Gly Thr Ala 885 890 895 Glu Leu Ile Arg Phe Ala Ile Thr Ser Arg Arg Lys Arg Phe Ser Tyr 900 905 910 Val Ser Thr Val Gly Val Ala Ala Val Ala Gly Ser Thr Val Phe Asp 915 920 925 Glu Asp Ser Asp Val Arg Gln Trp Asn Pro Ala Pro Asp Asp Arg Ala 930 935 940 Asn Tyr Ala Thr Gly Tyr Ser Thr Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Asp Ala His Asp Arg Tyr Gly Leu Pro Val Thr Val Phe Arg 965 970 975 Ser Ala Met Ile Leu Ala His Arg His Tyr Pro Gly Gln Val Asn Val 980 985 990 Ser Asp Arg Phe Thr Arg Leu Leu His Gly Val Leu Thr Thr Gly Leu 995 1000 1005 Ala Pro Ala Thr Phe Tyr Ser Thr Arg Pro Gly Ser Val Arg Ala 1010 1015 1020 His Tyr Asp Gly Leu Pro Val Asp Phe Val Ala Glu Ala Met Val 1025 1030 1035 Thr Leu Ala Arg Lys Ala Gln Gly Asp Phe Arg Thr Tyr His Val 1040 1045 1050 Val Asn Pro His Asp Asp Gly Ile Asp Leu Asp Ser Phe Val Asp 1055 1060 1065 Trp Met Ile Asp Ala Gly Phe Arg Ile Thr Arg Ile Asp Asp Tyr 1070 1075 1080 Ala Val Trp Val Glu Arg Val Ala Val Val Leu Ser Gly Leu Ser 1085 1090 1095 Gly Glu His Arg Gln Asn Ser Leu Leu Pro Leu Leu Asp Ser Tyr 1100 1105 1110 Arg Asn Pro Glu Thr Pro Val Ala Gly Ser Ala Leu Pro Ala Thr 1115 1120 1125 Ala Phe Val Ala Gly Val Arg Ala Gln Arg Ile Gly Asp His Gly 1130 1135 1140 Glu Ile Pro Arg Ile Thr Pro Asp Leu Ile Leu Glu Tyr Ala Asp 1145 1150 1155 Asp Leu Arg Arg Arg Ala Leu Leu 1160 1165 <210> 260 <211> 1159 <212> PRT <213> Artificial Sequence <220> <223> Brevibacterium casei <400> 260 Met Asn Leu Lys Gly Lys Thr Pro Met Leu Leu Asn Thr Gln Met Thr 1 5 10 15 Ser Ile Phe Glu Arg Phe Ser Gly Arg Pro Ala Leu Ala Asp Arg Arg 20 25 30 Pro Ile Pro Arg Ser Asn Gly Asp Arg Asp Leu Phe Asp Ser Glu Val 35 40 45 Leu Asp Trp Tyr Glu Thr Leu Ser Tyr Glu Glu Leu Arg Arg Arg Val 50 55 60 Leu Ala Ala Ala Ala Gln Leu His Gly Arg Arg Met Val Lys Gly Pro 65 70 75 80 Leu Ala Ser Gly Asp Arg Leu Ala Leu Leu Gly Phe Pro Gly Ile Asp 85 90 95 Phe Thr Thr Ile Asp Phe Ala Cys Asn Leu Ala Gly Val Thr Thr Val 100 105 110 Pro Leu Gln Thr Ser Gly Ser Leu Glu Gln His Arg Ser Ile Ile Gly 115 120 125 Glu Thr Ser Pro Arg Ala Leu Val Ile Ser Ile Ser Leu Leu Asn Lys 130 135 140 Ala Glu Ser Ile Leu Ser His Ala Asp Ser Ile Asp Arg Leu Ile Val 145 150 155 160 Leu Asp Tyr Arg Gly Gly Asp Leu Ser His Arg Arg Ile Leu Glu Ser 165 170 175 Ala Ala Asn Ser Leu Pro Ile Ala Pro Glu Leu Leu Glu Leu Asp Pro 180 185 190 Asp Pro Gly Asp Ala Phe Gly Asp Ile Cys Asp Asp His Leu Ser Met 195 200 205 Leu Leu Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr 210 215 220 Ser Ala Arg Leu Val Arg Glu Met Trp Gly Gly Glu Gly Trp Ser Glu 225 230 235 240 Phe Phe Ala Glu Gln Asp Glu Ile Ala Ser Phe His Tyr Met Pro Met 245 250 255 Ser His Val Ala Gly His Ser Ser Val Arg Ser Thr Leu Ser Arg Gly 260 265 270 Gly Val Thr Tyr Phe Ser Ser Thr Pro Asn Leu Ala Asn Phe Phe Asp 275 280 285 Asp Leu Ala Leu Ala Arg Pro Thr Glu Leu Ser Leu Val Pro Arg Val 290 295 300 Cys Glu Leu Leu His Gln Glu Tyr Gln Arg Arg Ala Glu Ser Arg Arg 305 310 315 320 Asp Asp Thr Asp Gly Tyr Ala Ser Gln Ala Val Leu Glu Asp Met Arg 325 330 335 Thr Ser Val Leu Gly Gly Arg Val Glu Trp Ala Ser Cys Thr Ser Ala 340 345 350 Pro Val Ser Ala Glu Leu Lys Ala Phe Met Glu Arg Leu Leu Gly Ile 355 360 365 Glu Leu His Glu Leu Tyr Gly Thr Thr Glu Ile Gly Gly Val Leu Ala 370 375 380 Asp Gly Arg Phe Leu Thr Pro Pro Val Ile Asp Tyr Arg Leu Asp Asp 385 390 395 400 Val Pro Glu Leu Gly Tyr Phe Arg Thr Asp Arg Pro Ser Ala Arg Gly 405 410 415 Glu Leu Leu Val Lys Ser Thr Ser Thr Val Pro Gly Tyr Phe Asn Arg 420 425 430 Pro Asp Leu Asn Ala Glu Ile Phe Thr Glu Asp Gly Tyr Tyr Arg Thr 435 440 445 Gly Asp Ile Ala Ala Val Asp Ser Asn Gly Thr Val Arg Ile Ile Asp 450 455 460 Arg Lys Asn Ser Ile Ile Lys Leu Ser Gln Gly Glu Phe Val Ala Leu 465 470 475 480 Pro Ser Leu Glu Ala Thr Phe Val Ala Gly Ser Thr Leu Ile Arg Gln 485 490 495 Val Phe Leu Tyr Gly Arg Ser Asp Trp Ser Ala Leu Val Ala Val Val 500 505 510 Val Pro Thr Asp Leu Ala Gln Ser Ala Ala Ala Asp Asp Glu Arg Asn 515 520 525 Gln Thr Met Ala Lys Leu Met Leu Asp Glu Leu Arg His Val Ala Glu 530 535 540 Arg Glu His Leu Asn Ser Tyr Glu Val Pro Ala Ala Val Ile Val Glu 545 550 555 560 Ser Glu Pro Phe Ser Glu Glu Asn Gly Leu Leu Ser Asp His Arg Lys 565 570 575 Pro Val Arg Pro Arg Leu His Asp Lys Tyr Gln Ser Gln Leu Glu Ala 580 585 590 Ile Tyr Glu Gln Ile Val Ala Ala Arg Asp Asp Ala Leu Thr Asp Leu 595 600 605 Ile Ala His Gly Ala Glu Asn Asp Thr Ala Ser Thr Ile Arg Asp Ala 610 615 620 Ala Ala Leu Thr Leu Gln Ile Glu Pro Ala Thr Val Ser Ile Asp Ala 625 630 635 640 Lys Phe Arg Asn Leu Gly Gly Asp Ser Leu Thr Ala Val His Leu Ser 645 650 655 Arg Leu Leu Asn Gln Ile Tyr Gly Leu His Ile Pro Val Asp Val Leu 660 665 670 Val Ser Glu Ala Arg Thr Phe Ala Asp Leu Gly Glu Tyr Met Asp Gly 675 680 685 Lys Arg Gly Gln Arg Glu Trp Leu Ala Thr Phe Glu Glu Ile His Thr 690 695 700 Ser Asp Met Arg Pro Leu Tyr Ala Glu Glu Leu Thr Val Glu Arg Phe 705 710 715 720 Leu Ser Ser Arg Ala Thr Ile Asn Pro Ser Ser Thr Arg Tyr Gly Ala 725 730 735 Pro Gln Gly Val Leu Ile Thr Gly Ala Ser Gly Phe Leu Gly Arg Phe 740 745 750 Leu Cys Leu Glu Trp Leu Arg Arg Phe Ala Gly Thr Thr Arg Arg Val 755 760 765 Thr Cys Leu Val Arg Ala Asn Ser His Ala Ala Ala Arg Ala Arg Leu 770 775 780 Arg Ala Thr Tyr Ser Ser Ser Pro Glu Leu Leu Ala Glu Phe Asp Arg 785 790 795 800 Leu Ala Gly Asn Leu Asp Val Val Ala Gly Asp Leu Ala Glu Pro Arg 805 810 815 Leu Gly Leu Asp Glu Gln Ile Trp Lys Ser Leu Ser Gln Asp Ile Thr 820 825 830 His Ile Ile His Ala Gly Ala Met Val Asn His Ala Leu Gly Tyr Arg 835 840 845 Glu Leu Phe Ala Ser Asn Val Ala Gly Thr Ala Glu Val Leu His Leu 850 855 860 Ala Leu Thr Gly Pro Leu Lys Arg Ile Thr Phe Met Ser Ser Ile Ala 865 870 875 880 Thr Ala Leu Leu Gln Gln Ala Gly Gly Pro Met Thr Glu Arg Val Asp 885 890 895 Ile Arg Glu Ala Leu Ser Gln Ile Glu Asp Ala Gly Gly Ile Val Asp 900 905 910 Gly Tyr Ala Ala Thr Lys Trp Ala Ser Glu Val Leu Leu Arg Asn Ala 915 920 925 Asn Glu Gln Phe Gly Val Pro Val Thr Val Phe Arg Ser Ser Met Ile 930 935 940 Leu Ala His Ser Arg Tyr Arg Gly Gln Ile Asn Val Pro Asp Thr Tyr 945 950 955 960 Thr Arg Leu Leu Phe Ser Val Leu Gln Ser Gly Ile Thr Pro Ser Ser 965 970 975 Phe Tyr Ala Ala Asn Gly Glu His Ala His Tyr Asp Gly Leu Pro Val 980 985 990 Asp Val Val Ser Glu Ala Ile Ala Ser Leu Ala Gln Asp Glu Thr Arg 995 1000 1005 Glu Tyr Arg Thr Tyr His Leu Val Asn Pro Phe Asp Asp Gly Ile 1010 1015 1020 Ser Leu Asp Arg Phe Val Glu Trp Leu Ile Glu Ala Gly Val Ser 1025 1030 1035 Leu Val Arg Val Gly Glu Tyr Gly Leu Trp Met Glu Arg Phe Lys 1040 1045 1050 Met Ala Leu Ser Val Leu Asp Asp Asp Asp Lys Arg Ala Ser Leu 1055 1060 1065 Leu Pro Leu Ile Asp Gly Phe Arg Ala Pro Glu Asp Pro Val Arg 1070 1075 1080 Gly Ser Arg Ile Asp Ser Thr Asp Leu His Gly Ala Leu Ala Gln 1085 1090 1095 Ala Gly Leu Ala Asp Arg Leu Gln Pro Leu Ser Gly Ser Ser Asp 1100 1105 1110 Ile Arg Trp Gly Ser Trp Gly Glu Ser Ala Gly Gly Glu Glu His 1115 1120 1125 Ala Glu Pro Val Val Val Pro Val Ala Val Ala Ala Gly Glu Ala 1130 1135 1140 Ala Val Glu Leu Asp Asp Pro Val His Gly Leu Gly Ala Thr Val 1145 1150 1155 Arg <210> 261 <211> 1126 <212> PRT <213> Artificial Sequence <220> <223> Myceligenerans xiligouense <400> 261 Met Ala Leu Ala Ser Thr Met Thr Ala Val Phe Glu Arg Tyr Thr Asp 1 5 10 15 Arg Pro Ala Leu Ala Glu Arg Thr Pro Val Pro Arg Ser Asp Glu Asp 20 25 30 Leu Thr Thr Phe Thr Ala Arg Ala Glu Asp Ser Tyr Asp Leu Leu Thr 35 40 45 Tyr Gly Glu Leu Ala Gln Arg Val Ser Ser Val Ala Ala Gln Leu Thr 50 55 60 Asp Asp Arg Arg Gly Ala Gly Arg Leu Thr Glu Gly Asp Met Thr Ala 65 70 75 80 Phe Leu Gly Phe Ala Gly Ala Asp Tyr Val Thr Ala Asp Leu Ala Cys 85 90 95 Asn Leu Ala Gly Ile Thr Thr Val Pro Leu Gln Thr Ser Ala Ser Leu 100 105 110 Asp Gln Gln Ala Ser Ile Leu Ala Thr Thr Ala Pro Arg Ala Leu Ala 115 120 125 Val Ser Val Ser Leu Leu Gly Arg Ala Val Glu Leu Leu Ala Ala Gln 130 135 140 Pro Thr Ile Thr Arg Leu Leu Val Leu Asp Tyr Arg Gly Gly Asp Pro 145 150 155 160 Asp His Val Arg Glu Leu Glu Ser Leu Asp Gly Thr Gly Val Pro Arg 165 170 175 Pro Glu Leu Leu Asp Leu Ser Gly Ala Gly Ala Ala Val Val Ala Pro 180 185 190 Trp Thr Glu Ser Arg Pro Val Met Leu Leu His Thr Ser Gly Ser Thr 195 200 205 Gly Thr Pro Lys Gly Ala Ile Tyr Pro Glu Arg Leu Val Thr Ala Met 210 215 220 Trp Gly Gly Asp Gly Trp Ser Glu Phe Phe Ala Ala Glu Pro Asp Val 225 230 235 240 Ser Thr Phe His Tyr Met Pro Met Ser His Val Ala Gly His Ser Ser 245 250 255 Val Arg Ser Thr Leu Ala Arg Gly Gly Leu Thr Tyr Phe Ala Ser Ser 260 265 270 Thr Asn Leu Ser Ser Leu Phe Asp Asp Leu Ala Leu Ala Arg Pro Thr 275 280 285 Glu Leu Ser Leu Val Pro Arg Val Cys Glu Leu Met Arg Gln Glu Phe 290 295 300 Arg Arg Arg Leu Gln Ala Ala Arg Ser His Thr Pro Asp Gly Asp Asp 305 310 315 320 Asp Val Leu Ala Ala Ser Val Arg Asp Glu Met Arg Thr Gln Val Leu 325 330 335 Gly Gly Asn Val Arg Trp Ala Ser Cys Thr Ser Ala Pro Ile Ser Ala 340 345 350 Glu Leu Lys Ala Phe Val Glu Asp Leu Leu Gln Ile Asp Val His Glu 355 360 365 Leu Tyr Gly Thr Thr Glu Ile Gly Gly Val Leu Ser Asn Gly Arg Phe 370 375 380 Leu Arg Pro Pro Val Leu Asp His Arg Leu Glu Asp Val Pro Glu Leu 385 390 395 400 Gly Tyr Tyr Ser Ser Asp Arg Pro Arg Ser Arg Gly Glu Leu Leu Ile 405 410 415 Arg Ser Thr Ser Thr Ile Pro Gly Tyr Tyr Gly Arg Pro Asp Leu Asp 420 425 430 Glu Gln Ile Phe Thr Asp Asp Gly Phe Tyr Arg Thr Gly Asp Ile Ala 435 440 445 Ser Val Asp Asp Thr Gly Thr Val Arg Ile Ile Asp Arg Lys Asn Ala 450 455 460 Ile Val Lys Leu Ser Gln Gly Glu Phe Val Ala Leu Pro Ser Leu Glu 465 470 475 480 Gly Thr Tyr Val Ser Arg Ser Glu Val Leu Arg Gln Val Tyr Leu His 485 490 495 Gly Asp Gly Gly Glu Ser Ser Ile Leu Ala Val Ala Val Pro Thr Asp 500 505 510 Glu Leu Val Asp Arg Leu Gly Gly Asp Val Pro Ala Ile Arg Glu His 515 520 525 Leu Leu Gln Glu Phe Arg Ala Ile Gly Ala Ala Glu Ala Leu Asn Ser 530 535 540 Tyr Glu Val Pro Arg Gly Val Leu Val Glu Leu Glu Pro Phe Ser Glu 545 550 555 560 Ser Asn Gly Leu Leu Ser Asp His Arg Lys Leu Val Arg Pro Glu Leu 565 570 575 Ala Arg Arg Tyr Gly Pro Val Leu Thr Ala Phe Tyr Glu Ser Leu Arg 580 585 590 Ser Ser Ser Asp Ala Leu Leu Glu Ser Leu Arg Asp Asn Ala Gly Asp 595 600 605 Ala Pro Thr Val Ala Thr Val Arg Asp Ala Ala Ala Ile Ala Ile Gly 610 615 620 Thr Ser Pro Ala Asp Ile Gly Ala Glu Asp Arg Phe Arg Asp Leu Gly 625 630 635 640 Gly Asp Ser Leu Thr Ala Val His Leu Ser Asn Leu Leu Glu Gln Ile 645 650 655 Phe Gly Val Arg Val Pro Val Asn Thr Ile Ala Gly Glu Ala Thr Thr 660 665 670 Ile Gly Arg Leu Ala Asp Leu Leu Asp Ala Arg Arg Asn Gly Asp Ala 675 680 685 Ala Val Val Ser Phe Glu Ser Val His Gly Asp Ala Pro Glu Leu Leu 690 695 700 Arg Ala Glu Asp Leu Arg Leu Ala Arg Phe Leu Gly Asp Gly Phe Thr 705 710 715 720 Pro Ala Pro Val Glu Ser Pro Thr Gly Asp Ala Pro Thr Val Leu Ile 725 730 735 Thr Gly Ala Asn Gly Phe Leu Gly Arg Phe Leu Cys Leu Glu Trp Leu 740 745 750 His Glu Val Ala Ala Thr Gly Gly Arg Val Ile Cys Ile Val Arg Ala 755 760 765 Ala Asp Asp Asp Glu Ala Tyr Glu Arg Leu Arg Arg Ala Phe Thr Ser 770 775 780 Asp Glu Arg Leu Leu Lys Thr Phe Asp Arg Phe Gly His Ala Leu Glu 785 790 795 800 Val Leu Ala Gly Asp Leu Ser Glu Pro Ala Leu Gly Leu Asp Ala Asp 805 810 815 Thr Trp Asp Arg Leu Ala Arg Asp Val His Arg Val Val His Ala Gly 820 825 830 Ala Met Val Asn His Ala Leu Pro Tyr Gln Glu Leu Phe Asp Ala Asn 835 840 845 Val Ala Gly Thr Ala Glu Val Val Arg Leu Ala Ala Ser Val Arg Leu 850 855 860 Lys Pro Val Ser Phe Val Ser Ser Ile Ala Thr Ala Leu Leu Ala Gly 865 870 875 880 Thr Glu Ser Pro Leu Asp Glu His Ala Asp Ile Arg Arg Ala Leu Pro 885 890 895 Ser Val Gly Thr Gly Thr Lys Asn Asn Val Glu Gly Tyr Ala Ala Thr 900 905 910 Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Ser Phe His 915 920 925 Leu Pro Val Thr Thr Phe Arg Ala Ser Met Ile Leu Ala His Ser Glu 930 935 940 Tyr Val Gly Gln Ile Asn Val Pro Asp Thr Phe Ser Arg Leu Val Tyr 945 950 955 960 Ser Leu Val Arg Thr Gly Val Val Pro Ser Ser Phe Tyr Ala Pro Gly 965 970 975 Gly Gly Arg Pro His Tyr Asp Gly Leu Pro Val Asp Val Val Ala Ser 980 985 990 Cys Ile Val Ala Leu Asp Ala Ala Gly Arg Gly Gly Tyr Ser Thr His 995 1000 1005 His Val Val Asn Pro Leu Asp Asp Gly Val Ser Leu Asp Thr Met 1010 1015 1020 Val Asp Trp Leu Thr Gly Leu Gly Val Glu Leu Thr Lys Val Asp 1025 1030 1035 Asp His Ala Asp Trp His Arg Arg Leu Gly Ala Gly Leu Arg Ala 1040 1045 1050 Leu Pro Glu Ser Glu Arg Arg Ala Ser Ile Leu Pro Leu Leu Asp 1055 1060 1065 Ser Phe Ser Ala Pro Glu Gln Pro Val Ala Gly Ser Ser Ile Ala 1070 1075 1080 Ser Pro Gly Phe Leu Ala Arg Val Arg Asp Leu Gly Leu Asp Thr 1085 1090 1095 Arg Ile Arg Ser Leu Asp Ala Arg Phe Val Glu Lys Ser Leu Ser 1100 1105 1110 Asp Leu Glu His Val His Gly Arg Pro Leu Arg Thr Ala 1115 1120 1125 <210> 262 <211> 1173 <212> PRT <213> Artificial Sequence <220> <223> Mycolicibacterium llatzerense <400> 262 Met Ser Asn Glu Glu Thr Ala Leu Thr Asp Glu Leu Thr Gln His Ile 1 5 10 15 Ala Asp Leu Cys Ala Thr Asp Pro Gln Leu Ala Ala Ala Arg Pro Leu 20 25 30 Ala Ala Val Gly Ala Ala Leu Asp Glu Pro Gly Ile Arg Leu Pro Asp 35 40 45 Met Ile Ser Ala Val Met Ala Ala Tyr Ala Asp Arg Pro Ala Leu Gly 50 55 60 Gln Arg Ala Val Glu Tyr Val Thr Asp Asp Ala Gly Arg Thr Val Ser 65 70 75 80 Arg Leu Leu Pro Arg Tyr Asp Thr Ile Thr Tyr Gly Glu Ala Trp Arg 85 90 95 Gln Ile Lys Ala Ile Gly Asn Ala Leu Leu Ala Gly Pro Asp Ala Val 100 105 110 Ala Ala Gly Asp Arg Val Ala Met Leu Gly Phe Thr Ser Ala Glu Phe 115 120 125 Thr Ile Ile Asp Thr Ala Leu Ala Arg Val Gly Val Val Ala Val Pro 130 135 140 Leu Gln Thr Ser Ala Pro Ala Glu Gln Leu Arg Pro Ile Leu Asp Glu 145 150 155 160 Thr Glu Pro Val Gly Leu Phe Ala Asp Val Lys Phe Leu Asp Glu Ala 165 170 175 Val Glu Leu Val Ser Gly Ser Gly Ala Ala Val Lys Arg Val Val Val 180 185 190 Phe Asp His His Ala Gln Val Asp Asp Asp Arg Ala Ala Val Glu Arg 195 200 205 Ala Ala Thr Gln Leu Ala Glu Arg Gly Val Val Val Glu Thr Leu Ala 210 215 220 Asp Leu Val Thr Arg Gly Thr Ala Leu Pro Thr Val Glu Pro Val Val 225 230 235 240 Ser Ala Asp Pro Asp Pro Leu Leu Val Leu Ile Tyr Thr Ser Gly Ser 245 250 255 Thr Gly Thr Pro Lys Gly Ala Met Tyr Pro Glu Arg Leu Val Ala Asn 260 265 270 Ala Trp Arg Thr Gly Leu Thr His Gln Gln Pro Ala Leu Pro Ser Ile 275 280 285 Val Leu Ser Phe Leu Pro Met Ser His Met Met Gly Arg Gly Thr Val 290 295 300 Tyr Arg Thr Leu Ala His Gly Gly Thr Val Tyr Phe Ala Ala Lys Ser 305 310 315 320 Asp Leu Ser Thr Leu Leu Glu Asp Ile Ala Leu Val Arg Pro Thr Gln 325 330 335 Met Thr Phe Val Pro Arg Val Trp Glu Met Ile His Gln Glu Val Gln 340 345 350 Ser Glu Val Asp Arg Arg Ala Leu Asp Gly Val Ser Glu Gln Gln Val 355 360 365 Leu Asp Glu Arg Ser Val Ser Leu Ile Gly Gly Arg Gln Leu Val Ala 370 375 380 Met Thr Gly Ser Ala Pro Ile Ser Pro Glu Leu Lys Ala Trp Val Gln 385 390 395 400 Lys Phe Leu Gly Leu Glu Leu Met Glu Ala Tyr Gly Ser Thr Glu Ala 405 410 415 Gly Gly Val Met Ile Ser Gly His Leu Ser Arg Pro Pro Val Leu Asp 420 425 430 Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Leu Ser Thr Asp Arg 435 440 445 Pro His Pro Arg Gly Glu Leu Leu Leu Lys Ser Thr Asp Leu Ile Pro 450 455 460 Gly Tyr Tyr Lys Arg Pro Asp Val Thr Ala Asp Val Phe Asp Val Asp 465 470 475 480 Gly Phe Tyr Arg Thr Gly Asp Ile Val Ala Glu Leu Gly Pro Asp His 485 490 495 Leu Gln Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys Leu Ala Gln Gly 500 505 510 Glu Phe Val Thr Val Ser Lys Leu Glu Ala Ala Phe Gly Thr Ser Pro 515 520 525 Leu Ile Arg Gln Ile Tyr Val Tyr Gly Asn Ser Ser Arg Ser Tyr Leu 530 535 540 Leu Ala Val Ile Val Pro Thr Ser Asp Ala Leu Ala Gly Val Ser Gly 545 550 555 560 Ala Glu Ala Leu Arg Pro Glu Leu Ala Asp Ala Leu Gln Thr Val Ala 565 570 575 Arg Glu Ser Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp Phe Ile Ile 580 585 590 Glu Thr Glu Pro Phe Ser Leu Glu Asn Gly Leu Leu Thr Gly Val Arg 595 600 605 Lys Leu Ala Trp Pro Lys Leu Lys Ala Arg Tyr Gly Ala Glu Leu Glu 610 615 620 Gln Leu Tyr Thr Glu Leu Ala Glu Gly Gln Ala Ala Glu Leu Arg Ala 625 630 635 640 Leu Arg Ser Leu Arg Ala Ser Asp Ala Pro Val Leu Glu Thr Val Leu 645 650 655 Arg Ala Val Gly Ala Thr Leu Gly Ala Ala Ser Ser Asp Val Ala Gly 660 665 670 Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr 675 680 685 Phe Gly Asn Leu Leu Glu Glu Ile Phe Glu Val Glu Val Pro Val Gly 690 695 700 Val Ile Val Ser Pro Ala Thr Asp Leu Ala Gly Val Ala Ala Tyr Val 705 710 715 720 Glu Gly Glu Arg Ala Pro Gly Ser Lys Arg Pro Thr Phe Ser Thr Val 725 730 735 His Gly Arg Gly Ala Thr Glu Ala Arg Ala Ala Asp Leu Thr Leu Asp 740 745 750 Lys Phe Ile Asp Ala Ala Thr Leu Ala Ala Ala Pro Ser Leu Pro Gly 755 760 765 Pro Val Ser Glu Val Arg Thr Val Leu Leu Thr Gly Ala Thr Gly Phe 770 775 780 Leu Gly Arg Tyr Leu Ala Leu Glu Trp Leu Glu Arg Met Asp Leu Val 785 790 795 800 Asp Gly Lys Val Ile Cys Leu Val Arg Gly Lys Ser Asp Ala Asp Ala 805 810 815 Arg Ala Arg Leu Asp Ala Thr Phe Asp Ser Gly Asp Pro Lys Leu Leu 820 825 830 Gln His Tyr Arg Ser Leu Ser Asp His Leu Glu Val Ile Ala Gly Asp 835 840 845 Lys Gly Glu Ala Asn Leu Gly Leu Pro Gln Glu Val Trp Gln Arg Leu 850 855 860 Ala Asp Thr Val Asp Phe Ile Val Asp Pro Ala Ala Leu Val Asn His 865 870 875 880 Val Leu Pro Tyr Ser Glu Leu Phe Gly Pro Asn Ala Leu Gly Thr Ala 885 890 895 Glu Leu Ile Arg Ile Ala Leu Thr Thr Arg Ile Lys Pro Phe Ala Tyr 900 905 910 Val Ser Thr Ile Ala Val Gly Gly Gly Val Ala Pro Gly Gln Phe Val 915 920 925 Glu Asp Ala Asp Val Arg Val Met Ser Ala Val Arg Ser Val Asp Asp 930 935 940 Ser Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu 945 950 955 960 Leu Arg Glu Ala Asn Asp Leu Cys Gly Leu Pro Val Ser Val Phe Arg 965 970 975 Cys Asp Met Ile Leu Ala Asp Thr Thr Tyr Ala Gly Gln Leu Asn Leu 980 985 990 Pro Asp Met Phe Thr Arg Met Met Phe Ser Leu Val Ala Thr Gly Ile 995 1000 1005 Ala Pro Tyr Ser Phe Tyr Glu Leu Ala Thr Asp Gly Asn Arg Gln 1010 1015 1020 Arg Ala His Tyr Asp Gly Leu Pro Val Glu Phe Val Ser Glu Ser 1025 1030 1035 Ile Ser Thr Leu Ala Val Gln Val Ala Ala Gly Glu Ser Asp Ser 1040 1045 1050 Thr Phe Glu Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Ile 1055 1060 1065 Gly Met Asp Glu Phe Val Asp Trp Leu Ile Glu Ala Gly Tyr Ser 1070 1075 1080 Ile Ala Arg Val Asp Asp Tyr Ala Asp Trp Leu Ala Arg Phe Glu 1085 1090 1095 Thr Gly Leu Arg Gly Leu Pro Asp Arg Gln Arg Gln Ala Ser Leu 1100 1105 1110 Leu Pro Leu Leu His Asn Tyr Gln Gln Pro Ser Tyr Pro Val Pro 1115 1120 1125 Gly Ser Ile Ala Pro Val Glu Arg Phe Arg Ala Ala Val Gln Asn 1130 1135 1140 Ala Lys Val Gly Ala Asp Lys Asp Ile Pro His Ile Gly Ala Pro 1145 1150 1155 Val Ile Val Lys Tyr Ile Thr Asp Leu Gln Leu Leu Gly Leu Leu 1160 1165 1170 <210> 263 <211> 1181 <212> PRT <213> Artificial Sequence <220> <223> Rhodococcus fascians D188 <400> 263 Met Thr Arg Thr Ile Ala Met Lys Ser Thr Val Ala Val Asp Ser Glu 1 5 10 15 His Asp Arg Asp Ile Arg Gln Arg Asp Arg Phe Gln His Leu His Asp 20 25 30 Ser Asp Pro Glu Phe Arg Ala Ala Glu Pro Asp Arg Ser Val Ala Asp 35 40 45 Ala Ala Arg Glu Leu Ala Pro Asn Leu Ala Arg Val Val Ala Glu Ile 50 55 60 Met Thr Arg Tyr Ala Asp Arg Pro Ala Leu Gly Arg Arg Ala Arg Thr 65 70 75 80 Ile Glu Asp Thr Asp Gly Ser Thr Thr Ala Arg Leu Leu Pro Arg Phe 85 90 95 Asp Thr Val Thr Tyr Gly Gln Ala Trp Ala Asp Ala Gly Ala Leu Ala 100 105 110 Ser Ala Leu Gly His Asp Asp Gly Gly Ile Ala Ala Gly Asp Phe Val 115 120 125 Ala Thr Leu Gly Phe Ala Gly Ile Asp Tyr Val Ile Thr Glu Leu Ala 130 135 140 Thr Ile Arg Val Gly Ala Val Ala Val Pro Leu Gln Ala Gly Ala Thr 145 150 155 160 Ala Gly Gln Leu Arg Ala Ile Val Asp Glu Val Glu Pro Val Val Leu 165 170 175 Ala Ser Asp Val Asp Asn Leu Ala Val Ala Met Glu Val Ala Gly His 180 185 190 Cys Arg Ser Ile Arg Thr Val Val Val Leu Asp Tyr Asp Asp Arg Ile 195 200 205 Asp Ala Asp Thr Arg Ala Leu Thr Ser Ala Arg Glu Gly Val His Gly 210 215 220 Ser Gly Ile Ala Val Arg Pro Leu Thr Glu Leu Val Asp Glu Gly Ser 225 230 235 240 Arg Leu Pro Gln Val Pro Leu Phe Asp Val Glu Asp Pro Glu Arg Leu 245 250 255 Ala Ala Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala 260 265 270 Met His Thr Glu Gln Ile Val Ser Gly Ala Trp Thr Gly Ala Trp His 275 280 285 Arg Thr Gly Ala Ser Ser Glu Gly Val Asp Glu Pro Ala Phe Pro Val 290 295 300 Ile Thr Leu Asp Tyr Leu Pro Met Ser His Leu Ala Gly Arg Gly Leu 305 310 315 320 Val Phe Ser Thr Leu Ala Ala Gly Gly Thr Val His Phe Ala Gly Ser 325 330 335 Ser Asp Leu Ser Thr Leu Phe Glu Asp Phe Ala Leu Ala Arg Pro Thr 340 345 350 Leu Ala Leu Leu Ile Pro Arg Val Cys Glu Met Ile Arg His Thr Val 355 360 365 Leu Ala Glu Ile Asp Arg Ala Val Asp Gly Thr Asp Ala Gly Glu His 370 375 380 Glu Gln Ile Ser Arg Gly Val Leu Glu Arg Val Arg Ser Glu Gln Phe 385 390 395 400 Gly Gly Arg Ile Leu Ala Ala Met Val Gly Thr Ala Pro Ile Ala Ala 405 410 415 Glu Val Lys Asp Phe Val Thr Asp Leu Leu Asp Val Arg Val Arg Asp 420 425 430 Asn Tyr Gly Ser Thr Glu Ala Gly Met Val Leu Leu Asp Gly Ile Val 435 440 445 Ala Arg Pro Pro Val Leu Glu Tyr Lys Leu Asp Asp Val Pro Glu Leu 450 455 460 Gly Tyr Phe Ser Thr Asp Thr Pro His Pro Arg Gly Glu Leu Leu Leu 465 470 475 480 Lys Thr Thr Ser Ile Ile Pro Gly Tyr Tyr Lys Arg Pro Asp Val Thr 485 490 495 Ala Asp Val Phe Asp Ser Asp Gly Phe Tyr Arg Thr Gly Asp Val Val 500 505 510 Ala Glu Leu Glu Pro Asp Arg Leu Ala Tyr Val Asp Arg Arg Lys Asn 515 520 525 Val Leu Lys Leu Ala Gln Gly Glu Phe Val Ala Leu Ala Arg Leu Glu 530 535 540 Ala Val Phe Gly Thr Ser Glu Leu Val Asp Gln Ile Phe Leu Tyr Gly 545 550 555 560 Asn Ser Gln Arg Ser Tyr Leu Leu Ala Ile Val Val Pro Ala His Ala 565 570 575 Asn Ser Thr Ala Gly Ala Ile Met Glu Ser Leu Gln Arg Ile Ala Arg 580 585 590 Thr Glu Ser Leu Asn Ser Tyr Glu Ile Pro Arg Glu Val Val Leu Glu 595 600 605 Arg Glu Pro Phe Thr Gln Asp Asn Gly Leu Leu Ser Gly Ala Gly Lys 610 615 620 Gln Leu Arg Pro Lys Leu Val Glu Arg Tyr Gly Asp Glu Leu Glu Arg 625 630 635 640 Arg Tyr Ala Glu Leu Glu Ser Gly Gln Thr Asp Arg Leu Arg Glu Leu 645 650 655 Arg Arg Ser Gly Ala Gln Ala Pro Val Leu Ala Thr Val Gly Asp Ala 660 665 670 Ala Gln Ala Leu Leu Gly Cys Ser Gly Ala Asp Ile Arg Pro Asp Ala 675 680 685 His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu Thr Phe Ser 690 695 700 Thr Leu Leu Arg Asp Ile Tyr Asp Val Asp Val Pro Val Gly Val Ile 705 710 715 720 Thr Gly Pro Ala Met Asp Leu Ala Ala Leu Ala Asp Tyr Ile Thr Ser 725 730 735 Ala Ile Asp Asn Asp Ser Asp Thr Ala Thr Phe Ala Ser Val His Gly 740 745 750 Arg Asp Ala Ser Val Ala Leu Ala Ser Asp Leu Thr Leu Ser Ala Phe 755 760 765 Leu Asp Ala Ser Leu Leu Asp Ala Ala His Arg Ile Pro Gly Pro Arg 770 775 780 Pro Val Thr Asn Thr Val Leu Leu Thr Gly Ala Asn Gly Tyr Leu Gly 785 790 795 800 Arg Phe Leu Cys Leu Glu Trp Leu Glu Lys Met Ala Ala Ala Gly Gly 805 810 815 Arg Val Ile Cys Leu Val Arg Gly Arg Ser Asp Ala Asp Ala Arg Gly 820 825 830 Arg Leu Asp Ala Ala Phe Asp Ser Gly Asp Ala Thr Leu Ser Asp Arg 835 840 845 Tyr Arg Ala Leu Ala Asp Ala Ala Leu Asp Val Ile Ala Gly Asp Leu 850 855 860 Gly Thr Pro Arg Phe Gly Leu Thr Asp Asp Val Trp Glu Glu Leu Ser 865 870 875 880 Arg Arg Val Asp Arg Val Val His Pro Ala Ala Leu Val Asn His Ala 885 890 895 Leu Pro Tyr Glu His Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu 900 905 910 Val Ile Arg Leu Ala Leu Thr Asp His Ile Lys Pro Val Thr Tyr Leu 915 920 925 Ser Thr Val Ala Val Ala Val Gly Val Asp Asp Phe His Glu Asn Gly 930 935 940 Asp Ile Arg Val Asp Ser Ala Gln Arg Ala Val Asp Glu Thr Tyr Ala 945 950 955 960 Asn Gly Tyr Gly Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Asn 965 970 975 Ala Phe Asp Glu Tyr Ser Leu Pro Val Ser Val Phe Arg Ser Asp Met 980 985 990 Ile Leu Ala His Ser Thr Trp Ser Gly Gln Leu Asn Val Pro Asp Val 995 1000 1005 Phe Thr Arg Leu Ile Leu Ser Val Val Ala Thr Gly Leu Ala Pro 1010 1015 1020 Arg Ser Phe Tyr Ala Thr Asp Thr Gly Ala Pro Thr Asp Glu Gln 1025 1030 1035 Gly Arg Pro Leu Ala His Tyr Asp Gly Leu Pro Ala Asp Phe Ser 1040 1045 1050 Ala Ala Ala Ile Thr Ser Ile Ala Gly Asp Asp Val Ala Gly Tyr 1055 1060 1065 Arg Thr Phe Asp Ile Leu Asn Pro His Asp Asp Asp Ile Ser Leu 1070 1075 1080 Asp Thr Phe Val Asp Trp Leu Arg Glu Ala Gly Cys Thr Ile Asp 1085 1090 1095 Ile Val Asp Asp Tyr Asp Glu Trp Phe Glu Arg Phe Ser Ala Ala 1100 1105 1110 Val Gln Glu Leu Pro Glu Lys Gln Arg Ser His Ser Leu Leu Pro 1115 1120 1125 Leu Ile His Ser Tyr Ala His Pro Gln His Pro Ser Ser Gly Ala 1130 1135 1140 Ile Leu Pro Ala Glu Glu Phe Ala Ser Ala Val Gly Asp Ile Pro 1145 1150 1155 His Leu Gly Arg Glu Leu Ile Glu Lys Tyr Leu Ala Asp Leu Val 1160 1165 1170 Ala Leu Gly Leu Val Ala Lys Ser 1175 1180 <210> 264 <211> 1178 <212> PRT <213> Artificial Sequence <220> <223> Mycobacteroides abscessus subsp. abscessus <400> 264 Met Thr Glu Thr Ile Ser Thr Ala Ala Val Pro Thr Thr Asp Leu Glu 1 5 10 15 Glu Gln Val Lys Arg Arg Ile Glu Gln Val Val Ser Asn Asp Pro Gln 20 25 30 Leu Ala Ala Leu Leu Pro Glu Asp Ser Val Thr Glu Ala Val Asn Glu 35 40 45 Pro Asp Leu Pro Leu Val Glu Val Ile Arg Arg Leu Leu Glu Gly Tyr 50 55 60 Gly Asp Arg Pro Ala Leu Gly Gln Arg Ala Phe Glu Phe Val Thr Gly 65 70 75 80 Asp Asp Gly Ala Thr Val Ile Ala Leu Lys Pro Glu Tyr Thr Thr Val 85 90 95 Ser Tyr Arg Glu Leu Trp Glu Arg Ala Glu Ala Ile Ala Ala Ala Trp 100 105 110 His Glu Gln Gly Ile Arg Asp Gly Asp Phe Val Ala Gln Leu Gly Phe 115 120 125 Thr Ser Thr Asp Phe Ala Ser Leu Asp Val Ala Gly Leu Arg Leu Gly 130 135 140 Thr Val Ser Val Pro Leu Gln Thr Gly Ala Ser Leu Gln Gln Arg Asn 145 150 155 160 Ala Ile Leu Glu Glu Thr Arg Pro Ala Val Phe Ala Ala Ser Ile Glu 165 170 175 Tyr Leu Asp Ala Ala Val Asp Ser Val Leu Ala Thr Pro Ser Val Arg 180 185 190 Leu Leu Ser Val Phe Asp Tyr His Ala Glu Val Asp Ser Gln Arg Glu 195 200 205 Ala Leu Glu Ala Val Arg Ala Arg Leu Glu Ser Ala Gly Arg Thr Ile 210 215 220 Val Val Glu Ala Leu Ala Glu Ala Leu Ala Arg Gly Arg Asp Leu Pro 225 230 235 240 Ala Ala Pro Leu Pro Ser Ala Asp Pro Asp Ala Leu Arg Leu Leu Ile 245 250 255 Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys Gly Ala Met Tyr Pro Gln 260 265 270 Trp Leu Val Ala Asn Leu Trp Gln Lys Lys Trp Leu Thr Asp Asp Val 275 280 285 Ile Pro Ser Ile Gly Val Asn Phe Met Pro Met Ser His Leu Ala Gly 290 295 300 Arg Leu Thr Leu Met Gly Thr Leu Ser Gly Gly Gly Thr Ala Tyr Tyr 305 310 315 320 Ile Ala Ser Ser Asp Leu Ser Thr Phe Phe Glu Asp Ile Ala Leu Ile 325 330 335 Arg Pro Ser Glu Val Leu Phe Val Pro Arg Val Val Glu Met Val Phe 340 345 350 Gln Arg Phe Gln Ala Glu Leu Asp Arg Ser Leu Ala Pro Gly Glu Ser 355 360 365 Asn Ser Glu Ile Ala Glu Arg Ile Lys Val Arg Ile Arg Glu Gln Asp 370 375 380 Phe Gly Gly Arg Val Leu Ser Ala Gly Ser Gly Ser Ala Pro Leu Ser 385 390 395 400 Pro Glu Met Thr Glu Phe Met Glu Ser Leu Leu Gln Val Pro Leu Arg 405 410 415 Asp Gly Tyr Gly Ser Thr Glu Ala Gly Gly Val Trp Arg Asp Gly Val 420 425 430 Leu Gln Arg Pro Pro Val Thr Asp Tyr Lys Leu Val Asp Val Pro Glu 435 440 445 Leu Gly Tyr Phe Thr Thr Asp Ser Pro His Pro Arg Gly Glu Leu Arg 450 455 460 Leu Lys Ser Glu Thr Met Phe Pro Gly Tyr Tyr Lys Arg Pro Glu Thr 465 470 475 480 Thr Ala Asp Val Phe Asp Asp Glu Gly Tyr Tyr Lys Thr Gly Asp Val 485 490 495 Val Ala Glu Leu Gly Pro Asp His Leu Lys Tyr Leu Asp Arg Val Lys 500 505 510 Asn Val Leu Lys Leu Ala Gln Gly Glu Phe Val Ala Val Ser Lys Leu 515 520 525 Glu Ala Ala Tyr Thr Gly Ser Pro Leu Val Arg Gln Ile Phe Val Tyr 530 535 540 Gly Asn Ser Glu Arg Ser Phe Leu Leu Ala Val Val Val Pro Thr Pro 545 550 555 560 Glu Val Leu Glu Arg Tyr Ala Asp Ser Pro Asp Ala Leu Lys Pro Leu 565 570 575 Ile Gln Asp Ser Leu Gln Gln Val Ala Lys Asp Ala Glu Leu Gln Ser 580 585 590 Tyr Glu Ile Pro Arg Asp Phe Ile Val Glu Thr Val Pro Phe Thr Val 595 600 605 Glu Ser Gly Leu Leu Ser Asp Ala Arg Lys Leu Leu Arg Pro Lys Leu 610 615 620 Lys Asp His Tyr Gly Glu Arg Leu Glu Ala Leu Tyr Ala Glu Leu Ala 625 630 635 640 Glu Ser Gln Asn Glu Arg Leu Arg Gln Leu Ala Arg Glu Ala Ala Thr 645 650 655 Arg Pro Val Leu Glu Thr Val Thr Asp Ala Ala Ala Ala Leu Leu Gly 660 665 670 Ala Ser Ser Ser Asp Leu Ala Pro Asp Val Arg Phe Ile Asp Leu Gly 675 680 685 Gly Asp Ser Leu Ser Ala Leu Ser Tyr Ser Glu Leu Leu Arg Asp Ile 690 695 700 Phe Glu Val Asp Val Pro Val Gly Val Ile Asn Ser Val Ala Asn Asp 705 710 715 720 Leu Ala Ala Ile Ala Arg His Ile Glu Ala Gln Arg Thr Gly Ala Ala 725 730 735 Thr Gln Pro Thr Phe Ala Ser Val His Gly Lys Asp Ala Thr Val Ile 740 745 750 Thr Ala Gly Glu Leu Thr Leu Asp Lys Phe Leu Asp Glu Ser Leu Leu 755 760 765 Lys Ala Ala Lys Asp Val Gln Pro Ala Thr Ala Asp Val Lys Thr Val 770 775 780 Leu Val Thr Gly Gly Asn Gly Trp Leu Gly Arg Trp Leu Val Leu Asp 785 790 795 800 Trp Leu Glu Arg Leu Ala Pro Asn Gly Gly Lys Val Tyr Ala Leu Ile 805 810 815 Arg Gly Ala Asp Ala Glu Ala Ala Arg Ala Arg Leu Asp Ala Val Tyr 820 825 830 Glu Ser Gly Asp Pro Lys Leu Ser Ala His Tyr Arg Gln Leu Ala Gln 835 840 845 Gln Ser Leu Glu Val Ile Ala Gly Asp Phe Gly Asp Gln Asp Leu Gly 850 855 860 Leu Ser Gln Glu Val Trp Gln Lys Leu Ala Lys Asp Val Asp Leu Ile 865 870 875 880 Val His Ser Gly Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu 885 890 895 Phe Gly Pro Asn Val Ala Gly Thr Ala Glu Ile Ile Lys Leu Ala Ile 900 905 910 Ser Glu Arg Leu Lys Pro Val Thr Tyr Leu Ser Thr Val Gly Ile Ala 915 920 925 Asp Gln Ile Pro Val Thr Glu Phe Glu Glu Asp Ser Asp Val Arg Val 930 935 940 Met Ser Ala Glu Arg Gln Ile Asn Asp Gly Tyr Ala Asn Gly Tyr Gly 945 950 955 960 Asn Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu 965 970 975 Ala Gly Leu Pro Val Arg Val Phe Arg Ser Asp Met Ile Leu Ala His 980 985 990 Ser Asp Tyr His Gly Gln Leu Asn Val Thr Asp Val Phe Thr Arg Ser 995 1000 1005 Ile Gln Ser Leu Leu Leu Thr Gly Val Ala Pro Ala Ser Phe Tyr 1010 1015 1020 Glu Leu Asp Ala Asp Gly Asn Arg Gln Arg Ala His Tyr Asp Gly 1025 1030 1035 Val Pro Gly Asp Phe Thr Ala Ala Ser Ile Thr Ala Ile Gly Gly 1040 1045 1050 Val Asn Val Val Asp Gly Tyr Arg Ser Phe Asp Val Phe Asn Pro 1055 1060 1065 His His Asp Gly Val Ser Met Asp Thr Phe Val Asp Trp Leu Ile 1070 1075 1080 Asp Ala Gly Tyr Lys Ile Ala Arg Ile Asp Asp Tyr Asp Gln Trp 1085 1090 1095 Leu Ala Arg Phe Glu Leu Ala Leu Lys Gly Leu Pro Glu Gln Gln 1100 1105 1110 Arg Gln Gln Ser Val Leu Pro Leu Leu Lys Met Tyr Glu Lys Pro 1115 1120 1125 Gln Pro Ala Ile Asp Gly Ser Ala Leu Pro Thr Ala Glu Phe Ser 1130 1135 1140 Arg Ala Val His Glu Ala Lys Val Gly Asp Ser Gly Glu Ile Pro 1145 1150 1155 His Val Thr Lys Glu Leu Ile Leu Lys Tyr Ala Ser Asp Ile Gln 1160 1165 1170 Leu Leu Gly Leu Val 1175 <210> 265 <211> 459 <212> PRT <213> Artificial Sequence <220> <223> Escherichia coli <400> 265 Met Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser Ala His 1 5 10 15 Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met Lys 20 25 30 Ala Leu Asn Arg Glu Val Ile Glu Tyr Phe Lys Glu His Val Asn Pro 35 40 45 Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly 50 55 60 Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln 65 70 75 80 Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val 85 90 95 Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu Ala 100 105 110 Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met 115 120 125 Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser 130 135 140 Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu 145 150 155 160 Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr 165 170 175 Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala 180 185 190 Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg 195 200 205 His Val Pro Phe Gly Asn Ile Glu Ala Met Arg Thr Ala Leu Asn Glu 210 215 220 Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile 225 230 235 240 Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Pro Gly Tyr Leu Thr Ala 245 250 255 Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp Glu 260 265 270 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His 275 280 285 Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly 290 295 300 Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe Ser 305 310 315 320 Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn 325 330 335 Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu 340 345 350 Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp 355 360 365 Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp Leu Val Gln Glu Ala 370 375 380 Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu Ile 385 390 395 400 Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala 405 410 415 Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr 420 425 430 Leu Thr Ile Glu Gln Cys Glu Leu Val Ile Lys Ala Ala Arg Lys Ala 435 440 445 Leu Ala Ala Met Arg Val Ser Val Glu Glu Ala 450 455 <210> 266 <211> 484 <212> PRT <213> Artificial Sequence <220> <223> Candidatus melainabacteria <400> 266 Met Gly Asn Ser Ile Asn His Leu Asn Asn Ala Tyr Ser Gln Lys Leu 1 5 10 15 Ser Gly Ala Glu Gly Ala Val Glu Phe Arg Asp Glu Gly Val Tyr Thr 20 25 30 Tyr Asp Asn Gln Gly Arg Arg Tyr Leu Asp Cys Leu Gly Gly Phe Gly 35 40 45 Ile Phe Asn Val Gly His Arg His Pro Lys Val Ile Asn Ala Val Lys 50 55 60 Ala Gln Leu Asp Gln Val Ala Leu His Ser Gln Glu Leu Ile Asn Pro 65 70 75 80 Trp Ala Ala His Leu Ala Ser Gln Leu Ala Ala Val Ala Pro Gly Asp 85 90 95 Leu Gln Tyr Cys Phe Phe Gly Asn Ser Gly Ser Glu Ala Val Glu Gly 100 105 110 Ala Ile Lys Leu Ala Arg Leu Tyr Thr Gly Lys Thr Glu Ile Ile Ser 115 120 125 Thr Lys Asn Ala Tyr His Gly Val Ser Met Gly Ala Leu Ser Ala Thr 130 135 140 Gly Arg Asp Val Phe Arg Lys Pro Phe Glu Pro Leu Leu Asn Gly Phe 145 150 155 160 Val His Val Pro Phe Gly Asp Ile Ala Ala Leu Glu Ala Ala Ile Asn 165 170 175 Glu Asn Thr Ala Ala Val Ile Leu Glu Pro Ile Gln Gly Glu Gly Gly 180 185 190 Ile Asn Val Pro Pro Thr Gly Tyr Leu Arg Lys Val Arg Gln Leu Thr 195 200 205 Arg Lys Lys Gly Val Leu Leu Ile Leu Asp Glu Val Gln Thr Gly Met 210 215 220 Gly Arg Thr Gly Arg Met Phe Ala Cys Glu His Glu Gly Val Val Pro 225 230 235 240 Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro Ile 245 250 255 Gly Cys Phe Met Ala Ser Ala Lys Val Trp Lys Val Leu Glu Pro Asn 260 265 270 Pro Thr Ile His Asn Ser Thr Phe Gly Gly Asn Pro Leu Ala Cys Ser 275 280 285 Ala Ala Ser Ala Cys Val Glu Val Leu Leu Glu Glu His Leu Pro Ala 290 295 300 Arg Ala Ala Val Met Gly Asn Tyr Phe Met Arg Lys Leu Asn Glu Leu 305 310 315 320 Lys Glu Arg Tyr Pro Ala His Val Ala Asp Val Arg Gly Lys Gly Leu 325 330 335 Leu Ile Gly Leu Glu Phe Thr Ser Lys Glu Leu Arg Glu Ala Val Gln 340 345 350 Val Glu Leu Phe Tyr Arg Gly Val Leu Val Ala Gly Thr Leu Asn Ala 355 360 365 Asn Arg Thr Phe Arg Ile Glu Pro Pro Leu Ile Ile Thr Glu Ser Gln 370 375 380 Ile Asn Phe Met Ile Glu Ala Leu Glu Ser Ile Leu Met Glu Ile Gly 385 390 395 400 Ala Asp Glu Leu Ser Glu Met Ala Ala Gln Ala Asn Ala Glu Ile Gly 405 410 415 Ala Ala Ala Lys Thr Ala Arg Arg Arg Ser Arg Lys Val Glu Ala Pro 420 425 430 Arg Ala Asp Ile Ala Pro Glu Pro Ala Gly Arg Val Leu Ala Pro Val 435 440 445 Lys Ala Ala Ala Thr Ser Arg Gly Ala Lys Ala Lys Thr Ala Lys Arg 450 455 460 Lys Pro Lys Lys Gly Lys Lys Val Lys Ala Lys Ser Val Tyr Lys Ala 465 470 475 480 Lys Gly Arg Lys <210> 267 <211> 476 <212> PRT <213> Artificial Sequence <220> <223> Enterobacteriaceae <400> 267 Met Gln Tyr Leu Thr Gln Tyr His Val Ile Arg Asp Pro Arg Glu His 1 5 10 15 Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Thr Ala 20 25 30 His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met 35 40 45 Lys Gln Leu Asn Arg Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn 50 55 60 Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr 65 70 75 80 Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr 85 90 95 Gln Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn 100 105 110 Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu 115 120 125 Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala 130 135 140 Met Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr 145 150 155 160 Ser Phe Phe Ser Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Ile Lys 165 170 175 Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala 180 185 190 Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr 195 200 205 Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe 210 215 220 Arg His Val Pro Phe Gly Asp Ile Asn Ala Met Arg Thr Val Leu Ser 225 230 235 240 Glu Cys Arg Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro 245 250 255 Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Pro 260 265 270 Ala Val Arg Gln Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Leu Asp 275 280 285 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu 290 295 300 His Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly 305 310 315 320 Gly Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe 325 330 335 Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 340 345 350 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu 355 360 365 Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu 370 375 380 Asp Gly Phe Arg Gln Leu Gly Arg Glu Tyr Pro Asp Leu Val Gln Glu 385 390 395 400 Ala Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu 405 410 415 Ile Gly Tyr Ser Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val 420 425 430 Ala Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Ile Glu Pro Pro Leu 435 440 445 Thr Leu Thr Ile Glu Gln Cys Glu Gln Val Leu Lys Ala Ala Arg Lys 450 455 460 Ala Leu Ala Ala Leu Arg Val Ser Val Glu Glu Ala 465 470 475 <210> 268 <211> 503 <212> PRT <213> Artificial Sequence <220> <223> Citrobacter <400> 268 Met Arg Leu Asn Val Val Gln Ala Arg Ser Ser Leu Val Phe Ile Pro 1 5 10 15 Ile Phe Val Lys Arg Val Gly Met Ala Gln Ser Leu Gln Tyr Leu Ile 20 25 30 Gln Tyr His Val Ile Arg Glu Leu Arg Glu His Ile Leu Asn Arg Leu 35 40 45 Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser Ala His Ala Leu Asn Leu 50 55 60 Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met Lys Ala Leu Asn Arg 65 70 75 80 Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn Pro Gly Phe Leu Glu 85 90 95 Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly Ala Val Glu Trp 100 105 110 Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln Gly Gln Glu Phe 115 120 125 Val Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val Gly His Arg Asn 130 135 140 Pro Val Val Val Ser Ala Val Gln Asn Gln Leu Ala Lys Gln Pro Leu 145 150 155 160 His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met Leu Ala Lys Thr 165 170 175 Leu Ala Ala Leu Ala Pro Gly Lys Leu Lys Tyr Ser Phe Phe Ser Asn 180 185 190 Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu Ala Lys Ala Tyr 195 200 205 Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr Ser Gly Ala Phe 210 215 220 His Gly Lys Ser Leu Gly Ser Leu Ser Ala Thr Ala Lys Ser Thr Phe 225 230 235 240 Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg His Val Pro Phe 245 250 255 Gly Asp Ile Asp Ala Met Arg Thr Val Leu Ser Glu Cys Lys Lys Thr 260 265 270 Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile Gln Gly Glu Gly 275 280 285 Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Thr Ala Val Arg Lys Leu 290 295 300 Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp Glu Val Gln Thr Gly 305 310 315 320 Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His Glu Asn Val Gln 325 330 335 Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro 340 345 350 Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe Ser Val Leu Phe Asp 355 360 365 Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn Pro Leu Ser Cys 370 375 380 Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu Gln Asn Leu Pro 385 390 395 400 Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp Gly Phe Arg His 405 410 415 Leu Ala Arg Glu Tyr Pro Asp Leu Val His Asp Val Arg Gly Lys Gly 420 425 430 Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu Ile Gly Tyr Ser Phe 435 440 445 Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala Gly Thr Leu Asn 450 455 460 Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr Leu Thr Ile Glu 465 470 475 480 Gln Cys Glu Leu Val Leu Arg Ser Thr Arg Lys Ala Leu Ala Ala Leu 485 490 495 Arg Val Ser Val Glu Gln Val 500 <210> 269 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Enterobacteriaceae <400> 269 Met Arg Cys Phe Leu Val Phe Ile Pro Ile Phe Ala Lys Arg Ala Gly 1 5 10 15 Met Ala Gln Ser Leu Gln Tyr Leu Asn Gln Tyr His Val Ile Arg Glu 20 25 30 Leu Arg Glu His Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu 35 40 45 Ala Cys Ser Ala His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp 50 55 60 His Glu Glu Met Lys Ser Leu Asn Lys Glu Val Ile Glu Tyr Phe Lys 65 70 75 80 Glu His Val Asn Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala 85 90 95 Gly Gly Asp Tyr Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr 100 105 110 Leu Val Asp Thr Gln Gly Gln Glu Phe Val Asp Cys Leu Gly Gly Phe 115 120 125 Gly Ile Phe Asn Val Gly His Arg Asn Pro Val Val Val Ser Ala Val 130 135 140 Gln Asn Gln Leu Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp 145 150 155 160 Pro Leu Arg Ala Met Leu Ala Lys Thr Leu Ala Ala Leu Ala Pro Gly 165 170 175 Lys Leu Lys Tyr Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu 180 185 190 Ala Ala Leu Lys Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe 195 200 205 Thr Phe Ile Ala Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala 210 215 220 Leu Ser Ala Thr Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu 225 230 235 240 Leu Pro Gly Phe Arg His Val Pro Phe Gly Asp Ile Asn Ala Met Arg 245 250 255 Thr Met Leu Ser Glu Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val 260 265 270 Ile Leu Glu Pro Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln 275 280 285 Gly Tyr Leu Thr Ala Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu 290 295 300 Met Ile Leu Asp Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met 305 310 315 320 Phe Ala Cys Glu His Glu Asn Val Gln Pro Asp Ile Met Cys Leu Ala 325 330 335 Lys Ala Leu Gly Gly Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr 340 345 350 Glu Glu Val Phe Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr 355 360 365 Thr Phe Gly Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile 370 375 380 Asn Val Leu Leu Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly 385 390 395 400 Asp Met Leu Leu Asp Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp 405 410 415 Leu Val His Asp Val Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe 420 425 430 Val Asp Asn Glu Ile Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln 435 440 445 Arg Val Leu Val Ala Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile 450 455 460 Glu Pro Pro Leu Thr Leu Thr Ile Glu Gln Cys Asp Leu Val Leu Arg 465 470 475 480 Ala Thr Arg Lys Ala Leu Ala Ala Leu Arg Val Ser Val Glu Gln Val 485 490 495 <210> 270 <211> 458 <212> PRT <213> Artificial Sequence <220> <223> Chloroflexi bacterium <400> 270 Met Glu Lys Met Val Met Ala Lys Asp Phe Gly Gly Ala Leu Asp Tyr 1 5 10 15 Ser Ser Arg Trp Leu Asp Met Ile Arg Arg Asn Glu Phe Pro Ser Val 20 25 30 Glu Glu Ala His Gln Ile Ile Glu Glu Ser Lys His Asn Phe Ala Glu 35 40 45 Tyr Tyr Asn Arg Asn Trp Leu Glu Tyr Arg Lys Ser Val Thr Glu Ala 50 55 60 Gly Asp Trp Ala Ala Val Glu Trp Thr Gly Ser Gly Ala Val Phe Gln 65 70 75 80 Asp Val Leu Gly Arg Glu Tyr Leu Asp Phe Leu Gly Gly Tyr Gly Met 85 90 95 Met Asp Leu Gly Trp Ser His Pro Glu Val Val Ala Ala Val Arg Ala 100 105 110 Gln Leu Glu Arg Thr Pro Met Pro Ser Gln Glu Leu Ile Asp Pro Leu 115 120 125 Arg Gly Val Leu Ala Arg Leu Met Ala Glu Ile Thr Pro Gly Asp Leu 130 135 140 Lys Tyr Ser Trp Phe Ala Ala Ser Gly Thr Glu Ala Ile Glu Ala Ala 145 150 155 160 Ile Lys Ile Ala Lys Leu Tyr Ser Lys Lys Ser Ala Phe Ile Val Ala 165 170 175 Val Lys Ala Phe His Gly Lys Thr Met Gly Ser Leu Ser Met Met Gly 180 185 190 Lys Ser Asp Tyr Arg Thr Pro Leu Gly Gln Leu Tyr Gly Gly His Val 195 200 205 Tyr His Val Pro Phe Gly Asp Ala Asp Ala Val Glu Lys Gln Leu Glu 210 215 220 Val Cys Glu Lys Val Gly Ile Gly Val Ala Ala Val Leu Phe Glu Pro 225 230 235 240 Ile Gln Gly Glu Ala Gly Gly Ile Ala Pro Pro Asp Asp Phe Trp Pro 245 250 255 Arg Val Arg Glu Ala Thr Arg Lys His Asp Val Leu Leu Ile Ala Asp 260 265 270 Glu Val Gln Thr Gly Leu Gly Arg Thr Gly Lys Leu Trp Gly Val Asp 275 280 285 His Trp Gly Val Val Pro Asp Ile Leu Ala Val Ala Lys Ser Leu Gly 290 295 300 Gly Gly Val Met Pro Val Ser Ala Val Cys Thr Thr Glu Glu Ile Phe 305 310 315 320 Gln Pro Met Met Tyr Pro Asn Pro Phe Met His Thr Thr Thr Thr Gly 325 330 335 Gly Asn Ala Leu Ala Cys Ser Ala Ala Ile Ala Ala Ile His Ile Thr 340 345 350 Leu Arg Asp Arg Leu Trp Glu Gln Ala Ala Glu Lys Gly Glu Tyr Leu 355 360 365 Ile Pro Lys Leu Gln Lys Leu Ala Asp Gln Tyr Pro Gln Ile Tyr Glu 370 375 380 Lys Ile Thr Gly Lys Gly Leu Leu Ile Gly Met His Phe Lys Thr Pro 385 390 395 400 Glu Ile Gly Tyr Lys Val Ala Ser Gly Leu Phe Lys Arg Asn Ile Leu 405 410 415 Val Ala Gly Thr Leu Thr Ser Ala Gln Thr Val Arg Ile Glu Pro Ser 420 425 430 Leu Leu Val Thr Tyr Gly Gln Leu Asp Thr Leu Leu Asp Arg Leu Glu 435 440 445 Asp Thr Leu Lys Ser Ile Gly Arg Ser Glu 450 455 <210> 271 <211> 487 <212> PRT <213> Artificial Sequence <220> <223> Anaerolineae bacterium <400> 271 Met Val Ile Gly Asn Trp Arg Leu Glu Ile Gly Asp Trp Leu Leu Cys 1 5 10 15 Arg Ile Phe Thr Ile Arg Asn Leu Glu Gln Gln Ile His Pro Asp Ile 20 25 30 Gln Tyr Leu Ser Pro Met Pro Ile Tyr Pro Asp Ala Val Ser Tyr Ala 35 40 45 His Arg Trp Leu Asp Ile Ile Ala Lys Pro Ser Leu Thr Gln Ala Glu 50 55 60 Gly Glu Ala Ile Val Glu Glu Thr Leu Tyr Asn Phe Ala Asn His Phe 65 70 75 80 Asn Arg Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Glu Ala Gly Met 85 90 95 Phe Ala Ala Thr Glu Trp Thr Gly Arg Gly Ala Val Met Gln Asp Ala 100 105 110 Phe Gly Arg Glu Trp Ile Asp Cys Leu Gly Gly Tyr Gly Leu Leu Ser 115 120 125 Leu Gly Trp Ser His Pro Arg Val Val Glu Ala Val Arg Ala Gln Leu 130 135 140 Ser Arg Thr Pro Met Pro Ser Gln Glu Leu Leu Asp Pro Leu Arg Gly 145 150 155 160 Val Leu Ala Arg Leu Leu Ala Met Ile Thr Pro Gly Asp Ile Gly Tyr 165 170 175 Phe Phe Phe Ala Ala Gly Gly Thr Glu Ala Val Glu Gly Ala Met Lys 180 185 190 Leu Ala Lys Met Tyr Thr Arg Lys Ala Gly Phe Ile Thr Ser Leu Arg 195 200 205 Gly Phe His Gly Lys Thr Met Gly Ser Leu Ser Leu Leu Gly Lys Ser 210 215 220 Asp Phe Arg Ala Pro Ala Leu Pro Leu Tyr Pro Tyr Val Gln Trp Val 225 230 235 240 Pro Phe Gly Asp Ala Asp Ala Val Glu Arg Gln Leu Gln Ile Ala Asp 245 250 255 Ala Val Gly Gln Asp Ile Ala Ala Val Val Met Glu Pro Ile Gln Gly 260 265 270 Glu Ala Gly Ala Ile Val Pro Pro Asp Asp Phe Trp Pro Arg Leu Arg 275 280 285 Gln Leu Cys Asp Arg Tyr Gly Val Leu Leu Ile Ala Asp Glu Val Gln 290 295 300 Thr Gly Leu Gly Arg Thr Gly Lys Leu Trp Gly Val Asp His Trp Glu 305 310 315 320 Val Val Pro Asp Ile Ile Thr Met Gly Lys Ala Leu Gly Gly Gly Val 325 330 335 Met Pro Val Ser Cys Phe Gly Ala Arg Glu Glu Ile Trp Gly Val Met 340 345 350 Met Glu Pro Asn Pro Phe Val His Thr Thr Thr Thr Gly Gly Asn Pro 355 360 365 Leu Ala Cys Ala Ala Ala Ile Ala Ala Ile Thr Val Thr Leu Glu Glu 370 375 380 Asp Leu Pro Arg Gln Ala Ala Glu Lys Gly Ala Tyr Phe Lys Ala Gly 385 390 395 400 Leu Glu Lys Leu Ala Ala Asn Tyr Pro Met Ile Tyr Asp Arg Ile Ser 405 410 415 Gly Arg Gly Leu Leu Leu Gly Gln His Phe Arg Asp Ala Glu Val Gly 420 425 430 Tyr Ser Val Ala Ala Gly Leu Phe Lys Arg Gly Val Val Val Ala Gly 435 440 445 Thr Leu Thr Asn Ala Arg Thr Val Arg Ile Glu Pro Pro Leu Val Ile 450 455 460 Glu Tyr Glu Gln Ile Asp Ala Val Leu Glu Arg Leu Asp Asp Thr Leu 465 470 475 480 Arg Glu Val Arg Ala Gly Leu 485 <210> 272 <211> 503 <212> PRT <213> Artificial Sequence <220> <223> Citrobacter freundii <400> 272 Met Ala Leu Asn Val Ala Gln Ile Arg Cys Phe Leu Val Phe Ile Pro 1 5 10 15 Ile Phe Ala Lys Arg Ala Gly Met Ala Gln Ser Leu Gln Tyr Leu Asn 20 25 30 Gln Tyr His Val Ile Arg Glu Leu Arg Glu His Ile Leu Asn Arg Leu 35 40 45 Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser Ala His Ala Leu Asn Leu 50 55 60 Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met Lys Ser Leu Asn Arg 65 70 75 80 Glu Val Ile Glu Tyr Phe Lys Glu His Val Asn Pro Gly Phe Leu Glu 85 90 95 Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly Ala Val Glu Trp 100 105 110 Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln Gly Gln Glu Phe 115 120 125 Val Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val Gly His Arg Asn 130 135 140 Pro Val Val Val Ser Ala Val Gln Asn Gln Leu Ala Lys Gln Pro Leu 145 150 155 160 His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met Leu Ala Lys Thr 165 170 175 Leu Ala Ala Leu Ala Pro Gly Lys Leu Lys Tyr Ser Phe Phe Cys Asn 180 185 190 Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu Ala Lys Ala Tyr 195 200 205 Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr Ser Gly Ala Phe 210 215 220 His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala Lys Ser Thr Phe 225 230 235 240 Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe His His Val Pro Phe 245 250 255 Gly Asp Val Asn Ala Met Arg Thr Met Leu Ser Glu Cys Lys Lys Thr 260 265 270 Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile Gln Gly Glu Gly 275 280 285 Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Thr Ala Val Arg Lys Leu 290 295 300 Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp Glu Val Gln Thr Gly 305 310 315 320 Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His Glu Asn Val Gln 325 330 335 Pro Asp Ile Met Cys Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro 340 345 350 Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe Ser Val Leu Phe Asp 355 360 365 Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn Pro Leu Ala Cys 370 375 380 Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu Gln Asn Leu Pro 385 390 395 400 Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp Gly Phe Arg Gln 405 410 415 Leu Ala Arg Glu Tyr Pro Asp Leu Val His Asp Val Arg Gly Lys Gly 420 425 430 Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu Ile Gly Tyr Asn Phe 435 440 445 Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala Gly Thr Leu Asn 450 455 460 Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr Leu Thr Ile Glu 465 470 475 480 Gln Cys Asp Leu Val Leu Arg Ser Thr Arg Lys Ala Leu Ala Ala Leu 485 490 495 Arg Val Ser Val Glu Gln Met 500 <210> 273 <211> 453 <212> PRT <213> Artificial Sequence <220> <223> Anaerovorax odorimutans <400> 273 Met Thr Ala Phe Asn Arg Glu Ala Ala Leu Glu Gln Val Arg Arg Ile 1 5 10 15 Val Gly Tyr Ile Glu Lys Pro Glu Leu Thr Asn Glu Glu Lys Asp Thr 20 25 30 Ile Val Lys Glu Ser Ile Ser Asn Phe Asn Glu Asn Val Asn Pro Gly 35 40 45 Trp Leu Glu Tyr Arg Lys Ser Val Ser Thr Asp Ala Thr Phe Val Glu 50 55 60 Trp Thr Asp Ser Val Asp His Phe Glu Asp Leu Tyr Gly His Glu Phe 65 70 75 80 Ile Asp Cys Leu Gly Gly Phe Gly Ile Tyr Thr Cys Gly His Arg Asn 85 90 95 Pro Glu Ile Leu Lys Thr Val Lys Ala Gln Leu Asp Arg Tyr Ala Leu 100 105 110 His Ser Gln Glu Leu Val Asp Pro Leu Arg Gly Tyr Leu Ala Asn Thr 115 120 125 Leu Ala Met Ile Thr Pro Gly Asp Leu Gln Tyr Cys Phe Phe Thr Asn 130 135 140 Gly Gly Ala Glu Ala Val Glu Met Ala Leu Lys Leu Ala Arg Leu Ala 145 150 155 160 Thr Gly Gly Arg Tyr Tyr Ile Ser Thr Val Gly Ala Phe His Gly Lys 165 170 175 Ser Tyr Gly Ala Ile Ser Met Gly Gly Lys Gly Ala Tyr Arg Glu Asp 180 185 190 Tyr Leu Pro Met Ile Gln Gln Val Gln His Val Glu Tyr Gly Asn Ala 195 200 205 Glu Ala Met Glu Ala Ala Ile Lys Asn Leu His Thr Val Gly Glu Lys 210 215 220 Val Ala Gly Val Ile Ile Glu Pro Ile Gln Gly Glu Ala Gly Val Ile 225 230 235 240 Ile Pro Pro Asp Gly Tyr Leu Thr Lys Val Arg Glu Ile Cys Asp Lys 245 250 255 Tyr Gly Val Ala Met Ile Leu Asp Glu Ile Gln Thr Gly Met Gly Arg 260 265 270 Cys Gly Thr Met Trp Arg Cys Glu His Glu Gly Val Thr Pro Asp Ile 275 280 285 Met Thr Tyr Gly Lys Ala Phe Gly Gly Gly Ile Met Pro Ile Thr Gly 290 295 300 Ile Ile Ala Arg Pro Asn Met Trp Gly Gln Lys Leu Ile Asp Asn Pro 305 310 315 320 Trp Ile Leu Gly Ser Pro Thr Phe Gly Gly Asn Pro Leu Ala Cys Ser 325 330 335 Ala Ala Leu Ala Thr Ile Lys Phe Met Leu Glu Asn Asp Val Pro Lys 340 345 350 Met Ala Lys Glu Lys Gly Asp Tyr Phe Met Val Lys Leu Asn Ala Leu 355 360 365 Lys Glu Lys Tyr Pro Thr Val Leu Lys Gln Val Arg Gly Ala Gly Leu 370 375 380 Leu Ile Cys Met Glu Phe Pro Glu Ala Glu Val Gly Tyr Glu Ile Thr 385 390 395 400 Lys Gly Leu Phe Ser Arg Lys Val Met Thr Ala Gly Thr Leu Val Asn 405 410 415 Ala Lys Thr Val Arg Ile Glu Pro Pro Ala Val Leu Ser Tyr Glu Lys 420 425 430 Ile Asp His Val Met Ala Met Leu Glu Glu Ser Ile Ile Asp Ala Lys 435 440 445 Lys Glu Phe Asn Leu 450 <210> 274 <211> 479 <212> PRT <213> Artificial Sequence <220> <223> Citrobacter braakii <400> 274 Met Gln Ser Leu Gln Tyr Leu Asn Gln Tyr His Val Ile Arg Glu Leu 1 5 10 15 Arg Glu His Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala 20 25 30 Cys Ser Ala His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His 35 40 45 Glu Glu Met Lys Ser Leu Asn Arg Glu Val Ile Glu Tyr Phe Lys Glu 50 55 60 His Val Asn Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly 65 70 75 80 Gly Asp Tyr Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu 85 90 95 Val Asp Thr Gln Gly Gln Glu Phe Val Asp Cys Leu Gly Gly Phe Gly 100 105 110 Ile Phe Asn Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln 115 120 125 Asn Gln Leu Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro 130 135 140 Leu Arg Ala Met Leu Ala Lys Thr Leu Ala Ala Leu Ala Pro Gly Lys 145 150 155 160 Leu Lys Tyr Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala 165 170 175 Ala Leu Lys Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr 180 185 190 Phe Ile Ala Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu 195 200 205 Ser Ala Thr Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu 210 215 220 Pro Gly Phe Arg His Val Pro Phe Gly Asp Ile Asn Ala Met Arg Thr 225 230 235 240 Met Leu Ser Glu Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Ile 245 250 255 Leu Glu Pro Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly 260 265 270 Tyr Leu Pro Ala Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met 275 280 285 Ile Leu Asp Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe 290 295 300 Ala Cys Glu His Glu Asn Val Gln Pro Asp Ile Met Cys Leu Ala Lys 305 310 315 320 Ala Leu Gly Gly Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu 325 330 335 Glu Val Phe Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr 340 345 350 Phe Gly Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn 355 360 365 Val Leu Leu Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp 370 375 380 Met Leu Leu Asp Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp Leu 385 390 395 400 Val His Asp Val Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val 405 410 415 Asp Asn Glu Ile Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg 420 425 430 Val Leu Val Ala Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu 435 440 445 Pro Pro Leu Thr Leu Thr Ile Glu Gln Cys Asp Leu Val Leu Arg Ser 450 455 460 Thr Arg Lys Ala Leu Ala Ala Leu Arg Val Ser Val Glu Gln Val 465 470 475 <210> 275 <211> 453 <212> PRT <213> Artificial Sequence <220> <223> Anaerolineaceae bacterium <400> 275 Met Ala Tyr Asp Tyr Glu Asp Ala Leu Asp Tyr Ser Ser Arg Trp Ile 1 5 10 15 Asp Leu Ile His Lys Asn Glu Phe Pro Thr Val Asp Glu Ala His Thr 20 25 30 Ile Ile Ser Glu Ser Thr His Asn Phe Ala Glu Tyr Tyr Asn Arg Asn 35 40 45 Trp Leu Glu Tyr Arg Lys Ser Val Thr Glu Ser Gly Asp Trp Ala Ala 50 55 60 Val Glu Trp Gly Gly Ser Gly Ala Val Phe Lys Asp Val Leu Gly Arg 65 70 75 80 Glu Tyr Leu Asp Phe Leu Gly Gly Tyr Gly Met Met Asp Leu Gly Trp 85 90 95 Ser His Pro Glu Val Val Lys Thr Val Arg Ala Gln Leu Glu Arg Ser 100 105 110 Pro Met Pro Ser Gln Glu Leu Leu Asp Pro Leu Arg Gly Val Leu Ala 115 120 125 Lys Leu Leu Ala Ser Ile Thr Pro Gly Asp Leu Lys Tyr Ser Trp Phe 130 135 140 Gly Ala Ser Gly Thr Glu Ala Asn Glu Ala Ala Met Lys Ile Ala Lys 145 150 155 160 Leu Tyr Thr Gly Lys Thr Ala Phe Ile Val Gly Val Arg Ala Phe His 165 170 175 Gly Lys Thr Met Gly Ser Leu Ser Leu Ile Gly Lys Ser Asp Phe Arg 180 185 190 Ala Ser Met Gly Ala Met Tyr Gly Gly Gln Val Tyr His Val Pro Phe 195 200 205 Gly Asp Ala Asp Ala Val Glu Lys Gln Leu Glu Ile Cys Glu Lys Val 210 215 220 Gly Ile Gly Val Ala Ala Val Met Phe Glu Pro Ile Gln Gly Glu Ser 225 230 235 240 Gly Ala Ile Val Pro Pro Asp Asp Phe Trp Pro Arg Ile Arg Ala Ala 245 250 255 Thr Lys Lys His Gly Val Leu Leu Ile Ala Asp Glu Val Gln Thr Gly 260 265 270 Leu Gly Arg Thr Gly Arg Leu Trp Gly Val Glu His Trp Asn Val Val 275 280 285 Pro Asp Ile Leu Thr Val Ala Lys Ser Leu Gly Gly Gly Val Met Pro 290 295 300 Ile Ser Ala Val Ile Thr Thr Glu Glu Val Phe His Pro Met Met Tyr 305 310 315 320 Pro Asn Pro Phe Met His Thr Thr Thr Thr Gly Gly Gly Ala Leu Ala 325 330 335 Cys Ser Ala Ala Ile Ala Ala Ile Asn Val Thr Leu Arg Glu Lys Met 340 345 350 Trp Glu Gln Ala Ala Asp Lys Gly Ala Tyr Leu Ile Pro Gln Leu Glu 355 360 365 Lys Phe Ala Ser Gln Tyr Pro Gln Ile Tyr Glu Lys Ile Thr Gly Lys 370 375 380 Gly Leu Leu Ile Gly Met His Phe Lys Thr Pro Gly Ile Gly Tyr Lys 385 390 395 400 Val Ala Ser Gly Leu Phe Lys Arg Gly Val Leu Val Ala Gly Thr Leu 405 410 415 Thr Ser Ala Gln Thr Val Arg Ile Glu Pro Pro Leu Val Val Thr Arg 420 425 430 Glu Gln Met Asp Met Leu Leu Asp Arg Leu Gly Asp Thr Leu Lys Glu 435 440 445 Ile Asn Thr Ala Met 450 <210> 276 <211> 482 <212> PRT <213> Artificial Sequence <220> <223> Citrobacter koseri <400> 276 Met Asp Met Ala Gln Ser Leu Gln Tyr Leu Thr Gln Tyr His Val Ile 1 5 10 15 Arg Glu Phe Arg Glu His Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser 20 25 30 Ala Leu Ala Cys Ser Ala His Ala Leu Asn Leu Ile Glu Lys Arg Thr 35 40 45 Leu Asp His Glu Glu Met Lys Ala Leu Asn Arg Glu Val Ile Asp Tyr 50 55 60 Phe Lys Glu His Val Asn Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val 65 70 75 80 Thr Ala Gly Gly Asp Tyr Gly Ala Val Glu Trp Gln Ala Gly Ser Leu 85 90 95 Asn Thr Leu Val Asp Thr Gln Gly Gln Glu Phe Ile Asp Cys Leu Gly 100 105 110 Gly Phe Gly Ile Phe Asn Val Gly His Arg Asn Pro Val Val Val Ser 115 120 125 Ala Val Gln Asn Gln Leu Ala Lys Gln Pro Leu His Ser Gln Glu Leu 130 135 140 Leu Asp Pro Leu Arg Ala Met Leu Ala Lys Thr Leu Ala Ala Leu Thr 145 150 155 160 Pro Gly Lys Leu Lys Tyr Ser Phe Phe Ser Asn Ser Gly Thr Glu Ser 165 170 175 Val Glu Ala Ala Leu Lys Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly 180 185 190 Lys Phe Thr Phe Ile Ala Thr Ser Gly Ala Phe His Gly Lys Ser Leu 195 200 205 Gly Ser Leu Ser Ala Thr Ala Lys Ser Thr Phe Arg Lys Pro Phe Met 210 215 220 Pro Leu Leu Pro Gly Phe Arg His Val Pro Phe Gly Asn Ile Glu Ala 225 230 235 240 Met Arg Thr Ala Leu Ser Glu Cys Lys Lys Thr Gly Asp Asp Val Ala 245 250 255 Ala Val Ile Leu Glu Pro Ile Gln Gly Glu Gly Gly Val Ile Leu Pro 260 265 270 Pro Gln Gly Tyr Leu Thr Ala Val Arg Lys Leu Cys Asp Glu Phe Gly 275 280 285 Ala Leu Met Ile Leu Asp Glu Val Gln Thr Gly Met Gly Arg Thr Gly 290 295 300 Lys Met Phe Ala Cys Glu His Glu Asn Val Gln Pro Asp Ile Leu Cys 305 310 315 320 Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro Val Gly Ala Thr Ile 325 330 335 Ala Thr Glu Glu Val Phe Ser Val Leu Phe Asp Asn Pro Phe Leu His 340 345 350 Thr Thr Thr Phe Gly Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala 355 360 365 Thr Ile Asn Val Leu Leu Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln 370 375 380 Lys Gly Asp Met Leu Leu Asp Gly Phe Leu Gln Leu Ala Arg Glu Tyr 385 390 395 400 Pro Asp Leu Val Gln Asp Ala Arg Gly Lys Gly Met Leu Met Ala Ile 405 410 415 Glu Phe Val Asp Asn Glu Ile Gly Tyr Asn Phe Ala Ser Glu Met Phe 420 425 430 Arg Gln Arg Val Leu Val Ala Gly Thr Leu Asn Asn Ser Lys Thr Ile 435 440 445 Arg Ile Glu Pro Pro Leu Thr Leu Thr Ile Glu Gln Cys Glu Gln Val 450 455 460 Leu Lys Ala Thr Arg Lys Ala Leu Ala Ala Leu Arg Val Ser Val Glu 465 470 475 480 Glu Thr <210> 277 <211> 443 <212> PRT <213> Artificial Sequence <220> <223> Enterobacteriaceae bacterium ATCC 29904 <400> 277 Met Leu Asn Leu Ile Glu Lys Gln Thr Leu Asp His Glu Glu Met Lys 1 5 10 15 Gln Leu Asn Arg Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn Pro 20 25 30 Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly 35 40 45 Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln 50 55 60 Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val 65 70 75 80 Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu Ala 85 90 95 Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met 100 105 110 Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser 115 120 125 Phe Phe Ser Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu 130 135 140 Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr 145 150 155 160 Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala 165 170 175 Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg 180 185 190 His Val Pro Phe Gly Asp Ile Ala Ala Leu Arg Leu Gln Leu Ser Glu 195 200 205 Cys Arg Asn Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile 210 215 220 Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Pro Ala 225 230 235 240 Val Arg Gln Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Phe Asp Glu 245 250 255 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His 260 265 270 Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly 275 280 285 Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe Ser 290 295 300 Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn 305 310 315 320 Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu 325 330 335 Glu Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp 340 345 350 Gly Phe Arg Gln Leu Gly Arg Glu Tyr Pro Asp Leu Val Gln Asp Ala 355 360 365 Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Ala Ile 370 375 380 Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala 385 390 395 400 Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr 405 410 415 Leu Thr Ile Glu Gln Cys Glu Gln Val Leu Lys Ala Ala Arg Lys Ala 420 425 430 Leu Ala Ala Leu Arg Val Ser Val Glu Glu Ala 435 440 <210> 278 <211> 443 <212> PRT <213> Artificial Sequence <220> <223> Lelliottia amnigena <400> 278 Met Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met Lys 1 5 10 15 Gln Leu Asn Arg Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn Pro 20 25 30 Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly 35 40 45 Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln 50 55 60 Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val 65 70 75 80 Gly His Arg Asn Pro Thr Val Val Ser Ala Val Gln Asn Gln Leu Glu 85 90 95 Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met 100 105 110 Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser 115 120 125 Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu 130 135 140 Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr 145 150 155 160 Thr Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala 165 170 175 Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg 180 185 190 His Val Pro Phe Gly Asp Ile Asn Ala Met Arg Thr Val Leu Ser Glu 195 200 205 Cys Arg Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile 210 215 220 Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Pro Ala 225 230 235 240 Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Leu Asp Glu 245 250 255 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His 260 265 270 Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly 275 280 285 Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe Ser 290 295 300 Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn 305 310 315 320 Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu 325 330 335 Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp 340 345 350 Gly Phe Leu Gln Leu Gly Arg Glu Tyr Pro Asp Leu Val Gln Asp Ala 355 360 365 Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu Ile 370 375 380 Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala 385 390 395 400 Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr 405 410 415 Leu Thr Ile Glu Gln Cys Glu Ala Val Leu Lys Ala Ala Arg Lys Ala 420 425 430 Leu Ala Ala Met Arg Val Ser Val Glu Glu Ala 435 440 <210> 279 <211> 476 <212> PRT <213> Artificial Sequence <220> <223> Enterobacter <400> 279 Met Gln Tyr Leu Ile Gln Tyr His Val Ile Arg Asp Pro Arg Glu His 1 5 10 15 Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Thr Ala 20 25 30 His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met 35 40 45 Lys Gln Leu Asn Arg Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn 50 55 60 Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr 65 70 75 80 Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr 85 90 95 Gln Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn 100 105 110 Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu 115 120 125 Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala 130 135 140 Met Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr 145 150 155 160 Ser Phe Phe Ser Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Ile Lys 165 170 175 Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala 180 185 190 Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr 195 200 205 Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe 210 215 220 Arg His Val Pro Phe Gly Asp Ile Ser Ala Met Arg Thr Met Leu Ser 225 230 235 240 Glu Cys Arg Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro 245 250 255 Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Pro 260 265 270 Ala Val Arg Gln Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Leu Asp 275 280 285 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu 290 295 300 His Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly 305 310 315 320 Gly Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe 325 330 335 Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 340 345 350 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu 355 360 365 Asp Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu 370 375 380 Asp Gly Phe Arg Gln Leu Gly Arg Glu Tyr Pro Asp Leu Val Gln Asp 385 390 395 400 Ala Arg Gly Lys Gly Leu Leu Met Ala Ile Glu Phe Val Asp Asn Glu 405 410 415 Ile Gly Tyr Ser Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val 420 425 430 Ala Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Ile Glu Pro Pro Leu 435 440 445 Thr Leu Thr Val Glu Gln Cys Glu Gln Val Leu Lys Ala Ala Arg Lys 450 455 460 Ala Leu Ala Ala Leu Arg Val Ser Val Glu Glu Ala 465 470 475 <210> 280 <211> 478 <212> PRT <213> Artificial Sequence <220> <223> Yokenella regensburgei <400> 280 Met Gln Tyr Leu Asn Arg Tyr His Val Ile Arg Glu Leu Pro Glu His 1 5 10 15 Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Thr Ala 20 25 30 His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met 35 40 45 Lys Ala Leu Asn Val Glu Val Lys Glu Tyr Phe Lys Glu His Val Asn 50 55 60 Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr 65 70 75 80 Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr 85 90 95 Gln Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn 100 105 110 Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu 115 120 125 Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala 130 135 140 Met Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr 145 150 155 160 Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Ile Lys 165 170 175 Leu Ala Lys Ala Tyr Gln Ser Pro Arg Ser Lys Phe Thr Phe Ile Ala 180 185 190 Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr 195 200 205 Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe 210 215 220 Arg His Ile Pro Phe Gly Asp Ile Ser Ala Met Arg Ser Val Leu Thr 225 230 235 240 Glu Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro 245 250 255 Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Pro Gly Tyr Leu Pro 260 265 270 Ala Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp 275 280 285 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu 290 295 300 His Glu Asn Val Gln Pro Asp Ile Met Cys Leu Ala Lys Ala Leu Gly 305 310 315 320 Gly Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe 325 330 335 Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 340 345 350 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu 355 360 365 Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu 370 375 380 Asp Gly Phe Arg Asn Leu Met Arg Glu Tyr Pro Asp Leu Ile Gln Asp 385 390 395 400 Val Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu 405 410 415 Thr Gly Tyr Thr Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val 420 425 430 Ala Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Val Glu Pro Pro Leu 435 440 445 Thr Leu Thr Pro Glu Gln Cys Gln Leu Val Leu Lys Ala Thr Arg Lys 450 455 460 Ala Leu Ala Ala Leu Arg Val Ala Val Glu Gln Glu Glu Ser 465 470 475 <210> 281 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Enterobacter huaxiensis <400> 281 Met Val Ile Arg Asp Pro Arg Glu His Ile Leu Asn Arg Leu Pro Ser 1 5 10 15 Ser Ala Ser Ala Leu Ala Cys Thr Ala His Ala Leu Asn Leu Ile Glu 20 25 30 Lys Arg Thr Leu Asp His Glu Glu Met Lys Gln Leu Asn Arg Glu Val 35 40 45 Ile Asp Tyr Phe Lys Glu His Val Asn Pro Gly Phe Leu Glu Tyr Arg 50 55 60 Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly Ala Val Glu Trp Gln Ala 65 70 75 80 Gly Ser Leu Asn Thr Leu Val Asp Thr Gln Gly Gln Glu Phe Ile Asp 85 90 95 Cys Leu Gly Gly Phe Gly Ile Phe Asn Val Gly His Arg Asn Pro Val 100 105 110 Val Val Ser Ala Val Gln Asn Gln Leu Ala Lys Gln Pro Leu His Ser 115 120 125 Gln Glu Leu Leu Asp Pro Leu Arg Ala Met Leu Ala Lys Thr Leu Ala 130 135 140 Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser Phe Phe Ser Asn Ser Gly 145 150 155 160 Thr Glu Ser Val Glu Ala Ala Leu Lys Leu Ala Lys Ala Tyr Gln Ser 165 170 175 Pro Arg Gly Lys Phe Thr Phe Val Ala Thr Ser Gly Ala Phe His Gly 180 185 190 Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala Lys Ser Thr Phe Arg Lys 195 200 205 Pro Phe Met Pro Leu Leu Pro Gly Phe Arg His Val Pro Phe Gly Asp 210 215 220 Ile Asn Ala Met Arg Ala Leu Leu Ser Glu Cys Arg Lys Thr Gly Asp 225 230 235 240 Asp Val Ala Ala Val Ile Leu Glu Pro Ile Gln Gly Glu Gly Gly Val 245 250 255 Ile Leu Pro Pro Gln Gly Tyr Leu Pro Ala Val Arg Gln Leu Cys Asp 260 265 270 Glu Phe Gly Ala Leu Leu Ile Phe Asp Glu Val Gln Thr Gly Met Gly 275 280 285 Arg Thr Gly Lys Met Phe Ala Cys Glu His Glu Asn Val Gln Pro Asp 290 295 300 Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro Ile Gly 305 310 315 320 Ala Thr Val Ala Thr Glu Glu Val Phe Ser Val Leu Phe Asp Asn Pro 325 330 335 Phe Leu His Thr Thr Thr Phe Gly Gly Asn Pro Leu Ala Cys Ala Ala 340 345 350 Ala Leu Ala Thr Ile Asn Val Leu Leu Glu Gln Asn Leu Pro Ala Gln 355 360 365 Ala Glu Gln Lys Gly Asp Met Leu Leu Asp Gly Phe Arg Gln Leu Gly 370 375 380 Arg Glu Tyr Pro Asp Leu Val Gln Asp Ala Arg Gly Lys Gly Met Leu 385 390 395 400 Met Ala Ile Glu Phe Val Asp Asn Glu Thr Gly Tyr Ser Phe Ala Ser 405 410 415 Glu Met Phe Arg Gln Arg Val Leu Val Ala Gly Thr Leu Asn Asn Ser 420 425 430 Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr Leu Thr Ile Glu Gln Cys 435 440 445 Glu Gln Val Leu Lys Ala Ala Arg Lys Ala Leu Ala Ala Leu Arg Val 450 455 460 Ser Val Glu Glu Ala 465 <210> 282 <211> 477 <212> PRT <213> Artificial Sequence <220> <223> Shigella dysenteriae <400> 282 Met Leu Gln Tyr Leu Asn Arg Tyr His Val Ile Arg Glu Pro Pro Glu 1 5 10 15 His Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser 20 25 30 Ala His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu 35 40 45 Met Lys Ala Leu Asn Arg Glu Val Ile Glu Tyr Phe Lys Glu His Val 50 55 60 Asn Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp 65 70 75 80 Tyr Gly Ala Val Glu Trp Gln Ala Gly Gly Leu Asn Thr Leu Val Asp 85 90 95 Thr Gln Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe 100 105 110 Asn Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln 115 120 125 Leu Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg 130 135 140 Ala Met Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys 145 150 155 160 Tyr Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu 165 170 175 Lys Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile 180 185 190 Ala Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala 195 200 205 Thr Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly 210 215 220 Phe Arg His Val Pro Phe Gly Asn Ile Glu Ala Met Arg Thr Ala Leu 225 230 235 240 Asn Glu Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Leu Leu Glu 245 250 255 Pro Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Pro Gly Tyr Leu 260 265 270 Thr Ala Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met Ile Leu 275 280 285 Asp Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys 290 295 300 Glu His Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu 305 310 315 320 Gly Gly Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu Glu Val 325 330 335 Phe Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly 340 345 350 Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu 355 360 365 Leu Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu 370 375 380 Leu Asp Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp Leu Val Gln 385 390 395 400 Glu Ala Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn 405 410 415 Glu Ile Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu 420 425 430 Val Ala Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro 435 440 445 Leu Thr Leu Thr Ile Glu Gln Cys Glu Leu Val Ile Lys Ala Ala Arg 450 455 460 Lys Ala Leu Ala Ala Met Arg Val Ser Val Glu Glu Ala 465 470 475 <210> 283 <211> 451 <212> PRT <213> Artificial Sequence <220> <223> Vibrio sp. LJC006 <400> 283 Met Asp Phe Ser Lys Arg Asn Val Asp Asp Ala Phe Met Glu Ala Thr 1 5 10 15 Lys Met Val Ser Leu Leu Thr Lys Glu Glu Lys Glu Ile Asn Glu Glu 20 25 30 Glu Arg Thr Trp Ile Ala Gln Ser Thr Tyr Glu Asn Phe Glu Asn His 35 40 45 Ile Asn Lys Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Glu Thr Glu 50 55 60 Gly Ile Ala Leu Thr Asp Trp Ser Gly Gln Gly Ser Ile Leu Lys Asp 65 70 75 80 Val Leu Gly Arg Glu Phe Ile Asp Met Leu Gly Gly Phe Gly Leu Tyr 85 90 95 Ser Pro Gly Ile Arg His Pro Lys Ile Val Ala Ala Ala Lys Ala Gln 100 105 110 Ile Asp Arg Ser Pro Gln Tyr Ser Gln Glu Met Leu Asp Pro Leu Arg 115 120 125 Ala His Leu Ala Lys Val Ile Ala Lys Leu Thr Pro Gly Asp Ile Gln 130 135 140 Tyr Gly Phe Phe Ala Asn Ser Gly Thr Glu Ala Val Asp Gly Ala Met 145 150 155 160 Lys Leu Ala Lys Met Tyr Thr Gly Lys Lys Gly Phe Ile Ser Thr Leu 165 170 175 Lys Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Leu Leu Gly Lys 180 185 190 Ala Val Tyr Arg Glu Pro Val Gly Pro Leu Leu Asp Gly Val Arg His 195 200 205 Val Pro Tyr Gly Asp Ala Asp Ala Val Glu Ala Gln Leu Gln Ala Ala 210 215 220 Gln Glu Val Gly Glu Gly Ile Ala Ala Val Ile Ala Glu Pro Ile Gln 225 230 235 240 Gly Glu Ala Gly Ala Ile Val Pro Pro Asp Asp Tyr Trp Pro Arg Leu 245 250 255 Arg Glu Ile Cys Asp Lys Tyr Gly Val Leu Leu Ile Ala Asp Glu Val 260 265 270 Gln Thr Gly Phe Gly Arg Thr Gly Lys Leu Phe Gly Val Asp His Trp 275 280 285 Asn Val Thr Pro Asp Ile Met Cys Phe Gly Lys Ala Leu Gly Gly Gly 290 295 300 Val Ile Ala Met Ser Gly Phe Phe Ala Ser Ala Lys Ile Trp Lys Val 305 310 315 320 Leu Glu Pro Asn Pro Phe Met His Thr Thr Thr Thr Gly Gly Asn Pro 325 330 335 Val Ala Cys Ala Ala Ala Leu Ala Gln Ile Ser Val Leu Leu Glu Glu 340 345 350 Asp Leu Ala Gly Gln Ala Ala Glu Lys Gly Asp Tyr Ile Lys Arg Lys 355 360 365 Leu Gly Glu Leu Gln Arg Arg Tyr Pro Asp Val Leu Lys Asp Val Thr 370 375 380 Gly Arg Gly Leu Leu Leu Gly Met Val Phe Lys Asn Asp Glu Val Gly 385 390 395 400 Phe Glu Val Val Ser Gly Leu Phe Lys Arg Gly Ile Leu Ile Ala Gly 405 410 415 Thr Leu Asn Asn Ser Glu Val Val Arg Val Glu Pro Ala Leu Asn Ile 420 425 430 Ser Tyr Asp Leu Ile Asp Thr Phe Leu Val Glu Leu Glu Glu Val Met 435 440 445 Lys Thr Leu 450 <210> 284 <211> 464 <212> PRT <213> Artificial Sequence <220> <223> Desulfobulbaceae bacterium <400> 284 Met Thr Glu Val Ala Arg Thr Thr Thr Gln His Pro Ala Ala Ala Glu 1 5 10 15 Arg Asn Val Asn Leu Ala Leu Glu Glu Ala Lys Arg Met Val Asp Leu 20 25 30 Ile Gly Thr Ala Glu Lys Asp Val Thr Met Glu Asp Arg Gln Trp Val 35 40 45 Ala Glu Thr Thr Tyr Gln Asn Phe Ala Asn His Ile Asn Lys Gly Phe 50 55 60 Leu Glu Tyr Arg Lys Ser Val Thr Glu Thr Glu Asp Phe Ala Leu Thr 65 70 75 80 Asp Trp Tyr Gly Glu Gly Ser Ile Leu Arg Asp Val Met Gly Arg Glu 85 90 95 Tyr Ile Asp Met Leu Gly Gly Phe Gly Leu Tyr Ser Pro Gly Ile Arg 100 105 110 His Pro Lys Ile Val Ala Ala Ala Lys Ala Gln Leu Asp Arg Ser Pro 115 120 125 Gln Tyr Ser Gln Glu Met Leu Asp Pro Leu Arg Ala His Leu Ala Lys 130 135 140 Val Ile Ala Gln Leu Thr Pro Gly Asp Ile Gln Tyr Gly Phe Phe Ala 145 150 155 160 Asn Ser Gly Thr Glu Ala Val Glu Gly Ala Met Lys Leu Ala Lys Leu 165 170 175 Tyr Thr Gly Lys Lys Gly Phe Ile Ser Thr Leu Asn Gly Phe His Gly 180 185 190 Lys Thr Leu Gly Ser Leu Ser Leu Ile Gly Lys Ser Val Tyr Arg Lys 195 200 205 Pro Leu Leu Pro Leu Leu Glu Gly Ile His Gln Val Pro Phe Gly Asp 210 215 220 Ala Gly Ala Val Glu Gln Val Leu Ala Ser Ala Lys Met Val Gly Asp 225 230 235 240 Gly Ile Ala Gly Val Val Val Glu Pro Ile Gln Gly Glu Ala Gly Ala 245 250 255 Val Val Pro Pro Asp Asp Tyr Trp Pro Lys Leu Arg Glu Ile Cys Asp 260 265 270 Lys Tyr Glu Val Leu Leu Ile Ala Asp Glu Val Gln Thr Gly Phe Gly 275 280 285 Arg Thr Gly Lys Leu Phe Gly Val Asp His Trp Asn Val Thr Pro Asp 290 295 300 Ile Met Cys Phe Gly Lys Ala Leu Gly Gly Gly Val Val Ala Met Ser 305 310 315 320 Gly Phe Phe Ser Thr Ala Lys Ile Trp Lys Cys Met Glu Pro Asn Pro 325 330 335 Phe Met His Thr Thr Thr Thr Gly Gly Asn Pro Leu Ala Cys Ala Ala 340 345 350 Ala Leu Ala Gln Ile Thr Val Leu Leu Glu Glu Asp Leu Ala Gly Gln 355 360 365 Ala Ala Ala Lys Gly Glu Tyr Ile Thr Ser Arg Met Leu Thr Leu Lys 370 375 380 Glu Lys Tyr Pro His Ile Leu Gln Gly Phe Arg Gly Arg Gly Leu Leu 385 390 395 400 Leu Ala Met Val Phe Pro Thr Asp Glu Ile Gly Tyr Lys Val Ala Thr 405 410 415 Gly Leu Phe Ser Arg Asn Val Leu Thr Ala Gly Thr Leu Asn Asn Ala 420 425 430 Arg Ala Ile Arg Ile Glu Pro Ala Leu Thr Val Ser Tyr Asp Ile Leu 435 440 445 Asp Glu Met Leu Arg Arg Met Glu Ala Thr Phe Ala Ser Ile Thr Ile 450 455 460 <210> 285 <211> 453 <212> PRT <213> Artificial Sequence <220> <223> Chloroflexi bacterium <400> 285 Met Thr Asn Thr Tyr Asp Asp Val Leu Ala Tyr Ser Asn Gln Trp Leu 1 5 10 15 Asp Ile Ile Lys Gln Glu Ser Phe Pro Glu Glu Gln Gln Ala Lys Trp 20 25 30 Ile Ile Ala Glu Ser Lys His Asn Phe Ala Glu His Phe Asn Arg Asn 35 40 45 Trp Leu Glu Tyr Arg Lys Ser Val Thr Glu Ala Gly Asp Trp Ala Ala 50 55 60 Val Glu Trp Ser Gly Lys Gly Ser Thr Phe Thr Asp Val Leu Gly Arg 65 70 75 80 Arg Tyr Ile Asp Trp Leu Gly Gly Phe Gly Met Leu Asp Leu Gly Trp 85 90 95 Cys His Pro Glu Val Val Ala Ala Val Thr Ala Gln Val Lys Arg Ser 100 105 110 Pro Met Pro Ser Gln Glu Leu Ile Asp Pro Leu Arg Gly Val Leu Ala 115 120 125 Arg Ile Leu Ala Glu Ile Thr Pro Gly Asp Leu Lys Tyr Ser Trp Phe 130 135 140 Ala Ala Ser Gly Thr Glu Ala Ile Glu Ala Ala Ile Lys Ile Ala Lys 145 150 155 160 Leu Tyr Thr Gly Asn Ser Ala Phe Ile Val Ala Val Lys Gly Phe His 165 170 175 Gly Lys Thr Leu Gly Ser Leu Ser Met Ile Gly Lys Ser Asp Phe Arg 180 185 190 Gln Ser Met Gly Val Met Tyr Gly Gly Lys Asp Tyr His Val Pro Tyr 195 200 205 Gly Asp Ala Gly Ala Val Glu Gln Gln Leu Glu Ile Cys Glu Lys Val 210 215 220 Gly Val Gly Val Ala Ala Val Ile Phe Glu Pro Ile Gln Gly Glu Ala 225 230 235 240 Gly Gly Ile Val Pro Pro Asp Asp Phe Trp Pro Arg Ile Arg Gln Ala 245 250 255 Thr Arg Asn His Gly Val Leu Leu Ile Ala Asp Glu Val Gln Thr Gly 260 265 270 Leu Ala Arg Thr Gly Lys Leu Trp Gly Val Asp His Trp Asp Val Ala 275 280 285 Pro Asp Ile Ile Ala Thr Ala Lys Ser Leu Gly Gly Gly Val Met Pro 290 295 300 Val Ser Ala Val Thr Thr Thr Glu Glu Ile Phe His Pro Met Met Tyr 305 310 315 320 Pro Asn Pro Phe Met His Thr Thr Thr Thr Gly Gly Gly Ala Leu Ala 325 330 335 Cys Ser Ala Ala Ile Ala Ser Ile Asn Val Ile Leu Arg Asp Arg Leu 340 345 350 Trp Glu Gly Ala Ala Ser Met Gly Ala Tyr Leu Lys Glu Lys Val Gln 355 360 365 Asp Leu Ala Asp Glu Phe Pro Gln Ile Tyr Gln Lys Val Thr Gly Lys 370 375 380 Gly Leu Leu Ile Gly Gln His Phe His Thr Pro Glu Leu Gly Tyr Lys 385 390 395 400 Val Ala Ala Glu Leu Phe Lys Arg Gly Val Leu Val Ala Gly Thr Leu 405 410 415 Thr Ser Ala Gln Thr Val Arg Ile Glu Pro Pro Leu Ile Ile Ser Gln 420 425 430 Glu Glu Ile Asp Glu Gly Leu Asn Arg Leu Ser Asp Ala Val Gly Ala 435 440 445 Val Ala Ala Ala Ile 450 <210> 286 <211> 453 <212> PRT <213> Artificial Sequence <220> <223> Bacillus sp. PK3_68 <400> 286 Met Arg Lys Ser Asn Glu Glu Ala Leu Gln Ile Ala Thr Glu Ile Leu 1 5 10 15 Glu Leu Ile Glu Ser Asp Ser Leu Ser Glu Lys Gln Lys Asp Gln Ile 20 25 30 Ile Glu Asp Ser Ile Tyr Asn Phe Thr Asn Phe Val Asn Lys Ala Ile 35 40 45 Leu Asp His Arg Lys Ser Ala Ser Thr Asp Phe Ser Phe Val Glu Trp 50 55 60 Glu Asp Glu Lys Ala Ile Phe Arg Asp Thr Lys Asn Arg Glu Phe Ile 65 70 75 80 Asp Cys Leu Gly Gly Tyr Gly Val Tyr Leu Leu Gly His Arg His Pro 85 90 95 Lys Val Val Lys Ala Val Glu Ala Gln Leu Lys Arg Tyr Ala Leu His 100 105 110 Ser Gln Glu Leu Val Asp Pro Leu Arg Gly Tyr Leu Ser Lys Leu Val 115 120 125 Ala Ala Ile Thr Pro Gly Asp Met Gln Tyr Thr Tyr Phe Thr Asn Ser 130 135 140 Gly Ala Glu Ala Asn Glu Met Ala Leu Lys Leu Ala Arg Leu Ala Thr 145 150 155 160 Gly Lys Thr His Phe Ile Ser Thr Val Asn Gly Phe His Gly Lys Thr 165 170 175 Phe Gly Ala Leu Ser Ser Ser Gly Lys Ala Val Phe Arg Glu Pro Tyr 180 185 190 Leu Pro Leu Val Pro Gly Phe His His Val Pro Phe Gly Asp Val Asp 195 200 205 Ala Met Glu Asn Met Ile Asn Gln Leu Glu Ala Thr Gly Glu Lys Val 210 215 220 Ala Gly Ile Ile Val Glu Pro Ile Gln Gly Glu Gly Gly Ile Asn Ile 225 230 235 240 Pro Ser Ala Asp Tyr Phe Pro Arg Leu Arg Glu Ile Cys Asp Glu His 245 250 255 Asn Cys Val Leu Ile Val Asp Glu Ile Gln Thr Gly Met Gly Arg Thr 260 265 270 Gly Thr Leu Phe Gly Ile Asp His Trp Asn Val Val Pro Asp Ile Met 275 280 285 Thr Leu Gly Lys Ala Phe Gly Gly Gly Val Met Pro Ile Thr Ala Met 290 295 300 Val Ala Arg Pro His Leu Trp Lys Lys Met Glu Glu Asn Pro Phe Leu 305 310 315 320 Leu Gly Ser Ser Thr Phe Gly Gly Asn Pro Leu Cys Cys Ala Gly Ala 325 330 335 Ile Ala Gly Ile Lys Thr Ile Leu Glu Glu Asn Ile Val Glu Gln Ala 340 345 350 Lys Glu Lys Gly Asp Tyr Ile Val Glu Lys Leu Ala Glu Ile Gln Lys 355 360 365 Ser Tyr Pro Glu Val Met Val Ala Val Arg Gly Lys Gly Leu Leu Ile 370 375 380 Gly Met Glu Phe Ala Thr Asn Glu Ile Gly Phe Glu Leu Ala Lys Arg 385 390 395 400 Leu Phe Asn Asp Gln Ile Leu Val Gly Gly Thr Leu Asn Asn Ala Thr 405 410 415 Val Ile Arg Ile Glu Pro Pro Ala Val Ile Thr Tyr Glu Gln Ile Asp 420 425 430 Thr Val Ile Gly Ala Ile Asp Lys His Val Ala Asn Leu Ala Lys Lys 435 440 445 Thr Ala Val Thr Ser 450 <210> 287 <211> 470 <212> PRT <213> Artificial Sequence <220> <223> Thermosporothrix hazakensis <400> 287 Met Arg Gly Asp Gly Leu Pro Gln Ala Leu His Asp Ser Gln Arg Tyr 1 5 10 15 Leu Asp Val Val Leu Lys Pro Gln Leu Ser Pro Thr Glu Ala Gln Trp 20 25 30 Leu Ile Glu Lys Thr Val Asp Asn Phe Thr Asn Tyr Phe Asn Ser Gly 35 40 45 Phe Ile Asp Tyr Arg Lys Ser Val Thr Glu Ala Gly Asp Tyr Ala Ala 50 55 60 Val Glu Trp Thr Gly Arg Gly Ala Thr Phe Lys Asp Ala Leu Gly Arg 65 70 75 80 Thr Phe Ile Asp Cys Leu Gly Gly Tyr Gly Leu Phe Asn Leu Gly Trp 85 90 95 Ala His Pro Glu Val Val Arg Ala Val Gln Thr Gln Ala Ala Lys Ser 100 105 110 Pro Leu Pro Ser Gln Glu Leu Leu Asp Pro Leu Arg Gly Met Leu Ala 115 120 125 His Leu Leu Ala Glu Ile Thr Pro Gly Asp Ile Gln Tyr Ser Phe Phe 130 135 140 Val Ser Ser Gly Thr Glu Ala Val Glu Gly Ala Met Lys Leu Ala Lys 145 150 155 160 Leu Tyr Thr Gly Lys Ser Gly Phe Ile Ala Ala Val Arg Gly Phe His 165 170 175 Gly Lys Thr Thr Gly Ser Leu Ala Leu Thr Gly Lys Ala Leu Tyr Arg 180 185 190 Arg Pro Pro Leu Pro Leu His Pro Asp Ile Tyr His Val Pro Tyr Gly 195 200 205 Asp Ala Glu Ala Val Glu Met Gln Leu Arg Ile Ala Arg Glu Val Gly 210 215 220 Asn Asp Ile Ala Ala Val Val Met Glu Pro Ile Gln Gly Glu Ala Gly 225 230 235 240 Ala Ile Val Pro Pro Asp Asp Phe Trp Pro Arg Leu Arg Gln Ile Cys 245 250 255 Asp Ala Tyr Gln Val Leu Leu Ile Ala Asp Glu Val Gln Thr Gly Met 260 265 270 Gly Arg Thr Gly Lys Met Trp Gly Val Glu His Trp Asn Val Val Pro 275 280 285 Asp Ile Met Thr Ser Ala Lys Ala Leu Gly Gly Gly Val Met Pro Val 290 295 300 Gly Ala Phe Met Ala Lys Pro Glu Ile Trp Gln Val Leu Asn Glu Asn 305 310 315 320 Pro Phe Ile His Thr Thr Thr Thr Gly Gly Asn Pro Leu Ala Cys Ala 325 330 335 Ala Ala Ile Ala Ala Ile His Val Ser Leu Arg Glu Arg Val Ala Glu 340 345 350 Gln Ala Ala Thr Lys Gly Glu Tyr Leu Leu Ala Gln Leu Arg Lys Leu 355 360 365 Ala Thr Gln Tyr Ser Asp Phe Phe Glu Asp Ile Thr Gly Lys Gly Leu 370 375 380 Leu Leu Gly Met His Phe Lys Asp Asp Glu Ile Gly Tyr Ala Ile Ser 385 390 395 400 Ala Gly Leu Phe Lys Arg Gly Val Leu Ile Ser Gly Thr Met Asn Asn 405 410 415 Ala Arg Val Ile Arg Val Glu Pro Pro Leu Val Ile Thr Arg Asp Glu 420 425 430 Ile Asp Thr Val Leu Asp Arg Leu Asp Asp Thr Leu Arg Ser Leu Arg 435 440 445 Val Ala Arg Ala Gly Glu Arg Asn Thr Asp Ala Leu Val Ala Val Lys 450 455 460 Asp Val Ala Val Ala Gly 465 470 <210> 288 <211> 466 <212> PRT <213> Artificial Sequence <220> <223> Hafnia alvei <400> 288 Met Ser Arg Thr Asn Val Val Leu Asn Pro Leu Glu Cys Thr Gln Gln 1 5 10 15 Ala Leu Asn Trp Ile Glu Lys Lys Ser Leu Thr His Asp Glu Met Val 20 25 30 Ala Leu Asn Lys Glu Val Leu Ser Asn Phe Arg Glu Tyr Val Asn Pro 35 40 45 Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Val Gly Gly Asp Tyr Gly 50 55 60 Ala Val Glu Trp Gln Ala Ser Gly Leu Asn Thr Leu Val Asp Thr Gln 65 70 75 80 Gly Asn Glu Tyr Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val 85 90 95 Gly His Arg Asn Pro Lys Val Ile Ser Ala Val Glu Ser Gln Leu Ala 100 105 110 Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ser Met 115 120 125 Leu Ala Lys Thr Leu Ala Ala Ile Thr Pro Gly Asp Leu Lys Tyr Thr 130 135 140 Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu 145 150 155 160 Ala Lys Ala Tyr Gln Ser Pro His Gly Lys Tyr Thr Phe Val Ala Ala 165 170 175 Thr Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala 180 185 190 Lys Ser Ile Phe Arg Arg Pro Phe Met Pro Leu Leu Pro Gly Phe His 195 200 205 His Val Pro Phe Gly Asp Ile Glu Ala Leu Arg Thr Gln Leu His Glu 210 215 220 Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Leu Leu Glu Pro Ile 225 230 235 240 Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Lys Gly Tyr Leu Pro Ala 245 250 255 Val Arg Ala Leu Cys Asp Glu Tyr Gly Ala Leu Leu Ile Phe Asp Glu 260 265 270 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His 275 280 285 Glu Asn Val Thr Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly 290 295 300 Gly Val Met Pro Ile Gly Ala Thr Val Ala Asn Glu Lys Val Phe Ser 305 310 315 320 Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn 325 330 335 Pro Leu Ser Cys Ala Ala Ala Leu Ala Thr Phe Asn Val Leu Leu Thr 340 345 350 Glu Asp Leu Pro Ala Lys Ala Thr Glu Arg Gly Gln Gln Leu Met Asp 355 360 365 Gly Phe Arg Arg Leu Ala Thr Gln Tyr Pro Glu Phe Met Met Glu Val 370 375 380 Arg Gly Gln Gly Leu Met Gln Ala Ile Glu Phe Ile Lys Ser Glu Val 385 390 395 400 Gly Tyr Ala Phe Ser Arg Glu Met Phe Gln Arg Asn Val Leu Val Ala 405 410 415 Gly Thr Leu Asn Asn Ser Lys Ser Ile Arg Ile Glu Pro Pro Leu Thr 420 425 430 Ile Thr Ala Glu Gln Cys Lys Gln Val Leu Thr Arg Ala Glu Glu Ala 435 440 445 Leu Lys Ala Met Arg Ala Leu Ser Pro Thr Gln Gln Pro Thr Met Ser 450 455 460 Val Ala 465 <210> 289 <211> 454 <212> PRT <213> Artificial Sequence <220> <223> Quasibacillus thermotolerans <400> 289 Met Ser Thr Glu Leu Lys Asn Lys Glu Gln Leu Ser Asn Val Ser Glu 1 5 10 15 Tyr Ile Lys Gln Val Leu Ala Leu Ile Glu Lys Glu Glu Val Thr Glu 20 25 30 Gln Glu Ala Glu Trp Val Thr Lys Glu Thr Val Asp Asn Phe Arg Glu 35 40 45 His Val Asn Pro Gly Phe Leu Ser Tyr Arg Lys Thr Val Thr Glu Gly 50 55 60 Gly Gln Phe Ala Ala Val Glu Trp Ser Asp Gly Gly Ser Cys Phe Thr 65 70 75 80 Asp Ile Ser Gly Lys Lys Tyr Ile Asp Cys Leu Gly Gly Phe Gly Ile 85 90 95 Tyr Asn Val Gly His Arg His Pro Lys Val Val Lys Ala Val Thr Asp 100 105 110 Gln Leu Asn Arg Gln Ala Leu His Ser Gln Asp Leu Leu Asp Pro Leu 115 120 125 Arg Ala Met Leu Ala Lys Ile Leu Ala Asp Ile Thr Pro Gly Asp Leu 130 135 140 Lys Tyr Ser Phe Phe Thr Asn Ser Gly Thr Glu Ser Val Glu Ala Ala 145 150 155 160 Leu Lys Leu Ala Lys Met Tyr Ser Asn Arg Ser Thr Ile Ile Ser Thr 165 170 175 Thr Arg Ser Phe His Gly Lys Ser Leu Gly Ser Leu Ser Gly Thr Ala 180 185 190 Lys Gly Val Phe Arg Lys Pro Phe Leu Pro Leu Ile Pro Gly Phe Arg 195 200 205 His Ile Pro Tyr Gly Asp Ile Asp Met Met Arg Lys Thr Phe Glu Ser 210 215 220 Cys Ala Leu Val Gly Glu Asp Val Gly Ala Val Ile Leu Glu Pro Ile 225 230 235 240 Gln Gly Glu Gly Gly Ile Ile Ile Pro Pro Ala Asp Tyr Leu Lys Glu 245 250 255 Val Arg Glu Leu Cys Asp Glu Tyr Asp Val Val Leu Ile Phe Asp Glu 260 265 270 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Ala Glu Leu 275 280 285 Cys Gly Val Thr Pro Asp Ile Ile Cys Leu Ala Lys Ala Phe Gly Gly 290 295 300 Gly Val Met Pro Ala Gly Ala Val Val Ala Asn Glu Lys Val Phe Lys 305 310 315 320 Asn Leu Phe Asp Asn Pro Phe Met His Thr Thr Thr Phe Gly Gly Asn 325 330 335 Pro Leu Ala Cys Ala Ala Ala Ile Ala Thr Ile Asp Val Leu Leu Glu 340 345 350 Glu Asn Leu Pro Glu Arg Ala Ala Glu Val Gly Asp Tyr Phe Leu Lys 355 360 365 Gly Leu Lys Glu Ala Ala Ser Gly His Glu Asp Lys Val Leu Glu Val 370 375 380 Arg Gly Gln Gly Leu Met Ile Gly Ile Glu Phe His Lys Asp Glu Ile 385 390 395 400 Gly Tyr Glu Val Ser Lys Gly Met Phe Asp Lys Gly Val Leu Val Ala 405 410 415 Gly Thr Leu Val Asn Ser Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr 420 425 430 Ile Ser Tyr Glu Glu Val Asp Thr Val Ile Arg Thr Phe Lys Glu Val 435 440 445 Leu Ser Lys Val Glu Lys 450 <210> 290 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Lelliottia <400> 290 Met Val Ile Arg Asp Pro Pro Glu Leu Ile Leu Asn Arg Leu Pro Ser 1 5 10 15 Ser Ala Ser Ala Leu Ala Cys Thr Ala His Ala Leu Asn Leu Ile Glu 20 25 30 Lys Arg Thr Leu Asp His Glu Glu Met Lys Gln Leu Asn Arg Glu Val 35 40 45 Ile Asp Tyr Phe Lys Glu His Val Asn Pro Gly Phe Leu Glu Tyr Arg 50 55 60 Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly Ala Val Glu Trp Gln Ala 65 70 75 80 Gly Ser Leu Asn Thr Leu Val Asp Thr Gln Gly Gln Glu Phe Ile Asp 85 90 95 Cys Leu Gly Gly Phe Gly Ile Phe Asn Val Gly His Arg Asn Pro Val 100 105 110 Val Val Ser Ala Val Gln Asn Gln Leu Ala Lys Gln Pro Leu His Ser 115 120 125 Gln Glu Leu Leu Asp Pro Leu Arg Ala Met Leu Ala Lys Thr Leu Ala 130 135 140 Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser Phe Phe Cys Asn Ser Gly 145 150 155 160 Thr Glu Ser Val Glu Ala Ala Leu Lys Leu Ala Lys Ala Tyr Gln Ser 165 170 175 Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr Thr Gly Ala Phe His Gly 180 185 190 Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala Lys Ser Thr Phe Arg Lys 195 200 205 Pro Phe Met Pro Leu Leu Pro Gly Phe Arg His Val Pro Phe Gly Asp 210 215 220 Ile Asn Ala Met Arg Thr Val Leu Thr Glu Cys Arg Lys Thr Gly Asp 225 230 235 240 Asp Val Ala Ala Ile Ile Leu Glu Pro Ile Gln Gly Glu Gly Gly Val 245 250 255 Ile Leu Pro Pro Gln Gly Tyr Leu Pro Ala Val Arg Lys Leu Cys Asp 260 265 270 Glu Phe Gly Ala Leu Leu Ile Leu Asp Glu Val Gln Thr Gly Met Gly 275 280 285 Arg Thr Gly Lys Met Phe Ala Cys Glu His Glu Asn Val Gln Pro Asp 290 295 300 Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly Gly Val Met Pro Ile Gly 305 310 315 320 Ala Thr Ile Ala Thr Glu Glu Val Phe Ser Val Leu Phe Asp Asn Pro 325 330 335 Phe Leu His Thr Thr Thr Phe Gly Gly Asn Pro Leu Ala Cys Ala Ala 340 345 350 Ala Leu Ala Thr Ile Asn Val Leu Leu Glu Gln Asn Leu Pro Ala Gln 355 360 365 Ala Glu Gln Lys Gly Asp Met Leu Leu Asp Gly Phe Leu Gln Leu Gly 370 375 380 Arg Glu Tyr Pro Asp Leu Val Gln Asp Ala Arg Gly Lys Gly Met Leu 385 390 395 400 Met Ala Ile Glu Phe Val Asp Asn Glu Ile Gly Tyr Asn Phe Ala Ser 405 410 415 Glu Met Phe Arg Gln Arg Val Leu Val Ala Gly Thr Leu Asn Asn Ser 420 425 430 Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr Leu Thr Ile Glu Gln Cys 435 440 445 Glu Gln Val Leu Lys Ala Ala Arg Lys Ala Leu Ala Ala Ile Arg Val 450 455 460 Ser Val Glu Glu Ala 465 <210> 291 <211> 459 <212> PRT <213> Artificial Sequence <220> <223> Aneurinibacillus thermoaerophilus <400> 291 Met Glu Thr Thr Met Asn Lys Tyr Lys Glu Val Tyr Glu Tyr Thr Ala 1 5 10 15 Lys Val Leu Asp Ile Ile Glu Lys Thr Asp Val Thr Lys Glu Glu Ala 20 25 30 Gln Trp Ile Thr Ser Glu Thr Val Asn Gly Phe Arg Glu Asn Val Asn 35 40 45 Ser Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Lys Gly Gly Gln Tyr 50 55 60 Ala Ser Val Glu Trp Lys Asp Ser Gly Leu Asn Cys Phe Ile Asp Val 65 70 75 80 Asn Gly Lys Glu Tyr Ile Asp Cys Leu Gly Gly Phe Gly Ile Tyr Asn 85 90 95 Val Gly His Arg His Pro Lys Val Val Lys Ala Val Lys Asp Gln Leu 100 105 110 Asp Lys Gln Ala Leu His Ser Gln Asp Leu Leu Asp Pro Leu Arg Ala 115 120 125 Met Leu Ala Lys Ala Leu Ala Met Leu Thr Pro Gly Asp Leu Lys Tyr 130 135 140 Ser Phe Phe Gly Asn Ser Gly Thr Glu Ala Val Glu Ala Ala Leu Lys 145 150 155 160 Leu Ala Lys Ile Tyr His His Lys Glu Gly Arg Ser Thr Phe Ile Ala 165 170 175 Thr Thr Arg Ala Phe His Gly Lys Ser Leu Gly Ser Leu Ser Gly Thr 180 185 190 Ala Lys Gly Val Phe Arg Lys Pro Phe Ile Pro Leu Val Ser Gly Phe 195 200 205 Arg His Val Ala Phe Gly Asp Ile Asp Met Met Lys Lys Thr Met His 210 215 220 Ala Cys His Met Val Gly Glu Asp Val Ala Ala Val Ile Val Glu Pro 225 230 235 240 Ile Gln Gly Glu Gly Gly Val Ile Ile Pro Pro Asp Asp Tyr Leu Pro 245 250 255 Lys Leu Arg Glu Leu Cys Asp Glu Tyr Gly Ala Leu Leu Ile Phe Asp 260 265 270 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Cys Ala Glu 275 280 285 His Tyr Gly Val Thr Pro Asp Ile Met Thr Leu Ala Lys Ala Phe Gly 290 295 300 Gly Gly Val Met Pro Ala Ser Ala Thr Ile Ala Thr Glu Glu Val Phe 305 310 315 320 Ser His Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 325 330 335 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Ile 340 345 350 Glu Glu Lys Leu Pro Glu Arg Ala Ala Glu Met Gly Glu Tyr Met Leu 355 360 365 Asn Gly Leu Arg Glu Ala Ala Lys Gly His Glu Asn Lys Val Leu Glu 370 375 380 Val Arg Gly Lys Gly Leu Leu Ile Gly Ile Glu Phe Val Ser Asp Glu 385 390 395 400 Ile Gly Tyr Glu Val Ala Lys Gly Phe Phe Asp Asn Gly Val Leu Thr 405 410 415 Ala Gly Thr Leu Ile Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu 420 425 430 Thr Ile Glu Lys Glu Gln Cys Asp Lys Val Cys Glu Thr Phe Ala Lys 435 440 445 Val Leu Lys Glu Val Asp Lys Ala Val Leu Val 450 455 <210> 292 <211> 447 <212> PRT <213> Artificial Sequence <220> <223> Buttiauxella noackiae <400> 292 Met Leu Asn Ile Ile Glu Lys Lys Ser Leu Ser His Glu Glu Met Lys 1 5 10 15 Ala Leu Asn Arg Glu Val Ile Glu Asn Phe Gln Gln His Val Asn Pro 20 25 30 Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly 35 40 45 Ala Val Glu Trp Gln Ala Asn Ser Leu Asn Thr Leu Val Asp Thr Gln 50 55 60 Gly Lys Glu Tyr Leu Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val 65 70 75 80 Gly His Arg Asn Pro Thr Val Val Ser Ala Val Gln His Gln Leu Glu 85 90 95 Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met 100 105 110 Leu Ala Lys Thr Leu Ala Thr Leu Thr Pro Gly Lys Leu Lys Tyr Ser 115 120 125 Phe Phe Ser Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Ile Lys Leu 130 135 140 Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Ala 145 150 155 160 Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala 165 170 175 Lys Ser Ala Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg 180 185 190 His Val Pro Phe Gly Asn Ile Asp Ala Leu Arg Thr Met Leu Ser Glu 195 200 205 Cys Arg Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile 210 215 220 Gln Gly Glu Gly Gly Val Ile Ile Pro Pro Ala Gly Tyr Leu Pro Ala 225 230 235 240 Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Phe Asp Glu 245 250 255 Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His 260 265 270 Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly 275 280 285 Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe Ser 290 295 300 Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn 305 310 315 320 Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile His Val Leu Leu Glu 325 330 335 Gln Asn Leu Pro Ala Gln Ala Ala Gln Lys Gly Gln Leu Leu Val Asp 340 345 350 Gly Phe Gln Ala Leu Lys Arg Glu Phe Pro Glu Leu Val Val Asp Ala 355 360 365 Arg Gly Gln Gly Leu Leu Ile Ala Ile Glu Phe Ser Asp Asn Glu Ile 370 375 380 Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Gln Val Leu Val Ala 385 390 395 400 Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Val Glu Pro Pro Leu Thr 405 410 415 Ile Thr Ile Glu Gln Cys Glu His Val Leu Gly Cys Ala Lys Lys Ala 420 425 430 Leu Thr Ser Leu Gln Val Ser Thr Leu Lys Thr Glu Leu Val Leu 435 440 445 <210> 293 <211> 452 <212> PRT <213> Artificial Sequence <220> <223> Desulfosarcina cetonica <400> 293 Met Arg Ser Tyr Lys Asp Ala Leu Ala Tyr Ser Ala Lys Trp Leu Asp 1 5 10 15 Ile Ile Lys Gln Asp Ser Ala Ser Ile Asp Glu Ala Thr Ala Lys Trp 20 25 30 Ile Ser Lys Glu Thr Lys Glu Asn Phe Val Asn His Phe Asn Ala Gly 35 40 45 Trp Val Asn Tyr Arg Lys Ser Met Thr Glu Ala Gly Asp Tyr Gly Ala 50 55 60 Val Glu Trp Arg Gly Lys Gly Ala Arg Phe Tyr Asp His Phe Gly Asn 65 70 75 80 Glu Tyr Leu Asp Phe Leu Gly Gly Tyr Gly Ala Leu Asp Leu Gly Trp 85 90 95 Ser His Pro Glu Val Val Glu Ala Val Arg Ala Gln Val Leu Lys Ser 100 105 110 Gly Ile Pro Ser Gln Glu Leu Met Asp Pro Leu Arg Gly Val Leu Ala 115 120 125 Lys Leu Leu Thr Glu Ile Thr Pro Gly Asp Ile Asp His Ala Phe Phe 130 135 140 Val Ala Ser Gly Thr Glu Ala Val Glu Gly Ala Leu Lys Ile Ala Arg 145 150 155 160 Leu His Thr Arg Lys His Ser Phe Ile Ser Thr Val Lys Ala Phe His 165 170 175 Gly Lys Thr Ser Gly Ser Leu Ser Val Met Gly Lys Lys Ala Phe Arg 180 185 190 Ala Pro Leu Gln Pro Tyr Gly Ala Gln Ile Phe Phe Val Pro Phe Gly 195 200 205 Asp Ala Asp Ala Leu Glu Arg Gln Leu Glu Ile Cys Asp Ala Val Gly 210 215 220 Ile Glu Ile Ala Gly Phe Val Ala Glu Pro Ile Gln Gly Glu Ala Gly 225 230 235 240 Ala Ile Val Pro Pro Asp Ala Tyr Trp Pro Arg Val Arg Glu Ile Cys 245 250 255 Asp Arg Phe Gly Ile Leu Met Ile Cys Asp Glu Val Gln Thr Gly Leu 260 265 270 Gly Arg Thr Gly Ala Leu Trp Gly Val Asp His Trp Asn Val Lys Pro 275 280 285 Asp Ile Met Met Ala Ala Lys Ser Leu Gly Gly Gly Val Met Pro Val 290 295 300 Gly Cys Phe Met Gly Asn Gly Arg Ile Trp Lys Ser Leu Glu Glu Pro 305 310 315 320 Asn Pro Phe Met His Thr Thr Thr Thr Gly Gly Asn Pro Leu Ala Cys 325 330 335 Ala Ala Ala Ile Ala Thr Ile Gln Val Thr Leu Arg Asp Asn Leu Pro 340 345 350 Arg Arg Ala Ala Glu Leu Gly Asp Tyr Phe Leu Cys Lys Leu Ser Val 355 360 365 Leu Ala Glu Gly Phe Pro Gly Ile Tyr Glu Lys Ile Thr Gly Lys Gly 370 375 380 Leu Leu Ile Gly Gln His Phe Lys Asp Asp Ala Val Gly Tyr Arg Val 385 390 395 400 Ala Ala Gly Leu Phe Arg Arg Lys Val Leu Val Ala Gly Thr Leu Val 405 410 415 Asn Ala Lys Ala Ile Arg Phe Glu Pro Pro Leu Val Val Thr Arg Glu 420 425 430 Glu Ile Asp Glu Val Leu Asn Arg Leu Glu Asp Thr Leu Lys Ser Val 435 440 445 Ser Lys Met Ala 450 <210> 294 <211> 492 <212> PRT <213> Artificial Sequence <220> <223> Leclercia adecarboxylata <400> 294 Met Ala Phe Ile Pro Ile Phe Ala Pro Ser Pro Asp Val Ala Gln Ser 1 5 10 15 Leu Gln Tyr Leu Ile Gln Tyr His Val Ile Arg His Ser Arg Glu His 20 25 30 Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Thr Ala 35 40 45 His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met 50 55 60 Lys Gln Leu Asn Arg Glu Val Ile Asp Tyr Phe Lys Glu His Val Asn 65 70 75 80 Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr 85 90 95 Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr 100 105 110 Gln Gly Gln Glu Phe Val Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn 115 120 125 Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu 130 135 140 Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala 145 150 155 160 Met Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr 165 170 175 Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Ile Lys 180 185 190 Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala 195 200 205 Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr 210 215 220 Ala Lys Ser Ala Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe 225 230 235 240 Arg His Val Pro Phe Gly Asp Ile Asn Ala Met Arg Ser Ala Leu Ser 245 250 255 Glu Cys Arg Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro 260 265 270 Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Ala Gly Tyr Leu Pro 275 280 285 Ala Val Arg Gln Leu Cys Asp Glu Phe Gly Ala Leu Leu Ile Leu Asp 290 295 300 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu 305 310 315 320 His Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly 325 330 335 Gly Gly Val Met Pro Ile Gly Ala Thr Val Ala Thr Glu Glu Val Phe 340 345 350 Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 355 360 365 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu 370 375 380 Glu Glu Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu 385 390 395 400 Asp Gly Phe Arg Gln Leu Gly Arg Glu Tyr Pro Asp Leu Val Gln Asp 405 410 415 Ala Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu 420 425 430 Thr Gly Tyr Ser Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val 435 440 445 Ala Gly Thr Leu Asn Asn Ser Lys Thr Ile Arg Ile Glu Pro Pro Leu 450 455 460 Thr Leu Thr Ile Glu Gln Cys Glu Leu Val Leu Lys Ala Ala Arg Gln 465 470 475 480 Ala Leu Ala Ala Leu Arg Val Ser Val Thr Glu Ala 485 490 <210> 295 <211> 459 <212> PRT <213> Artificial Sequence <220> <223> Neisseria arctica <400> 295 Met Gln Lys Thr Ser Pro Ala Ser Arg Asn Leu Asp Glu Ala Tyr Leu 1 5 10 15 Glu Ala Ser Arg Met Leu Asp Ile Val Asn Thr Pro Glu Glu Gln Leu 20 25 30 Asn Asp Glu Gln Arg His Trp Val Ser Ser Gln Val Ala Glu Asn Phe 35 40 45 Ala Asn His Val Asn Arg Gly Phe Leu Asn Tyr Arg Lys Ser Val Thr 50 55 60 Glu Thr Thr Asp Phe Ala Leu Thr Asp Trp Cys Gly Glu Gly Ser Ile 65 70 75 80 Leu Arg Asp Ile Met Gly Arg Glu Tyr Ile Asp Met Leu Gly Gly Phe 85 90 95 Gly Leu Tyr Ser Pro Gly Ile Arg His Pro Lys Ile Val Ala Ala Val 100 105 110 Lys Ala Gln Leu Asp Arg Ser Pro Gln Tyr Ser Gln Glu Met Leu Asp 115 120 125 Pro Leu Arg Gly Gln Leu Ala Lys Val Leu Ala Lys Leu Thr Pro Gly 130 135 140 Asn Leu Gln Tyr Gly Phe Phe Ala Asn Ser Gly Thr Glu Ala Val Asp 145 150 155 160 Gly Ala Met Lys Leu Ala Lys Leu Tyr Thr Gly Arg Arg Gly Phe Ile 165 170 175 Ser Thr Thr Gly Gly Phe His Gly Lys Ser Leu Gly Ala Leu Ser Leu 180 185 190 Leu Gly Lys Phe Val Tyr Arg Glu Pro Leu Leu Pro Leu Leu Gly Gly 195 200 205 Ile Arg His Val Pro Tyr Gly Asp Ala Asp Ala Val Glu Gln Leu Leu 210 215 220 Arg Ile Ala Asp Ser Val Gly Ser Met Asp Val Ala Ala Val Val Ala 225 230 235 240 Glu Pro Val Gln Gly Glu Ala Gly Ala Ile Val Pro Pro Asp Asp Tyr 245 250 255 Trp Pro Arg Leu Arg Glu Ile Cys Ser Arg Tyr Gly Val Leu Leu Ile 260 265 270 Ala Asp Glu Val Gln Thr Gly Phe Gly Arg Thr Gly Lys Val Phe Gly 275 280 285 Val Asp His Trp Gly Val Thr Pro Asp Ile Ile Cys Phe Gly Lys Ala 290 295 300 Leu Gly Gly Gly Val Val Pro Met Ser Gly Phe Phe Ser Ser Ala Glu 305 310 315 320 Ile Trp Ala Cys Leu Glu Pro Asn Pro Phe Met His Thr Thr Thr Thr 325 330 335 Gly Gly Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Gly Ile Ser Val 340 345 350 Met Leu Glu Glu Asn Leu Pro Gln Gln Ala Ala Glu Lys Gly Glu Tyr 355 360 365 Leu Met Lys Lys Ile Gly Met Leu Arg Asn Lys Tyr Pro His Ile Leu 370 375 380 Lys Asp Ile Arg Gly Lys Gly Leu Leu Leu Ala Met Val Phe Glu Asn 385 390 395 400 Asp Glu Ile Gly Tyr Lys Val Val Ser Gly Leu Phe Lys Arg Asn Val 405 410 415 Leu Thr Ser Gly Thr Leu Asn Asn Ser Ser Val Val Arg Leu Glu Pro 420 425 430 Ala Leu Asn Ile Ser Tyr Glu Leu Leu Asp Glu Val Leu Leu Arg Leu 435 440 445 Glu Asp Thr Leu Lys Ser Val Ser Glu Ala Val 450 455 <210> 296 <211> 492 <212> PRT <213> Artificial Sequence <220> <223> Citrobacter freundii <400> 296 Met Val Phe Ile Pro Ile Phe Ala Lys Arg Ala Gly Met Ala Gln Ser 1 5 10 15 Leu Gln Tyr Leu Asn Gln Tyr His Val Ile Arg Glu Leu Arg Glu His 20 25 30 Ile Leu Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser Ala 35 40 45 His Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met 50 55 60 Lys Ser Leu Asn Arg Glu Val Ile Glu Tyr Phe Lys Glu His Val Asn 65 70 75 80 Pro Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr 85 90 95 Gly Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr 100 105 110 Gln Gly Gln Glu Phe Val Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn 115 120 125 Val Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu 130 135 140 Ala Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala 145 150 155 160 Met Leu Ala Lys Thr Leu Ala Ala Leu Ala Pro Gly Lys Leu Lys Tyr 165 170 175 Ser Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys 180 185 190 Leu Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala 195 200 205 Thr Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ser Leu Ser Ala Thr 210 215 220 Ala Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe 225 230 235 240 Arg His Val Pro Phe Gly Asp Val Asn Ala Met Arg Thr Met Leu Ser 245 250 255 Glu Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro 260 265 270 Ile Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Gln Gly Tyr Leu Thr 275 280 285 Ala Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp 290 295 300 Glu Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu 305 310 315 320 His Glu Asn Val Gln Pro Asp Ile Met Cys Leu Ala Lys Ala Leu Gly 325 330 335 Gly Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe 340 345 350 Ser Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly 355 360 365 Asn Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu 370 375 380 Glu Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu 385 390 395 400 Asp Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp Leu Val His Asp 405 410 415 Val Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu 420 425 430 Ile Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val 435 440 445 Ala Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu 450 455 460 Thr Leu Thr Ile Glu Gln Cys Asp Leu Val Leu Arg Ser Thr Arg Lys 465 470 475 480 Ala Leu Ala Ala Leu Arg Val Ser Val Glu Gln Met 485 490 <210> 297 <211> 463 <212> PRT <213> Artificial Sequence <220> <223> Kluyvera intestine <400> 297 Met Asn Thr Thr Glu Leu Glu Thr Leu Ile Arg Thr Ile Leu Ser Glu 1 5 10 15 Gln Leu Thr Pro Thr Gln Glu Lys Lys Glu Ser Cys Thr Lys Gly Val 20 25 30 Phe Ala Thr Pro Ala Glu Ala Ile Asp Ala Ala His Gln Ala Phe Leu 35 40 45 Arg Tyr Gln Gln Cys Pro Leu Lys Thr Arg Gly Ala Ile Ile Gly Gly 50 55 60 Ile Arg Asp Glu Leu Ala Pro Tyr Leu Ala Glu Leu Ala Asp Glu Ser 65 70 75 80 Ala Thr Glu Thr Gly Met Gly Asn Lys Glu Asp Lys Phe Leu Lys Asn 85 90 95 Lys Ala Ala Leu Glu Asn Thr Pro Gly Ile Glu Asp Leu Thr Thr Thr 100 105 110 Ala Leu Thr Gly Asp Gly Gly Met Val Leu Phe Glu Tyr Ser Pro Phe 115 120 125 Gly Val Ile Gly Ser Val Ala Pro Ser Thr Asn Pro Thr Glu Thr Ile 130 135 140 Ile Asn Asn Ser Ile Ser Met Leu Ala Ala Gly Asn Thr Ile Tyr Phe 145 150 155 160 Ser Pro His Pro Gly Ala Lys Lys Val Ser Leu Lys Leu Ile Arg Ile 165 170 175 Ile Glu Asp Ile Ala Phe Arg His Thr Gly Ile Arg Asn Leu Val Val 180 185 190 Thr Val Ala Glu Pro Thr Phe Glu Ala Thr Gln Gln Met Met Ala His 195 200 205 Pro Lys Ile Ala Leu Leu Ala Ile Thr Gly Gly Pro Gly Ile Val Leu 210 215 220 Met Gly Leu Lys Ser Gly Lys Lys Val Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Cys Ile Val Asp Glu Thr Ala Asp Leu Val Lys Ala Ala Glu 245 250 255 Asp Ile Ile Asn Gly Ala Ser Phe Asp Tyr Asn Leu Pro Cys Ile Ala 260 265 270 Glu Lys Ser Leu Ile Val Val Asp Cys Val Ala Asp Arg Leu Met Gln 275 280 285 Gln Met Gln Ala Phe Gly Ala Leu Arg Ile Thr Gly Ala Asp Ile Asp 290 295 300 Lys Leu Arg Ala Val Cys Ile Gln Asp Gly Val Ala Asn Lys Lys Leu 305 310 315 320 Val Gly Lys Ser Pro Ser His Ile Leu Gln Ala Ala Gly Leu Ser Val 325 330 335 Pro Pro Lys Ala Pro Arg Leu Leu Ile Ala Glu Val Gln Gly Asn Asp 340 345 350 Pro Leu Val Thr Ala Glu Gln Leu Met Pro Val Leu Pro Val Val Arg 355 360 365 Val Asn Asp Phe Asp Ala Ala Leu Ala Leu Ala Leu Val Val Glu Glu 370 375 380 Gly Leu His His Thr Ala Val Met His Ser Gln Asn Val Ser Arg Leu 385 390 395 400 Asn Leu Ala Ala Arg Ser Leu Gln Thr Ser Ile Phe Val Lys Asn Gly 405 410 415 Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Phe Thr Thr Phe 420 425 430 Thr Ile Ala Thr Pro Thr Gly Glu Gly Thr Thr Ser Ala Lys Thr Phe 435 440 445 Ala Arg Ser Arg Arg Cys Val Leu Thr Asn Gly Phe Ser Ile Arg 450 455 460 <210> 298 <211> 455 <212> PRT <213> Artificial Sequence <220> <223> Peptostreptococcaceae bacterium oral <400> 298 Met Leu Asp Pro Asn Ser Met Val Asn Glu Leu Ile Arg Arg Ala Arg 1 5 10 15 Thr Ala Gln Thr Glu Phe Glu Thr Tyr Ser Gln Glu Arg Val Asp Lys 20 25 30 Ala Val Arg Ala Ile Gly Lys Ser Ile Tyr Asp His Gly Asp Glu Leu 35 40 45 Ala Lys Met Gly Ala Glu Glu Ser Gly Met Gly Arg Tyr Glu Asp Lys 50 55 60 Ile Val Lys Asn Gln Gly Lys Ser Lys Met Thr Trp Trp Arg Leu Lys 65 70 75 80 Gly Val Lys Ser Arg Gly Ile Ile Asn Ile Asp Arg Glu Lys Gln Ile 85 90 95 Tyr Glu Ile Ala Lys Pro Ile Gly Val Leu Gly Val Val Thr Pro Ala 100 105 110 Thr Asn Pro Thr Met Thr Pro Val His Asn Ala Met Ile Ala Leu Lys 115 120 125 Gly Ala Asn Ala Val Ile Ile Cys Pro His Pro Lys Thr Arg Lys Thr 130 135 140 Thr Ser Lys Thr Val Glu Tyr Met Arg Leu Ala Leu Lys Asp Ile Ser 145 150 155 160 Val Pro Glu Asp Leu Ile Gln Ile Val Asp Asp Pro Ser Ile Glu Val 165 170 175 Ser Gln Ala Leu Met Ala Phe Cys Asp Thr Thr Ile Ser Thr Gly Gly 180 185 190 Pro Gly Met Val Lys Ser Ala Tyr Ser Ser Gly Lys Pro Ala Ile Gly 195 200 205 Val Gly Pro Gly Asn Val Gln Cys Leu Val Gly Asp Asp Ala Asp Ile 210 215 220 Asp Ala Ile Val Pro Lys Ile Met Lys Gly Arg Thr Tyr Asp Asn Gly 225 230 235 240 Val Leu Cys Thr Cys Glu Gln Ser Ile Ile Cys Ala Glu Asn Leu Tyr 245 250 255 Asp Arg Leu Val Lys Gly Leu Val Asp Asn Gly Ala Tyr Phe Val Lys 260 265 270 Glu Asp Glu Val Glu Lys Leu Arg Asn Gly Phe Phe Pro Gly Gly Val 275 280 285 Met Asn Lys Asn Leu Val Gly Ser Ser Pro Phe Glu Ile Ala Lys Ala 290 295 300 Ser Gly Phe Glu Val Gln Glu Glu Ser Lys Ile Leu Leu Val Pro Val 305 310 315 320 Ser Lys Thr Gly Lys Asp Glu Phe Leu Ala Lys Glu Lys Leu Ala Pro 325 330 335 Ile Leu Ala Leu Tyr Lys Tyr Ser Glu Trp Lys Glu Ala Val Asp Ile 340 345 350 Ala Leu Lys Asn Leu Leu Asn Glu Gly Arg Gly His Ser Val Val Ile 355 360 365 His Ser Ala Asn Lys Thr Asn Ile Glu Tyr Ala Ala Asn Ile Leu Pro 370 375 380 Val Ser Arg Val Gly Val Gly Met Val Gly Ser Ser Gly Leu Gly Gly 385 390 395 400 Gly Phe Asp Asn Gly Phe Met Pro Thr Ala Thr Leu Gly Cys Gly Ser 405 410 415 Trp Gly Asn Asn Ser Ile Ala Gly Asn Val Trp Trp Asn His Leu Val 420 425 430 Asn Ile Thr Lys Leu Ala Tyr Val Leu Asn Asp Val Ser Ile Pro Thr 435 440 445 Asp Glu Glu Ile Trp Ala Glu 450 455 <210> 299 <211> 452 <212> PRT <213> Artificial Sequence <220> <223> Anaerocolumna jejuensis <400> 299 Met Asn Gln Ile Ile Gln Ser Leu Val Glu Arg Ser Arg Lys Ala Gln 1 5 10 15 Gln Ile Leu Tyr Thr Tyr Asn Gln Glu Lys Thr Asp Glu Ile Val Glu 20 25 30 Met Phe Ala Ser Val Val Phe Asn His Ala Glu Pro Leu Ala Arg Met 35 40 45 Ala Val Glu Glu Ser Arg Met Gly Val Tyr Glu Asp Lys Ile Thr Lys 50 55 60 Asn Lys Glu Lys Ala Lys Thr Ile Trp Asn Ser Leu Lys Gly Lys Lys 65 70 75 80 Ser Ile Gly Ile Ile Gly Arg Glu Glu Glu Ala Gly Leu Ile Glu Ile 85 90 95 Ala Lys Pro Met Gly Val Ile Ala Ala Ala Met Pro Cys Thr Asn Pro 100 105 110 Ile Ile Thr Pro Met Cys Asn Ala Met Phe Ala Val Lys Cys Gln Asn 115 120 125 Thr Ile Ile Val Ala Pro His Pro Arg Gly Lys Lys Cys Ala Met Ala 130 135 140 Leu Ala Glu Leu Tyr Tyr Lys Glu Leu Asp Gly Met Gly Val Pro Arg 145 150 155 160 Asp Ile Phe Leu Val Val Glu Glu Pro Thr Ile Asp Leu Thr Thr Glu 165 170 175 Leu Met Ser Ala Cys Asp Thr Val Ile Ala Thr Gly Gly Met Gly Val 180 185 190 Val Lys Ser Ala Tyr Ser Ser Gly Lys Pro Ser Tyr Gly Val Gly Pro 195 200 205 Gly Asn Val Gln Gly Leu Ile Asp Glu Gly Ile Asp Tyr Arg Ala Ala 210 215 220 Ala Gly Arg Met Ile Ala Ser Arg Ile Phe Asp Asn Gly Ile Leu Cys 225 230 235 240 Thr Ser Thr Gln Ser Ile Ile Ala Pro Glu Lys Asp Tyr Glu Ser Val 245 250 255 Ile Lys Glu Phe Val Ala Gln Gly Ala Tyr Tyr Ile Asp Asp Pro Ala 260 265 270 Val Ile Ala Ser Leu Ser Glu Val Val Phe Pro Gly Gly Val Ile Asn 275 280 285 Lys Asn Val Val Gly Gln Ser Val Lys Thr Ile Ala Gly Leu Ala Gly 290 295 300 Ile Ser Ile Pro Glu Gly Thr Lys Val Ile Ile Val Lys Pro Glu Arg 305 310 315 320 His Gly Ala Gly Val Val Trp Ser Arg Glu Lys Met Cys Pro Met Met 325 330 335 Thr Ala Tyr Ser Tyr Lys Thr Trp Glu Glu Ala Val Gln Ile Ala Tyr 340 345 350 Asp Asn Leu Leu Val Glu Gly Glu Gly His Thr Ala Asp Ile Gln Ser 355 360 365 Asp Asn Gln Ala His Ile Glu Tyr Ala Gly Val Lys Leu Pro Val Ser 370 375 380 Arg Val Val Val Asn Gln Ser Cys Ser Val Met Ala Gly Gly Ala Phe 385 390 395 400 Gly Asn Ala Leu Asn Pro Ser Ala Thr Leu Gly Cys Gly Ser Trp Gly 405 410 415 Asn Asn Ala Ile Ser Glu Asn Leu Phe Tyr Thr His Leu Met Asn Lys 420 425 430 Ser Arg Ile Ala Phe Val Arg Lys Asn Trp Lys Gln Pro Ser Asp Glu 435 440 445 Glu Ile Phe Ala 450 <210> 300 <211> 475 <212> PRT <213> Artificial Sequence <220> <223> Bacillus soli <400> 300 Met Gln Ile Asn Glu Thr Asp Ile Lys Lys Met Val Glu Gln Val Leu 1 5 10 15 Lys Gln Leu Gly Glu Ser Gln Pro Ala Ser Ala Pro Ala Ala Ser Leu 20 25 30 Lys Asp Val Ser Tyr Gly Asp Gly Val Phe Ala Thr Val Asp Glu Ala 35 40 45 Ala Glu Ala Ala Arg Leu Ala Trp Glu Lys Leu Arg Lys Leu Pro Leu 50 55 60 Ala Ala Arg Arg Gln Met Ile Glu Asn Met Arg Glu Val Ser Arg Gln 65 70 75 80 His Val Asn Glu Leu Ala Thr Leu Ala Val Glu Glu Thr Lys Leu Gly 85 90 95 Arg Val Glu Asp Lys Val Ala Lys Ile Leu Leu Ala Val Asn Lys Thr 100 105 110 Pro Gly Val Glu Asp Leu Val Ser Thr Ala Phe Ser Gly Asp Asp Gly 115 120 125 Leu Thr Leu Val Glu Tyr Ala Pro Ile Gly Val Phe Gly Ser Ile Thr 130 135 140 Pro Ser Thr Asn Pro Ala Ala Thr Ile Ile Asn Asn Ser Ile Ser Leu 145 150 155 160 Val Ala Ala Gly Asn Thr Val Val Tyr Asn Pro His Pro Ser Ala Lys 165 170 175 Arg Val Ser Ile Lys Thr Leu Gln Leu Leu Asn Gln Ala Ile Val Ala 180 185 190 Ala Gly Gly Pro Glu Asn Thr Leu Thr Ser Val Ala Ala Pro Asn Leu 195 200 205 Glu Thr Ser Ala Gln Val Met Asn His Pro Lys Val His Ala Leu Val 210 215 220 Val Thr Gly Gly Gly Pro Val Val Lys Ala Ala Met Ala Val Gly Lys 225 230 235 240 Lys Val Ile Ala Ala Gly Pro Gly Asn Pro Pro Val Val Val Asp Glu 245 250 255 Thr Ala Ile Ile Ser Lys Ala Ala Ala Asp Ile Val Gln Gly Ala Ser 260 265 270 Phe Asp Asn Asn Val Leu Cys Thr Ala Glu Lys Glu Val Phe Val Val 275 280 285 Asp Lys Val Ala Asn Ala Leu Lys Ala Glu Met Val Lys Ser Gly Ala 290 295 300 Met Glu Leu Lys Gly Phe Gln Leu Glu Lys Leu Leu Glu Lys Val Leu 305 310 315 320 Val Lys Lys Asn Asp Lys Phe Tyr Pro Asn Arg Asp Leu Ile Gly Lys 325 330 335 Asp Ala Ala Val Ile Leu Gln Ala Ala Gly Ile Gln Ala Ser Pro Ser 340 345 350 Val Lys Leu Ile Ile Ala Glu Thr Thr Lys Asp His Pro Leu Val Met 355 360 365 Thr Glu Met Leu Met Pro Ile Leu Pro Ile Val Arg Val Ser Asn Val 370 375 380 Asp Gln Ala Ile Glu Leu Ala Val Ile Ala Glu Lys Gly Asn Arg His 385 390 395 400 Thr Ala Val Met His Ser Gln Asn Ile Thr Asn Leu Thr Lys Met Ala 405 410 415 Gln Glu Ile Gln Ala Thr Ile Phe Val Lys Asn Gly Pro Ser Val Ala 420 425 430 Gly Leu Gly Phe Glu Ser Glu Gly Phe Thr Thr Leu Thr Ile Ala Gly 435 440 445 Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys Thr Phe Thr Arg Gln Arg 450 455 460 Arg Cys Val Leu Val Asp Gly Leu Arg Ile Ile 465 470 475 <210> 301 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Desnuesiella massiliensis <400> 301 Met Asn Ile Thr Glu Asn Asp Ile Glu Lys Ile Ile Gln Gln Val Leu 1 5 10 15 Val Asn Ile Thr Ser Lys Pro Ser Glu Asp Val Lys Lys Asp Ala Thr 20 25 30 Pro Glu Val Lys Ala Glu Ala Thr Pro Leu Arg Lys Lys Tyr Leu Gly 35 40 45 Val Phe Glu Lys Ala Glu Asp Ala Ile Glu Ala Ala Ser Lys Ala Gln 50 55 60 Lys Lys Leu Leu Lys Glu Phe Lys Ile Glu Asp Arg Glu Arg Phe Ile 65 70 75 80 Ile Ser Ile Lys Lys Ala Thr Val Ala Asn Ala Glu Ile Leu Ala Arg 85 90 95 Met Ile Ile Asp Glu Thr Gly Met Gly Lys Tyr Glu Asp Lys Val Leu 100 105 110 Lys His Lys Leu Val Ser Glu Lys Thr Pro Gly Thr Asp Ile Leu Thr 115 120 125 Thr Glu Ala Trp Ser Gly Asp Asn Gly Leu Thr Ile Val Glu Met Ala 130 135 140 Pro Tyr Gly Val Ile Gly Ala Val Thr Pro Ser Thr Asn Pro Ser Glu 145 150 155 160 Thr Ala Ile Cys Asn Ser Ile Gly Met Ile Gly Ala Gly Asn Ser Val 165 170 175 Val Phe Asn Ala His Pro Gly Ala Lys Glu Cys Val Ala Tyr Ala Val 180 185 190 Asp Met Met Asn Lys Ala Ile Val Glu Ala Gly Gly Pro Glu Asn Leu 195 200 205 Ile Thr Met Val Ala Glu Pro Thr Met Glu Ser Leu Glu Ala Ile Met 210 215 220 Lys His Pro Glu Ile Arg Leu Leu Cys Gly Thr Gly Gly Pro Gly Leu 225 230 235 240 Val Lys Thr Leu Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala 245 250 255 Gly Asn Pro Pro Val Ile Val Asp Asp Thr Ala Asn Val Lys Lys Ala 260 265 270 Gly Lys Asp Ile Ile Glu Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys 275 280 285 Ile Ala Glu Lys Glu Val Phe Val Phe Glu Asn Val Ala Asp Asp Leu 290 295 300 Ile Tyr His Met Leu Gln Asn Lys Ala Tyr Met Leu Thr Lys Asn Gln 305 310 315 320 Val Glu Glu Leu Val Lys Ile Val Leu His Glu Asn Ile Glu Glu Lys 325 330 335 Ala Val Gly Cys Ser Leu Asp Arg Lys Arg His Tyr Val Ile Asn Lys 340 345 350 Lys Trp Val Gly Lys Asp Ala Ala Leu Tyr Leu Lys Ala Leu Gly Ile 355 360 365 Glu Gly Lys Asp Asp Ile Gln Cys Leu Ile Cys Glu Val Asp Leu Asp 370 375 380 His Pro Phe Val Met Thr Glu Leu Met Met Pro Ile Leu Pro Ile Val 385 390 395 400 Arg Val Lys Gly Ile Asp Gln Ala Ile Ala Tyr Ala Lys Lys Ala Glu 405 410 415 His Gly Asn Arg His Ser Ala His Met His Ser Lys Asn Val Asp Asn 420 425 430 Leu Thr Arg Phe Ala Arg Glu Ile Glu Thr Thr Ile Phe Val Lys Asn 435 440 445 Ala Lys Ser Phe Ala Gly Val Gly Phe Gly Gly Glu Gly Phe Thr Thr 450 455 460 Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Ile Thr Ser Ala Arg Thr 465 470 475 480 Phe Thr Arg Gln Arg Arg Cys Val Leu Ala Glu Gly Phe Ser Ile Ile 485 490 495 <210> 302 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Caldanaerobius polysaccharolyticus <400> 302 Met Ala Gly Ile Arg Glu Glu Asp Ile Glu Leu Ile Val Arg Arg Val 1 5 10 15 Leu Ser Asn Leu Asp Leu Lys Asn Leu Lys Ala Ala Val Lys Lys Asp 20 25 30 Ile Gly Val Phe Glu Asp Met Lys Gln Ala Ile Ser Ala Ala Lys Lys 35 40 45 Ala Gln Lys Glu Leu Lys Ser Met Ser Ile Glu Phe Arg Glu Lys Ile 50 55 60 Ile Gln Asn Ile Arg Lys Lys Thr Leu Glu Asn Ala Arg Ile Met Ala 65 70 75 80 Glu Met Gly Val Gln Glu Thr Gly Met Gly Lys Val Glu His Lys Val 85 90 95 Leu Lys His Glu Leu Val Ala Arg Lys Thr Pro Gly Thr Glu Asp Ile 100 105 110 Ile Thr Thr Ala Trp Ser Gly Asp Lys Gly Leu Thr Leu Val Glu Met 115 120 125 Gly Pro Trp Gly Val Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro Ser 130 135 140 Glu Thr Val Ile Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn Ser 145 150 155 160 Val Val Phe Asn Pro His Pro Gly Ala Val Gly Val Ser Asn Tyr Ala 165 170 175 Val Arg Leu Ile Asn Glu Ala Val Val Glu Ala Gly Gly Pro Pro Asn 180 185 190 Leu Ala Val Ser Val Ala Lys Pro Thr Leu Glu Thr Ala Glu Ile Met 195 200 205 Phe Lys His Pro Asp Ile Asn Leu Leu Val Ala Thr Gly Gly Pro Gly 210 215 220 Val Val Thr Ala Val Leu Ser Thr Gly Lys Arg Ala Ile Gly Ala Gly 225 230 235 240 Ala Gly Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Arg Lys 245 250 255 Ala Ala Lys Asp Ile Val Asp Gly Ala Thr Phe Asp Asn Asn Leu Pro 260 265 270 Cys Ile Ala Glu Lys Glu Val Ile Ala Val Asn Lys Val Ala Asp Glu 275 280 285 Leu Ile Tyr Tyr Met Lys Gln Asn Gly Cys Tyr Met Ala Ser Lys Glu 290 295 300 Glu Ile Glu Glu Leu Lys Ala Met Val Leu Gln Thr Arg Asp Gly Lys 305 310 315 320 Tyr Tyr Leu Asn Arg Lys Trp Val Gly Lys Asp Ala Ser Thr Leu Leu 325 330 335 Lys Gly Ile Gly Val Asp Val Asp Asp Lys Val Arg Cys Ile Ile Phe 340 345 350 Glu Ala Thr Lys Asp His Pro Phe Val Val Glu Glu Leu Met Met Pro 355 360 365 Ile Leu Gly Ile Ile Arg Ala Glu Asn Val Asp Glu Ala Ile Ala Ile 370 375 380 Ala Val Glu Leu Glu His Gly Phe Arg His Ser Ala His Met His Ser 385 390 395 400 Lys Asn Val Asp Asn Leu Thr Lys Phe Ala Arg Ala Ile Asp Thr Ala 405 410 415 Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Ala Ile Gly Phe Gly Gly 420 425 430 Glu Gly Tyr Cys Thr Phe Thr Ile Ala Ser Arg Thr Gly Glu Gly Leu 435 440 445 Thr Ser Ala Arg Thr Phe Thr Lys Ser Arg Arg Cys Val Leu Ala Asp 450 455 460 Gly Leu Ser Ile Arg 465 <210> 303 <211> 472 <212> PRT <213> Artificial Sequence <220> <223> Cellulosilyticum sp. I15G10I2 <400> 303 Met Asn Glu Ile Glu Leu Lys Gln Val Val Glu Glu Val Val Arg Lys 1 5 10 15 Leu Gly Val Pro Ser Ala Thr Ala Pro Lys Thr Ala Pro Thr Ile Gly 20 25 30 Leu Gly Gln Gly Val Phe Glu Ser Met Asp Glu Ala Ile Thr Ala Ala 35 40 45 Lys Ala Ala Gln Glu Asp Leu His Met Met Pro Leu Glu Phe Arg Glu 50 55 60 Lys Ile Ile Ala Arg Ile Arg Glu Lys Ile Met Ala Asn Lys Glu Thr 65 70 75 80 Leu Ala Lys Met Ala Val His Glu Thr Gly Met Gly Lys Ile Gly His 85 90 95 Lys Ile Leu Lys His Glu Leu Thr Ala Lys Lys Thr Pro Gly Thr Glu 100 105 110 Cys Ile Lys Thr Arg Ala Trp Ser Gly Asp Gln Gly Leu Thr Val Ile 115 120 125 Glu Ser Gly Pro Phe Gly Val Val Gly Ala Ile Thr Pro Ser Thr Asn 130 135 140 Pro Ser Glu Thr Val Phe Cys Asn Ala Ile Gly Met Ile Ala Ala Gly 145 150 155 160 Asn Thr Val Val Phe Asn Ser His Pro Asn Ala Ala Arg Thr Ser Asn 165 170 175 Phe Ala Val Gln Leu Val Asn Glu Ala Ala Val Glu Val Gly Gly Phe 180 185 190 Glu Asn Leu Ala Thr Ser Val Leu Lys Pro Thr Val Glu Ser Gly Asn 195 200 205 Thr Leu Phe Lys His Pro Asp Ile Gln Leu Leu Val Ala Thr Gly Gly 210 215 220 Pro Gly Val Val Lys Ala Ile Leu Gln Ser Gly Lys Arg Gly Ile Ala 225 230 235 240 Ala Gly Ala Gly Asn Pro Pro Val Leu Val Asp Glu Thr Ala Asn Ile 245 250 255 Lys Lys Ala Ala Ala Asp Ile Ile Asn Gly Ala Thr Phe Asp Asn Asn 260 265 270 Leu Pro Cys Ile Ala Glu Lys Glu Val Ile Val Val Asn Glu Val Ala 275 280 285 Asp Glu Leu Ile His Tyr Met Thr Ser Glu Asn Asp Cys Tyr Met Leu 290 295 300 Lys Gly Glu Gln Ile Glu Lys Leu Ala Gln Thr Ile Leu Val Glu Lys 305 310 315 320 Asn Gly His Tyr Ile Val Asn Arg Asp Tyr Val Gly Arg Asp Ala His 325 330 335 Val Ile Leu Lys Gly Ile Gly Ile Glu Ala Pro Glu Ser Ile Arg Cys 340 345 350 Ile Ile Phe Glu Ala Ser Lys Glu His Ile Leu Val Val Glu Glu Leu 355 360 365 Met Met Pro Val Leu Gly Ile Val Arg Val Ala Asn Val Asp Glu Gly 370 375 380 Ile Ala Val Ala Lys Val Leu Glu Gly Gly Asn Arg His Ser Ala His 385 390 395 400 Met His Ser Ser Asn Val Tyr Asn Leu Thr Lys Tyr Gly Arg Ala Leu 405 410 415 Asp Thr Ala Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Gly Ile Gly 420 425 430 Phe Gly Gly Glu Gly Phe Ala Thr Phe Thr Ile Ala Ser Lys Thr Gly 435 440 445 Glu Gly Leu Thr Asn Ala Ala Ser Phe Thr Lys Ser Arg Arg Cys Val 450 455 460 Met Ala Asp Ala Leu Tyr Ile Arg 465 470 <210> 304 <211> 455 <212> PRT <213> Artificial Sequence <220> <223> Geosporobacter ferrireducens <400> 304 Met Ile Val Lys Lys Ile Leu Thr Glu Ile Thr Leu Lys Asn Glu Ala 1 5 10 15 Thr Asp Ser Ala Tyr Gly Ile Phe Asp His Met Glu Glu Ala Ile Glu 20 25 30 Ala Ala Trp Ile Ala Gln Lys Glu Leu Val Lys Tyr Ser Leu Glu Cys 35 40 45 Arg Gly Lys Phe Ile Ala Ala Met Arg Ala Ala Ala Arg Lys Asn Ile 50 55 60 Glu Leu Phe Ser Lys Met Ala Val Glu Glu Thr Gly Met Gly Arg Tyr 65 70 75 80 Glu His Lys Val Met Lys Asn Thr Val Ala Ile Glu Lys Thr Pro Gly 85 90 95 Ile Glu Asp Leu Lys Pro Asp Ala Val Ser Gly Asp His Gly Leu Thr 100 105 110 Val Phe Glu Leu Ser Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro Thr 115 120 125 Thr Asn Pro Thr Glu Thr Val Ile Cys Asn Ala Ile Gly Met Ile Ala 130 135 140 Ala Gly Asn Ala Val Val Phe Ala Pro His Pro Arg Ala Lys Asn Thr 145 150 155 160 Ser Arg Lys Ala Ile Glu Ile Leu Asn Gln Ala Ile Ile Glu Ala Gly 165 170 175 Gly Pro Ala Asn Leu Ile Thr Ala Ile Lys Glu Pro Thr Ile Glu Ser 180 185 190 Ala Asn Ile Met Met Gln His Lys Lys Ile Lys Met Leu Val Ala Thr 195 200 205 Gly Gly Pro Asp Val Val Arg Thr Val Leu Ser Ser Gly Lys Lys Ala 210 215 220 Ile Gly Ala Gly Ala Gly Asn Pro Pro Ala Val Val Asp Glu Thr Ala 225 230 235 240 Asp Ile Glu Lys Ala Ala Lys Asp Ile Ile Asp Gly Cys Ser Phe Asp 245 250 255 Asn Asn Leu Pro Cys Val Ala Glu Lys Glu Val Ile Val Val Asp Ser 260 265 270 Val Ala Asp Tyr Leu Ile Phe Asn Met Gln Lys His Asn Ala Tyr Leu 275 280 285 Leu Ser Asp Glu Asn Leu Ile Lys Lys Leu Glu Lys Leu Val Phe Asn 290 295 300 Asp Lys Gly His Leu Asn Arg Asp Leu Val Gly Lys Asp Ala Asp Tyr 305 310 315 320 Ile Leu Arg Lys Ile Gly Val Asp Cys Asp Pro Ser Ile Arg Ala Ile 325 330 335 Ile Val Glu Thr Asp Lys Asn His Asp Phe Val Gln Glu Glu Leu Met 340 345 350 Met Pro Ile Leu Pro Ile Val Arg Val Lys Asp Val Asn Glu Ala Ile 355 360 365 Glu Leu Ala Val Glu Val Glu His Gly Tyr Arg His Thr Ala Ile Ile 370 375 380 His Ser Lys Asn Ile Asp Asn Leu Ser Lys Met Ala Lys Glu Ile Gln 385 390 395 400 Thr Thr Ile Phe Val Lys Asn Gly Pro Ser Tyr Ala Gly Ile Gly Val 405 410 415 Gly Gly Glu Gly Tyr Ser Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu 420 425 430 Gly Leu Thr Thr Ala Lys Ser Phe Thr Arg Ser Arg Arg Cys Val Leu 435 440 445 Val Asp Gly Phe Ser Ile Arg 450 455 <210> 305 <211> 465 <212> PRT <213> Artificial Sequence <220> <223> Bacillus korlensis <400> 305 Met Ile Glu Val Lys Gln Ile Glu Asp Ile Val Met Gln Val Leu Ala 1 5 10 15 Gly Leu Asn Asn His Glu Asp Pro Pro Leu Asp Gly Glu Asn Gly Leu 20 25 30 Tyr Ser Glu Met Asn Asp Ala Ile Asp Ala Ala Phe Val Ala Gln Lys 35 40 45 Glu Leu Val Lys Leu Ser Leu Ala Glu Arg Gly Arg Ile Ile Glu Ser 50 55 60 Ile Arg Thr Glu Phe Arg Lys His Ile Glu Leu Leu Ser Glu Met Ala 65 70 75 80 Val Glu Glu Thr Gly Met Gly Arg Val Lys Asp Lys Ile Asn Lys Asn 85 90 95 Leu Val Ala Val Asn Asn Thr Pro Gly Ile Glu Asp Leu Thr Thr Ala 100 105 110 Ala Cys Ser Gly Asp Asn Gly Leu Thr Val Glu Glu Leu Ser Pro Tyr 115 120 125 Gly Val Ile Gly Ser Ile Thr Pro Thr Thr Asn Pro Ser Glu Thr Ile 130 135 140 Ile Cys Asn Thr Ile Gly Met Leu Ala Ala Gly Asn Ala Ile Val Phe 145 150 155 160 Ser Pro His Pro Thr Ala Lys Arg Thr Ser Ile Glu Thr Ile Lys Ile 165 170 175 Ile Ser Lys Ala Ile Ser Lys Ala Gly Gly Pro Lys Asn Leu Val Val 180 185 190 Ser Thr Leu Gln Pro Ser Ile Glu Gln Ala Asn Ile Met Met Asn His 195 200 205 Lys Lys Val Arg Met Leu Val Ala Thr Gly Gly Pro Ala Val Val Lys 210 215 220 Ala Val Leu Ser Thr Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Glu Lys Ala Ala Lys 245 250 255 Asp Ile Ile Asp Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys Val Ala 260 265 270 Glu Lys Glu Val Ile Ala Val Asp Cys Ile Ala Asp Cys Leu Ile Glu 275 280 285 Asn Met Lys Asn Asn Gly Ala Tyr Gln Leu Thr Asp Pro Val Gln Ile 290 295 300 Gln Arg Leu Val Asp Leu Val Val Arg Asn Gly His Ala Asn Lys Asp 305 310 315 320 Phe Val Gly Lys Asn Ala Asp Phe Ile Leu Arg Gln Leu Gly Ile Glu 325 330 335 Val Gly Pro Glu Val Arg Val Val Ile Val Asp Val Lys Tyr Glu Gly 340 345 350 Arg His Pro Leu Val Leu Ala Glu Leu Met Met Pro Val Leu Pro Ile 355 360 365 Val Arg Val Asn Asn Val Asp Glu Gly Ile Asp Leu Ala Val Glu Val 370 375 380 Glu His Gly Phe Arg His Thr Ala Ile Met His Ser Lys Asn Ile Asp 385 390 395 400 Asn Leu Thr Lys Phe Ala Lys Glu Ile Gln Thr Thr Ile Phe Val Lys 405 410 415 Asn Gly Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Val Gly Tyr Thr 420 425 430 Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys 435 440 445 His Phe Ala Arg Lys Arg Arg Cys Val Leu Val Asp Gly Leu Ser Ile 450 455 460 Arg 465 <210> 306 <211> 459 <212> PRT <213> Artificial Sequence <220> <223> Acidaminococcus massiliensis <400> 306 Met Glu Gln Ala Val Lys Asp Tyr Leu Asp Lys Met Val Ala Ala Ser 1 5 10 15 Arg Ile Ala Gln Gln Glu Phe Ala Thr Tyr Pro Gln Glu Thr Val Asp 20 25 30 Lys Ala Val Arg Thr Val Gly Lys Ala Ile Tyr Asp Asn Ala Glu Leu 35 40 45 Leu Ala His Met Ala Val Asp Glu Thr Lys Met Gly Asn Tyr Ala Asp 50 55 60 Lys Ile Ala Lys Cys Val Asn Lys Ser Lys Ser Val Trp Trp Arg Met 65 70 75 80 Lys Asp Lys Lys Ser Arg Gly Ile Ile Lys Arg Ile Pro Glu Leu Gly 85 90 95 Leu Val Glu Val Ala Lys Pro Ile Gly Val Ile Gly Cys Val Ala Pro 100 105 110 Thr Thr Asn Pro Val Ile Asn Val Met Gln Asn Ala Met Cys Ala Leu 115 120 125 Lys Cys Gly Asn Ser Met Ile Val Ser Pro His Pro Arg Ala Lys His 130 135 140 Ser Ser Val Lys Thr Val Glu Val Ile Asn Glu Ala Leu Ala Ala Leu 145 150 155 160 Gly Met Pro Lys Asn Leu Ile Gln Val Ile Thr Glu Pro Ser Met Glu 165 170 175 Leu Ser Ala Gly Leu Met Ser Ala Val Asp Leu Cys Ile Cys Thr Gly 180 185 190 Gly Pro Gly Leu Val Lys Ala Ala Tyr Ser Ser Gly Lys Pro Ala Ile 195 200 205 Gly Val Gly Gln Gly Asn Val Gln Val Leu Val Asp Arg Asp Ala Asp 210 215 220 Leu Asp Gln Val Ala Ala Met Val Ile Lys Gly Arg Thr Phe Asp Asn 225 230 235 240 Gly Val Leu Cys Thr Cys Glu Gln Asn Val Ile Cys Pro Glu Asp Lys 245 250 255 Lys Glu Glu Met Ile Ala Ala Leu Lys Lys His Gly Ala Tyr Tyr Ile 260 265 270 Gly Asn Ser Glu Asp Ala Ala Lys Leu Arg Asp Thr Ala Phe Pro Asn 275 280 285 Gly Gly Pro Val Ser Lys Glu Tyr Pro Gly Ala Ser Val Lys Lys Ile 290 295 300 Ala Gln Leu Ser Gly Ile Gln Gly Ile Pro Glu Asp Ala Lys Val Ile 305 310 315 320 Val Ser Cys Thr Arg Gly Tyr Gly Lys Asp Glu Pro Leu Ala Lys Glu 325 330 335 Lys Leu Phe Pro Val Leu Ala Phe Phe Thr Tyr Asp Lys Trp Glu Asp 340 345 350 Ala Ile His Ile Ala Lys Thr Asn Leu Glu Met Glu Gly Ile Gly His 355 360 365 Ser Val Val Ile His Ser Asn Thr Pro Glu His Ile Glu Ala Val Ala 370 375 380 Glu Ala Ile Pro Val Ser Arg Phe Ala Val Asn Gln Val Gly Gly Thr 385 390 395 400 Asn Leu Gly Gly Ala Met Asp Asn Gly Leu Asn Pro Thr Thr Thr Leu 405 410 415 Gly Cys Gly Thr Trp Gly Asn Asn Ser Ile Ser Glu Asn Phe Thr Tyr 420 425 430 Tyr His Leu Met Asn Leu Thr Arg Val Ser Tyr Arg Val Pro Asp Met 435 440 445 Tyr Ile Pro Thr Asp Glu Glu Ile Trp Ala Glu 450 455 <210> 307 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Lachnospiraceae bacterium 32 <400> 307 Val Ser Val Asn Glu Lys Met Val Gln Asp Val Val Lys Glu Val Met 1 5 10 15 Ala Lys Leu Gln Leu Ala Ala Gly Ala Ser Glu Gly Lys Gly Ile Phe 20 25 30 Ala Asp Met Asn Asp Ala Ile Ala Ala Ala Lys Lys Ala Gln Arg Tyr 35 40 45 Ile His Arg Met Ser Met Asp Gln Arg Glu Gln Ile Ile Ser Asn Ile 50 55 60 Arg Arg Lys Thr Lys Glu Asn Ala Glu Ile Leu Ala Arg Met Gly Val 65 70 75 80 Glu Glu Thr Gly Met Gly Asn Val Pro His Lys Ile Leu Lys His Gln 85 90 95 Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Lys Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Ile Ile 130 135 140 Cys Asn Thr Ile Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Val Lys Thr Ser Gln Phe Ala Val Asn Met Leu 165 170 175 Asn Glu Ala Ser Ile Glu Ala Gly Gly Pro Glu Asn Ile Ala Cys Thr 180 185 190 Val Gly Lys Pro Thr Met Glu Ser Ser Asn Ile Met Met Lys His Lys 195 200 205 Asp Ile Gln Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Arg Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Gly Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Asp Ser Val Val Ser Glu Leu Met His Tyr 275 280 285 Met Val Asn Glu Gln Asp Cys Tyr Leu Ala Ser Lys Glu Glu Gln Asp 290 295 300 Lys Leu Thr Ala Thr Val Leu Thr Pro Lys Gly Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Lys Thr Leu Leu Gly Met Ile Gly Val Thr Val 325 330 335 Pro Asp Asn Ile Arg Cys Ile Val Phe Glu Gly Glu Lys Glu His Pro 340 345 350 Leu Ile Ala Thr Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Lys Asp Phe Glu Asp Ala Val Glu Lys Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Ile Asp Asn Ile Thr 385 390 395 400 Arg Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Ala Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Phe Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Ser Glu Ser Leu Cys Ile Arg 450 455 460 <210> 308 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Eubacterium plexicaudatum <400> 308 Val Ser Val Asn Asp Gln Met Val Gln Asp Ile Val Arg Gln Val Leu 1 5 10 15 Ala Asn Met Arg Ile Ser Ser Asp Ala Ser Gly Ser Arg Gly Val Phe 20 25 30 Ser Asp Met Asn Glu Ala Val Glu Ala Ala Lys Lys Ala Gln Ala Val 35 40 45 Ile Gly Lys Met Pro Met Asp His Arg Glu Lys Ile Ile Ser Ser Ile 50 55 60 Arg Ala Lys Ile Met Glu Asn Ala Glu Ile Leu Ala Arg Met Gly Val 65 70 75 80 Lys Glu Thr Gly Met Gly Asn Val Gly His Lys Ile Leu Lys His Gln 85 90 95 Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Lys Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Ile Leu 130 135 140 Cys Asn Thr Ile Gly Met Val Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Phe Ala Val Asn Leu Val 165 170 175 Asn Glu Ala Ser Val Glu Ala Gly Gly Pro Asp Asn Ile Ala Cys Thr 180 185 190 Val Glu His Pro Thr Leu Asp Thr Ser Ala Ile Met Met Lys His Lys 195 200 205 Asp Ile His Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Glu Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Asp Ser Ile Ala Asp Glu Leu Met His Tyr 275 280 285 Met Ile Ser Glu Gln Gly Cys Tyr Leu Ala Ser Ala Lys Glu Gln Glu 290 295 300 Ala Leu Ile Ser Val Val Leu Lys Gly Gly Gln Leu Asn Arg Asp Cys 305 310 315 320 Val Gly Arg Asp Ala Lys Thr Leu Leu Gly Met Ile Gly Val Gln Ala 325 330 335 Pro Asp Asn Ile Arg Cys Ile Thr Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Thr Glu Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Asp Ser Phe Glu Asp Ala Val Glu Lys Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Val Asp His Ile Thr 385 390 395 400 Thr Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Gly Pro 405 410 415 Ser Tyr Ala Ala Ile Gly Phe Gly Gly Glu Gly Tyr Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Ala Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Cys Asp Ser Leu Cys Ile Arg 450 455 460 <210> 309 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Clostridium sp. KNHs205 <400> 309 Val Asn Leu Lys Glu Ala Gln Val Lys Asp Ile Val Arg Lys Val Leu 1 5 10 15 Leu Gln Met Glu Ala Ser Asn Lys Glu Glu Gln Lys Leu Ser Gly Ile 20 25 30 Phe Thr Glu Met Asn Asp Ala Ile Gly Ala Ser Ile Lys Ala Gln Lys 35 40 45 Val Met Gln Gln Leu Ser Met Asp Ser Arg Glu Lys Ile Ile Ser Asn 50 55 60 Ile Arg Lys Lys Thr Leu Glu Asn Ala Glu Leu Phe Ala Arg Met Gly 65 70 75 80 Val Glu Glu Thr Gly Met Gly Asn Val Gly His Lys Ile Leu Lys His 85 90 95 Gln Leu Leu Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Ser Thr Val 100 105 110 Ala Trp Ser Gly Asp Arg Gly Leu Thr Leu Val Glu Met Gly Pro Phe 115 120 125 Gly Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Ile 130 135 140 Leu Cys Asn Ser Ile Gly Met Ile Ala Gly Gly Asn Thr Val Val Phe 145 150 155 160 Asn Pro His Pro Ala Ala Ile Gly Val Ser Asn Leu Ala Val His Met 165 170 175 Val Asn Glu Ala Ser Arg Glu Ala Gly Gly Pro Asp Asn Ile Ala Val 180 185 190 Ser Val Val Lys Pro Thr Leu Ala Ser Gly Asp Ile Met Met Lys His 195 200 205 Gln Asn Ile Pro Leu Ile Val Ala Thr Gly Gly Pro Gly Val Val Thr 210 215 220 Thr Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Val Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Met 245 250 255 Asp Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala 260 265 270 Glu Lys Glu Val Val Ala Val Gly Lys Ile Met Asp Glu Leu Leu His 275 280 285 Tyr Leu Ile Glu Asn Gly Cys Tyr Val Ile Ser Lys Glu Glu Gln Glu 290 295 300 Lys Leu Thr Ala Val Val Leu Lys Asp Asn Arg Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Lys Asp Ala Arg Thr Ile Leu Ser Met Ile Gly Ile Glu Thr 325 330 335 Pro Glu Asn Ile Arg Cys Ile Ile Phe Glu Gly Glu Lys Glu His Pro 340 345 350 Leu Ile Ala Glu Glu Leu Met Met Pro Ile Leu Gly Ile Val Arg Ala 355 360 365 Lys Asp Ile Asp Asp Ala Ile Glu Lys Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Met His Ser Lys Asn Val Asp Asn Leu Thr 385 390 395 400 Arg Phe Gly Lys Ala Val Asp Thr Ala Ile Phe Val Lys Asn Ala Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Phe Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Arg Thr Phe Thr 435 440 445 Lys Gln Arg Arg Cys Val Met Ala Asp Ser Leu Cys Ile Arg 450 455 460 <210> 310 <211> 470 <212> PRT <213> Artificial Sequence <220> <223> Robinsoniella peoriensis <400> 310 Met Ala Ile Asn Glu Gln Glu Ile Gln Asp Ile Val Arg Ser Val Leu 1 5 10 15 Lys Gly Met Gly Thr Thr Ala Asp Lys Pro Ala Gly Ser Ser Lys Lys 20 25 30 Leu Leu Gly Val Phe Asp Asp Ile Asn Asp Ala Ile Ala Ala Ala Lys 35 40 45 Glu Ala Gln Lys Glu Ile Gln Pro Met Pro Leu Glu Phe Arg Glu Lys 50 55 60 Ile Ile Ser Asn Ile Arg Lys Lys Thr Leu Glu Asn Ala Lys Met Phe 65 70 75 80 Ala Glu Leu Gly Val Glu Glu Thr Gly Met Gly Asn Val Gly His Lys 85 90 95 Ile Leu Lys His Gln Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp 100 105 110 Leu Ser Thr Val Ala Trp Ser Gly Asp Arg Gly Leu Thr Leu Val Glu 115 120 125 Met Gly Pro Phe Gly Val Ile Gly Ala Val Cys Pro Ser Thr Asn Pro 130 135 140 Thr Glu Thr Val Val Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn 145 150 155 160 Thr Val Val Phe Ala Pro His Pro Ser Ala Lys Asn Val Ser Asn Leu 165 170 175 Ala Ile Asp Met Ile Asn Arg Ala Ser Val Glu Val Gly Gly Pro Glu 180 185 190 Asn Ile Ala Val Ala Val Lys Glu Pro Thr Met Glu Val Ser Lys Val 195 200 205 Ile Phe Ser His Lys Asp Ile Ser Leu Leu Val Ala Thr Gly Gly Pro 210 215 220 Gly Val Val Thr Thr Val Leu Ser Ser Gly Lys Arg Ala Met Gly Ala 225 230 235 240 Gly Ala Gly Asn Pro Pro Val Leu Val Asp Glu Thr Ala Asn Ile Pro 245 250 255 Lys Ala Ala Glu Asp Ile Ile Asn Gly Cys Thr Phe Asp Asn Asn Leu 260 265 270 Pro Cys Ile Ala Glu Lys Glu Val Val Ala Val Asp Met Ile Ala Asp 275 280 285 Glu Leu Ile Tyr His Met Glu Gln Val Gly Cys Tyr His Ala Asn Ala 290 295 300 Glu Glu Val Gln Lys Leu Ile Gln Thr Val Phe Ile Glu Asn Asn Gly 305 310 315 320 Lys Arg Thr Leu Asn Arg Gln Cys Val Gly Arg Ser Ala Lys Val Leu 325 330 335 Leu Gly Lys Ile Gly Val Thr Val Gly Asp Glu Ile Arg Cys Ile Ile 340 345 350 Phe Glu Gly Glu Lys Thr Asn Pro Met Ile Trp Glu Glu Leu Met Met 355 360 365 Pro Ile Leu Gly Ile Val Arg Val Lys Asn Val Glu Glu Gly Met Gly 370 375 380 Ile Ala Leu Glu Leu Glu His Gly Asn Arg His Ser Ala His Met His 385 390 395 400 Ser Thr Asn Val Asn Asn Leu Thr Lys Phe Gly Lys Met Ile Asp Thr 405 410 415 Ala Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Ala Leu Gly Phe Gly 420 425 430 Gly Glu Gly Tyr Pro Thr Phe Thr Ile Cys Ser Arg Thr Gly Glu Gly 435 440 445 Leu Thr Ser Ala Lys Asn Phe Thr Lys Ser Arg Arg Cys Val Met Gly 450 455 460 Asp Ala Leu Cys Ile Arg 465 470 <210> 311 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Caldithrix abyssi <400> 311 Met His Leu Asp Asp Lys Gln Ile Ala Gln Ile Val Glu Thr Val Leu 1 5 10 15 Ser Arg Leu Glu Arg Asn Glu Ser Arg Thr Gly Arg Ser Arg His Pro 20 25 30 Gln Gly Val Phe Glu Thr Leu Asp Glu Ala Val Glu Ala Ala Arg Gln 35 40 45 Ala Gln Lys Lys Ile Arg Lys Leu Glu Leu Arg Ala Lys Ile Ile Gln 50 55 60 Ala Ile Arg Gln Ala Gly Val Lys His Ala Arg Glu Leu Ala Glu Met 65 70 75 80 Ala Val Gln Glu Thr Gly Met Gly Arg Val Glu Asp Lys Ile Ala Lys 85 90 95 Asn Ile Ser Gln Ala Glu Lys Thr Pro Gly Ile Glu Asp Leu Gln Pro 100 105 110 Leu Ala Leu Ser Gly Asp His Gly Leu Thr Leu Ile Glu Asn Ala Ala 115 120 125 Trp Gly Val Ile Ala Ser Val Thr Pro Ser Thr Asn Pro Gly Ala Thr 130 135 140 Val Ile Asn Asn Ser Ile Ser Met Ile Ala Ala Gly Asn Ala Val Val 145 150 155 160 Tyr Ala Pro His Pro Ala Ala Lys Lys Val Ser Gln Arg Ala Ile Glu 165 170 175 Ile Leu Asn Lys Ala Ile Glu Ala Ala Gly Gly Pro Ala Thr Leu Leu 180 185 190 Thr Thr Val Ala Glu Pro Ser Ile Glu Thr Ala Gln Lys Leu Phe Val 195 200 205 Tyr Pro Gly Ile Asp Leu Leu Val Val Thr Gly Gly Glu Ala Val Val 210 215 220 Lys Ala Ala Arg Lys Val Thr Asp Lys Arg Leu Met Ala Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Ala Lys Ala 245 250 255 Ala Arg Asp Ile Val Trp Gly Ala Ser Phe Asp Asn Asn Ile Val Cys 260 265 270 Ala Asp Glu Lys Glu Ile Ile Ala Val Asp Ala Ile Ala Asp Arg Leu 275 280 285 Lys Glu Glu Met Lys Lys His Gln Ala Val Glu Leu Thr Pro Gln Gln 290 295 300 Gly Glu Glu Leu Ala Gln Ile Ile Leu Glu Asp Tyr Pro Gly Pro Asn 305 310 315 320 Ala Arg Ile Asn Arg Lys Trp Val Gly Lys Asp Ala Tyr Lys Phe Ala 325 330 335 Arg Glu Ile Gly Leu Asn Val Ser Lys Glu Thr Arg Leu Leu Phe Val 340 345 350 Glu Ala Asp Lys Asp His Pro Phe Ala Gln Leu Glu Leu Met Met Pro 355 360 365 Val Ile Pro Leu Ile Arg Ala Ala Asp Ala Asp Lys Ala Ile Asp Leu 370 375 380 Ala Ile Glu Leu Glu His Gly Tyr Arg His Thr Ala Ala Met His Ser 385 390 395 400 Arg His Ile Asp His Met Asp Arg Met Ala Asn Glu Ile Asn Thr Ser 405 410 415 Ile Phe Val Lys Asn Gly Pro Cys Leu Ala Gly Leu Gly Phe Gly Gly 420 425 430 Glu Gly Trp Thr Ser Met Thr Ile Thr Thr Pro Thr Gly Glu Gly Val 435 440 445 Thr Ser Ala Arg Ser Phe Val Arg Leu Arg Arg Cys Val Val Val Asp 450 455 460 His Phe Arg Ile Val 465 <210> 312 <211> 479 <212> PRT <213> Artificial Sequence <220> <223> Sporomusa sphaeroides <400> 312 Met Thr Ile Asp Pro Asn Leu Ile Ala Lys Ile Ala Ala Glu Val Met 1 5 10 15 Ala Arg Val Gln Glu Arg Gln Pro Glu Thr Val Ser Ala Gly Glu Gly 20 25 30 Ile Phe Pro Thr Val Asp Glu Ala Val Ala Ala Ala Arg Ala Ala Gln 35 40 45 Lys Gln Leu Lys Lys Leu Ser Ile Glu Lys Arg Glu Glu Leu Ile Gln 50 55 60 Ala Met Arg Gln Ala Ala Cys Asp Asn Ala Glu Leu Leu Ala Glu Met 65 70 75 80 Gly Val Ser Glu Ser Gly Met Gly Arg Val Ser Asp Lys Val Ile Lys 85 90 95 Asn Arg Leu Ala Ala Thr Lys Thr Pro Gly Thr Glu Asp Leu Lys Ser 100 105 110 Glu Ala Trp Ser Gly Asp Arg Gly Leu Thr Leu Ile Glu Met Gly Pro 115 120 125 Tyr Gly Val Ile Gly Ser Ile Thr Pro Thr Thr Asn Pro Ser Glu Thr 130 135 140 Val Ile Cys Asn Gly Ile Gly Met Ile Ala Ala Gly Asn Ala Val Val 145 150 155 160 Phe Ser Pro His Pro Thr Ala Lys Asn Thr Ser Leu Val Thr Ile Lys 165 170 175 Leu Leu Asn Lys Ala Ile Ile Gln Ala Gly Gly Pro Pro Asn Leu Leu 180 185 190 Thr Ala Val Ala Glu Pro Ser Leu Ala Ala Thr Asn Ala Met Met Gln 195 200 205 His Pro Asp Ile Asn Met Leu Val Ala Thr Gly Gly Pro Ala Val Val 210 215 220 Lys Ala Val Met Ser Cys Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly 225 230 235 240 Asn Pro Pro Ala Val Val Asp Glu Thr Ala Asp Ile Glu Lys Ala Ala 245 250 255 Lys Asp Ile Ile Asp Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys Ile 260 265 270 Ala Glu Lys Glu Val Ile Val Val Gly Ser Val Ala Asp Lys Leu Met 275 280 285 Ala Tyr Met Gln Arg Tyr Gly Ala Tyr Leu Ile Ser Gly Pro Asp Val 290 295 300 Asp Arg Leu Ala Lys Val Ile Leu Thr Glu Lys Ala Glu Leu Ala Ala 305 310 315 320 Ala Gly Cys Thr Glu Lys Pro Lys Lys Ser Tyr Ala Val Asn Lys Asn 325 330 335 Tyr Val Gly Lys Asp Ala Arg Tyr Ile Leu Ser Gln Ile Gly Ile Gln 340 345 350 Val Pro Asp Ser Ile Arg Ala Val Ile Cys Glu Thr Pro Ala Asp His 355 360 365 Pro Phe Val Val Glu Glu Leu Met Met Pro Val Leu Pro Val Val Gln 370 375 380 Val Lys Asp Ile Asp Ala Ala Ile Glu Leu Ala Val Lys Val Glu His 385 390 395 400 Gly Asn Arg His Thr Ala Ile Met His Ser Lys Asn Val Asp Asn Leu 405 410 415 Thr Lys Leu Ala Lys Ala Ile Glu Thr Thr Ile Phe Val Lys Asn Ala 420 425 430 Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Phe Thr Thr Phe 435 440 445 Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Pro Arg Ser Phe 450 455 460 Thr Arg Gln Arg Arg Cys Val Leu Val Asp Ala Leu Ser Ile Val 465 470 475 <210> 313 <211> 524 <212> PRT <213> Artificial Sequence <220> <223> Bacillus sp. FJAT-25547 <400> 313 Met Gly Val Asn Met Ser Glu Gln Asp Ile Gln Lys Ile Ile Gln Ser 1 5 10 15 Val Leu Gln Asn Ile Glu Ala Val Ser Glu Gln Asn Ser Gly His Gln 20 25 30 Val Leu His Ser Asn Asp Asn Thr Asn Pro Pro Lys Pro Leu Lys Met 35 40 45 Lys Arg Val Leu Pro Leu Ser Gln Gln Ile Asn Thr Ala Glu Leu Ser 50 55 60 His Gln Val Asn Glu Pro Gly Ala Asn Gly Val Phe Val Arg Ile Glu 65 70 75 80 Asp Ala Ile Glu Ala Gly Tyr Ile Ala Gln Leu Asn Tyr Val Lys His 85 90 95 Phe Gln Leu Lys Asp Arg Glu Lys Ile Ile Ala Ala Ile Arg Glu Ala 100 105 110 Val Ile Glu Asn Lys Glu Lys Leu Ala Gln Met Val Phe Glu Glu Thr 115 120 125 Lys Leu Gly Arg Tyr Glu Asp Lys Ile Ala Lys His Glu Leu Val Ala 130 135 140 Ser Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Ala Ala Phe Ser Gly 145 150 155 160 Asp Glu Gly Leu Thr Ile Val Glu Gln Ala Pro Phe Gly Leu Val Gly 165 170 175 Ala Val Thr Pro Val Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn Ser 180 185 190 Ile Ser Leu Leu Ala Ala Gly Asn Ala Val Val Leu Asn Val His Pro 195 200 205 Ser Ser Lys Ala Ser Cys Ala Phe Val Val Asn Leu Ile Asn Gln Ala 210 215 220 Ile Gln Asp Ala Gly Gly Pro Lys Asn Leu Val Ser Met Val Lys Asp 225 230 235 240 Pro Thr Leu Glu Thr Leu Asn Arg Ile Ile Glu Ser Pro Lys Val Lys 245 250 255 Leu Leu Val Gly Thr Gly Gly Pro Gly Met Val Lys Thr Leu Leu Lys 260 265 270 Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile 275 280 285 Val Asp Glu Thr Ala Asp Leu Lys Gln Ala Ala Lys Ser Ile Ile Glu 290 295 300 Gly Ala Ser Phe Asp Asn Asn Leu Leu Cys Ile Ala Glu Lys Glu Leu 305 310 315 320 Phe Val Ile Asp Ser Val Ala Asp Asp Leu Ile Phe Gln Met Leu Asn 325 330 335 Glu Gly Ala Tyr Met Leu Asp Gln Gln Gln Leu Ser Lys Leu Met Ser 340 345 350 Phe Ala Leu Glu Glu Asn Val His Gln Glu Ala Gly Gly Cys Ser Leu 355 360 365 Asp Asn Lys Arg Glu Tyr His Val Ser Lys Asp Trp Val Gly Lys Asp 370 375 380 Ala Ala Ser Phe Leu Arg Gln Ile Gly Val Ala Cys Glu Glu Asn Ile 385 390 395 400 Lys Leu Leu Ile Cys Glu Val Asp Phe Asp His Pro Phe Val Gln Leu 405 410 415 Glu Gln Met Met Pro Val Phe Pro Ile Val Arg Val Gly Asp Leu Asp 420 425 430 Glu Ala Ile Glu Met Ala Leu Leu Ala Glu His Gly Asn Arg His Thr 435 440 445 Ala Ile Met His Ser Lys Asn Val Asp His Leu Thr Lys Phe Ala Arg 450 455 460 Ala Ile Glu Thr Thr Ile Phe Val Lys Asn Ala Ser Ser Leu Ala Gly 465 470 475 480 Val Gly Phe Gly Gly Glu Gly His Thr Thr Met Thr Ile Ala Gly Pro 485 490 495 Thr Gly Glu Gly Ile Thr Ser Ala Lys Thr Phe Thr Arg Gln Arg Arg 500 505 510 Cys Val Leu Ala Glu Gly Gly Phe Arg Ile Ile Gly 515 520 <210> 314 <211> 471 <212> PRT <213> Artificial Sequence <220> <223> Dorea sp. D27 <400> 314 Met Glu Ile Ser Thr Ser Gln Ile Ser Arg Tyr Ile Leu Asp Leu Gln 1 5 10 15 Asn Glu Leu Lys Gly Asp Ser Pro Ser Pro Ala His Met Ser Ala Gly 20 25 30 Glu His Gly Ile Phe Gln Asp Ala Glu Cys Ala Ile Met Ala Ala Ser 35 40 45 Gln Ala Gln Lys Arg Leu Met Glu Tyr Ser Leu Lys Glu Arg Glu Thr 50 55 60 Phe Ile Glu Ala Met Arg Ala Ala Ala Arg Glu Asn Ala Arg Lys Leu 65 70 75 80 Ala Glu Thr Ala His Asp Glu Thr Gly Tyr Gly His Val Glu Asp Lys 85 90 95 Val Ala Lys Asn Val Leu Ala Ala Asp Lys Thr Pro Gly Ile Glu Asp 100 105 110 Leu Asn Thr Met Ala Val Ser Gly Asp Ala Gly Leu Met Leu Thr Glu 115 120 125 Met Ala Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro 130 135 140 Thr Ala Thr Val Ile Asn Asn Gly Ile Gly Met Ile Ala Gly Gly Asn 145 150 155 160 Ala Val Val Phe Asn Pro His Pro Gly Ala Lys Lys Ala Ser Leu Leu 165 170 175 Thr Ile Lys Leu Met Asn Glu Ala Ile Val Gly Ala Gly Gly Pro Asp 180 185 190 Asn Leu Leu Cys Ala Pro Glu Glu Pro Thr Leu Asp Thr Ser Ser Val 195 200 205 Ile Met Ser His Pro Leu Val Lys Leu Leu Val Val Thr Gly Gly Glu 210 215 220 Ala Val Val Arg Thr Ala Met Lys Thr Gly Lys Lys Cys Ile Ala Ala 225 230 235 240 Gly Pro Gly Asn Pro Pro Val Val Val Asp Gly Thr Ala Asp Ile Lys 245 250 255 Arg Ala Ala Ala Asp Ile Val Lys Gly Ala His Tyr Glu Asn Cys Ile 260 265 270 Leu Cys Ile Ala Glu Lys Glu Ile Leu Val Glu Ser Cys Val Ala Asp 275 280 285 Glu Leu Ile Arg Glu Met Val Lys Glu Gly Ala Tyr Leu Ala Asp Glu 290 295 300 Lys Glu Leu Ser Ala Ile Val Gly Lys Val Met Ile Thr Ala Lys Asp 305 310 315 320 Gly Ser Tyr Ala Pro Asn Lys Lys Tyr Val Gly Arg Asp Ala Thr Tyr 325 330 335 Ile Leu Lys Glu Ala Gly Ile Cys Val Asp Arg Glu Ala Lys Ile Ile 340 345 350 Ile Ala Glu Val Pro Phe Gly His Pro Leu Val Met Thr Glu Met Leu 355 360 365 Met Pro Val Ile Pro Val Thr Arg Val Ala Thr Val Glu Glu Ala Ile 370 375 380 Glu Lys Ala Val Ile Ala Glu Asn Gly Cys His His Thr Ala Met Met 385 390 395 400 His Ser Glu Asn Val Ser Asn Leu Thr Lys Met Ala Arg Ala Ala Asp 405 410 415 Thr Thr Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Gly Leu Gly Ile 420 425 430 Asp Gly Glu Gly Tyr Thr Thr Leu Thr Ile Ala Thr Pro Thr Gly Glu 435 440 445 Gly Leu Thr Ser Ala Arg Asn Phe Thr Arg Ser Arg Arg Cys Thr Leu 450 455 460 His Gly Ser Phe Arg Ile Val 465 470 <210> 315 <211> 448 <212> PRT <213> Artificial Sequence <220> <223> Enterococcus phoeniculicola <400> 315 Ile Met Asn Thr Leu Ser Asp Lys Ile Leu Arg Gly Arg Gln Ala Met 1 5 10 15 Gln Ser Ile Ser Asn Tyr Thr Gln Glu Gln Val Asp Glu Met Leu Ser 20 25 30 Val Ile Ser Lys Thr Ile Phe Asp His Ala Glu Glu Leu Ala Lys Glu 35 40 45 Ala Val Glu Glu Thr Gly Leu Gly Asn Tyr Glu His Lys Ile Gly Lys 50 55 60 Asn Gln Asn Met Ala Ile Asn Ile Phe Ser His Leu Lys Gly Lys Lys 65 70 75 80 Ser Val Gly Ile Ile Gln Thr Leu Lys Glu Glu Gly Val Val Glu Ile 85 90 95 Ala His Pro Val Gly Val Ile Gly Ser Val Thr Pro Thr Thr Asn Pro 100 105 110 Thr Ile Thr Pro Leu Gly Asn Gly Leu Met Ala Leu Lys Gly Lys Asn 115 120 125 Ala Met Ile Val Ser Pro His Pro Arg Ala Lys Lys Thr Thr Lys His 130 135 140 Thr Ile Asp Leu Met Arg Ser Ala Leu Glu Ser Ile His Ala Pro Lys 145 150 155 160 Asp Leu Leu Gln Val Ile Glu Glu Pro Ser Leu Glu Leu Ser Gln Gln 165 170 175 Leu Met Arg Glu Ser Asp Val Ile Val Ala Thr Gly Gly Pro Gly Leu 180 185 190 Val Arg Ala Ala Tyr Ser Ser Gly Lys Pro Ala Phe Gly Val Gly Pro 195 200 205 Gly Asn Val Gln Ala Ile Leu Asp Asp Asp Phe Asp Ile Asn Leu Ala 210 215 220 Ala Glu Leu Thr Val Ile Gly Arg Ser Phe Asp Asn Gly Ile Val Cys 225 230 235 240 Ala Cys Gln Gln Ser Leu Leu Tyr Pro Glu Lys Lys Glu Glu Glu Leu 245 250 255 Phe Gln Ala Leu Glu Asn Asn Lys Ala Tyr Ile Ile Lys Glu Glu Ile 260 265 270 Asp Val Gln Lys Met Arg Glu Leu Leu Phe Pro Gly Gly Lys Ser Asn 275 280 285 Pro Asp Leu Val Gly Gln Thr Ala Thr Phe Ile Ala Glu Lys Ala Gly 290 295 300 Ile Lys Val Pro Glu Asp Thr Ile Ile Leu Ala Val Lys Val Thr Thr 305 310 315 320 Ser Gly Gln Glu Glu Leu Leu Val Lys Glu Lys Met Asn Pro Val Leu 325 330 335 Val Val Lys Gly Cys Glu Ser Phe Glu Glu Ala Leu Leu Asp Ala Lys 340 345 350 Asn Asn Leu Trp Val Glu Gly Ala Gly His Ser Thr Gly Ile Phe Ser 355 360 365 Asn Asn Glu Gln His Ile Leu Ser Ala Gly Glu Thr Leu Pro Val Ser 370 375 380 Arg Val Val Val Asn Gln Pro Thr Ile Asp Ala Gly Gly Ser Pro Thr 385 390 395 400 Asn Gly Leu Asn Pro Thr Val Ser Leu Gly Cys Gly Ser Trp Gly Asn 405 410 415 Asn Ser Ile Ser Glu Asn Leu Ser Tyr His His Leu Ile Asn Ile Ser 420 425 430 Arg Ile Ala Tyr Pro Ile Ser Pro Lys His Thr Glu Thr Pro Trp Asn 435 440 445 <210> 316 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Blautia schinkii <400> 316 Met Pro Ile Ser Asp Ser Met Val Gln Glu Ile Val Gln Glu Val Met 1 5 10 15 Ala Lys Met Gln Ile Ala Asp Ala Pro Ala Gly Lys His Gly Val Phe 20 25 30 Lys Asp Met Asn Glu Ala Ile Glu Ala Ala Lys Lys Thr Glu Asn Ile 35 40 45 Val Lys Arg Met Ser Met Asp Gln Arg Glu Lys Ile Ile Thr Cys Ile 50 55 60 Arg Lys Ser Ile Lys Lys Asn Ala Glu Ile Met Ala Arg Met Gly Val 65 70 75 80 Asp Glu Thr Gly Met Gly Asn Val Gly Asp Lys Ile Leu Lys His His 85 90 95 Leu Val Ala Asp Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Val Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Ile Leu 130 135 140 Cys Asn Thr Met Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Tyr Ala Val Asn Leu Leu 165 170 175 Asn Glu Ala Ser Leu Glu Ala Gly Gly Pro Asp Asn Ile Ala Val Thr 180 185 190 Val Glu Gln Pro Thr Leu Glu Thr Ser Asn Ile Met Met Lys His Lys 195 200 205 Asp Ile Pro Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Val Arg Lys Ala Ala Gln Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Ser Pro Ile Val Asp Glu Leu Met His Tyr 275 280 285 Leu Val Ser Glu Asn Asp Cys Tyr Leu Ala Ser Lys Glu Glu Gln Asp 290 295 300 Lys Leu Thr Glu Val Val Leu Ala Gly Gly Arg Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Arg Thr Leu Leu Ser Met Ile Gly Val Asn Val 325 330 335 Pro Ala Asn Ile Arg Cys Ile Val Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Ala Thr Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Lys Asp Phe Asp Asp Ala Val Glu Gln Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Ile Asp Asn Ile Thr 385 390 395 400 Lys Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Ala Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Tyr Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Ser Asp Ser Leu Cys Ile Arg 450 455 460 <210> 317 <211> 472 <212> PRT <213> Artificial Sequence <220> <223> Clostridium intestinale <400> 317 Met Ser Ile Asp Ala Thr Leu Val Glu Lys Leu Val Arg Gln Ala Ile 1 5 10 15 Glu Glu Ala Lys Ser Lys Asn Leu Ile Ser Phe Asn Lys Val Glu Thr 20 25 30 Leu Asn Asn Tyr Gly Ile Phe Asn Thr Met Asp Glu Ala Ile Glu Ala 35 40 45 Ser Asp Val Ala Gln Lys Glu Leu Leu Asn Thr Ser Met Ala Asn Arg 50 55 60 Gln Lys Tyr Ile Asn Ile Ile Lys Ser Thr Val Leu Lys Arg Glu Asn 65 70 75 80 Leu Glu Leu Ile Ser Arg Met Ala Val Glu Glu Thr Glu Ile Gly Arg 85 90 95 Tyr Glu His Lys Leu Ile Lys Asn Arg Val Ala Ala Glu Lys Thr Pro 100 105 110 Gly Thr Glu Asp Leu Val Thr Glu Ala Ile Thr Gly Asp Asn Gly Ile 115 120 125 Thr Leu Ile Glu Tyr Cys Pro Phe Gly Val Ile Gly Ser Ile Thr Pro 130 135 140 Thr Thr Asn Pro Thr Glu Thr Ile Ile Cys Asn Ser Met Ser Met Ile 145 150 155 160 Ala Gly Gly Asn Thr Val Val Phe Ser Pro His Pro Arg Ala Lys Asn 165 170 175 Val Ser Ile Lys Leu Ile Thr Met Leu Asn Lys Ala Leu Glu Glu Ala 180 185 190 Gly Ala Pro Lys Asn Leu Ile Val Thr Val Lys Glu Pro Ser Ile Glu 195 200 205 Asn Thr Asn Ala Met Met Asp His Pro Lys Val Arg Val Leu Val Ala 210 215 220 Thr Gly Gly Pro Ala Ile Val Lys Lys Val Met Ser Thr Gly Lys Lys 225 230 235 240 Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Val Val Asp Glu Thr 245 250 255 Ala Asn Val Glu Lys Ala Ala Ile Asp Ile Val Asn Gly Cys Ser Phe 260 265 270 Asp Asn Asn Val Pro Cys Val Ala Glu Lys Glu Val Phe Ala Val Asp 275 280 285 Gln Ile Cys Asp Tyr Leu Ile His Tyr Met Lys Leu Asn Gly Ala Tyr 290 295 300 Glu Ile Lys Asp Arg Asn Thr Ile Gln Lys Leu Leu Glu Leu Val Thr 305 310 315 320 Asn Glu Asn Gly Gly Pro Lys Val Ser Phe Val Gly Lys Asn Ala Ser 325 330 335 Tyr Ile Leu Ser Lys Leu Gly Ile Asn Val Asp Asp Asn Ile Lys Ile 340 345 350 Ile Ile Met Glu Val Asp Lys Asp His His Phe Val Lys Glu Glu Met 355 360 365 Met Met Pro Ile Leu Pro Ile Val Arg Thr Arg Asp Val Asp Glu Ala 370 375 380 Ile Glu Tyr Ala Tyr Val Ala Glu Asn Gly Asn Arg His Thr Ala Ile 385 390 395 400 Met His Ser Lys Asn Val Asp Lys Leu Thr Lys Met Ala Arg Leu Leu 405 410 415 Glu Thr Thr Ile Phe Val Lys Asn Ala Pro Ser Phe Ala Gly Leu Gly 420 425 430 Val Gly Gly Glu Gly Asn Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly 435 440 445 Glu Gly Leu Thr Thr Ala Lys Ser Phe Cys Arg Lys Arg Arg Cys Ile 450 455 460 Met Val Asp Ala Phe Asn Ile Arg 465 470 <210> 318 <211> 483 <212> PRT <213> Artificial Sequence <220> <223> Massilioclostridium coli <400> 318 Met Val Phe Ser Gln Asn Gln Ile Asp Ser Ile Val Gln Ser Val Val 1 5 10 15 Ala Gln Met Gln Gly Thr Thr Pro Thr Ser Ala Pro Ala Tyr Asp Ser 20 25 30 Thr Gln Tyr Asn Gly Arg Gln Tyr Leu Gly Val Tyr Ala Thr Met Glu 35 40 45 Glu Gly Ile Asp Ala Ala Ala Asp Ser Tyr Lys Val Ile Arg Asn Met 50 55 60 Ser Val Glu Gln Arg Glu Lys Ile Ile Thr Glu Ile Arg Lys Leu Thr 65 70 75 80 Arg Ala Glu Ala Glu Ile Met Ala Lys Leu Gly Val Glu Glu Thr Lys 85 90 95 Met Gly Arg Val Glu His Lys Thr Leu Lys His Ile Leu Val Ala Asp 100 105 110 Lys Thr Pro Gly Thr Glu Asp Ile Gln Thr Glu Ala Gln Ser Gly Asp 115 120 125 Gly Gly Leu Thr Leu Val Glu Met Ala Pro Phe Gly Ile Ile Gly Ala 130 135 140 Ile Thr Pro Ser Thr Asn Pro Ser Glu Thr Val Ile Cys Asn Ser Ile 145 150 155 160 Ala Met Ile Ala Ala Gly Asn Ala Val Val Phe Asn Pro His Pro Gly 165 170 175 Ala Ile Lys Val Ser Asn Tyr Ala Val Asp Leu Val Asn Arg Ala Ser 180 185 190 Leu Ala Ala Gly Gly Pro Ala Ser Leu Val Cys Ser Met Val Lys Pro 195 200 205 Thr Met Gln Thr Ala Asp Val Met Tyr Lys Asp Pro Arg Val Arg Met 210 215 220 Leu Val Cys Thr Gly Gly Pro Gly Val Val Lys Ser Val Leu Ser Ser 225 230 235 240 Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val 245 250 255 Asp Asp Thr Ala Asp Ile Lys Lys Ala Ala Lys Asp Ile Ile Asp Gly 260 265 270 Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu Val Phe 275 280 285 Ala Phe Ser Asn Ile Ala Asp Glu Leu Met Tyr Asn Met Gln Gln Asn 290 295 300 Gly Ala Tyr Phe Ile Thr Ala Ala Gln Ala Asp Glu Leu Ala Lys Ile 305 310 315 320 Val Leu Val Glu Lys Lys Asn Glu Lys Thr Gly Lys Ile Thr Tyr Ser 325 330 335 Val Ser Arg Asp Trp Val Gly Arg Asp Ala Lys Lys Phe Ala Ala Ala 340 345 350 Leu Gly Ile Glu Val Asp Asp Ser Val Arg Cys Leu Ile Cys Glu Val 355 360 365 Glu Glu Asp His Leu Phe Val Gln Thr Glu Leu Met Met Pro Ile Leu 370 375 380 Ala Val Val Arg Val Lys Asp Ile Asp Glu Ala Ile Glu Lys Ala Val 385 390 395 400 Arg Ala Glu His Gly Asn Arg His Ser Ala His Met His Ser Lys Asn 405 410 415 Ile Glu Asn Leu Ser Lys Phe Ala Lys Ala Ile Glu Thr Thr Ile Phe 420 425 430 Val Lys Asn Ala Pro Ser Tyr Ala Gly Ile Gly Phe Gly Ala Glu Gly 435 440 445 His Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser 450 455 460 Ala Arg Ser Phe Thr Arg Lys Arg Arg Cys Val Met Lys Asp Met Phe 465 470 475 480 His Ile Ile <210> 319 <211> 466 <212> PRT <213> Artificial Sequence <220> <223> Cloacibacillus porcorum <400> 319 Met Asn Ile Asp Ala Ala Leu Ile Glu Gly Ile Val Lys Gly Val Met 1 5 10 15 Arg Lys Ile Asp Glu Ser Glu Asn Asn Ser Ala Gly Ser Cys Gly Ile 20 25 30 Phe Ala Asp Met Asn Asp Ala Ile Glu Ala Ala Ala Ala Ala Gln Arg 35 40 45 Arg Tyr Leu Asp Cys Ser Met Ala Asp Arg Ala Arg Phe Val Glu Ala 50 55 60 Ile Arg Gly Thr Val Leu Asn Glu Glu Asn Leu Lys Phe Met Ser Leu 65 70 75 80 Ser Thr Ile Glu Glu Thr Gly Met Gly Asn Tyr Glu His Lys Leu Val 85 90 95 Lys Asn Arg Leu Ala Ala Thr Lys Thr Pro Gly Ile Glu Asp Leu Thr 100 105 110 Thr Asp Ala Ile Thr Gly Asp Asp Gly Leu Thr Ile Val Glu Tyr Ser 115 120 125 Pro Phe Gly Val Ile Gly Ala Ile Thr Pro Thr Thr Asn Pro Thr Glu 130 135 140 Thr Ile Ile Cys Asn Ser Ile Gly Met Leu Ala Ala Gly Asn Thr Val 145 150 155 160 Val Phe Ser Pro His Pro Arg Ala Lys Lys Val Ser Leu Trp Leu Val 165 170 175 Ser Glu Leu Asn Arg Ala Leu Ala Ala Ala Gly Ala Pro Ala Asn Leu 180 185 190 Ile Val Thr Val Ser Glu Pro Ser Ile Glu Asn Thr Asn Leu Met Met 195 200 205 Ala His Pro Lys Val Arg Met Leu Val Ala Thr Gly Gly Pro Ala Ile 210 215 220 Val Lys Thr Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Ala Val Val Asp Glu Ser Ala Asn Ile Glu Lys Ala 245 250 255 Ala Lys Asp Ile Val Asp Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys 260 265 270 Ile Ala Glu Lys Glu Val Ile Val Val Asp Ser Ala Ala Asp Tyr Leu 275 280 285 Ile Phe Asn Met Lys Lys Asn Gly Ala Phe Glu Val Lys Asp Pro Ala 290 295 300 Val Ile Glu Arg Leu Val Gly Leu Val Thr Lys Glu Gly Lys Ser Pro 305 310 315 320 Lys Thr Glu Phe Val Gly Lys Ser Ala Lys Tyr Ile Leu Glu Lys Ala 325 330 335 Gly Val Glu Ala Pro Glu Asp Thr Arg Val Ile Ile Met Glu Ala Arg 340 345 350 Glu Glu His Pro Phe Val Gln Val Glu Leu Met Met Pro Ile Leu Pro 355 360 365 Ile Val Arg Ala Asp Asn Val Asn Glu Ala Ile Glu Met Ala Val Arg 370 375 380 Val Glu His Gly Asn Arg His Thr Ala Met Met His Ser Arg Asn Val 385 390 395 400 Asp Ser Leu Thr Lys Met Ala Lys Leu Ile Gln Thr Thr Ile Phe Val 405 410 415 Lys Asn Gly Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Met Gly His 420 425 430 Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala 435 440 445 Lys Thr Phe Ala Arg Arg Arg Arg Cys Val Leu Val Gly Gly Met Asp 450 455 460 Ile Arg 465 <210> 320 <211> 500 <212> PRT <213> Artificial Sequence <220> <223> Sporosarcina globispora <400> 320 Met Gln Glu Met Arg Asp Ala Val Lys Arg Ala Lys Glu Ala Gln Leu 1 5 10 15 Glu Tyr Met Ala Phe Thr Gln Glu Gln Val Asp Glu Ile Val Lys Asn 20 25 30 Ala Ala Asp Ala Ala Tyr Ala Lys Ser Leu Tyr Leu Ala Gln Met Ala 35 40 45 Val Glu Glu Thr Gly Met Gly Ile Val Glu His Lys Lys Ile Lys Asn 50 55 60 Glu Val Gly Ser Lys Ala Val Tyr Glu Ser Ile Lys Asp Glu Lys Thr 65 70 75 80 Val Gly Ile Ile Arg Glu Asp Arg Val Asn Lys Val Thr Glu Ile Ala 85 90 95 Tyr Pro Tyr Gly Val Val Ala Gly Ile Ile Pro Thr Thr Asn Pro Thr 100 105 110 Ser Thr Ala Ile Phe Lys Ala Leu Ile Ser Leu Lys Thr Arg Asn Ala 115 120 125 Ile Val Val Ser Pro His Pro Arg Ala Val Lys Cys Thr Val Glu Ala 130 135 140 Leu Lys Ile Val Asn Glu Ala Ala Ile Gln Ala Gly Ala Pro Glu Gly 145 150 155 160 Leu Ile Gly Trp Ile Ser Lys Pro Ser Met Gly Ala Thr Asn Glu Leu 165 170 175 Met Lys His Arg Asp Ile Ser Leu Ile Leu Ala Thr Gly Gly Gly Gly 180 185 190 Leu Val Arg Ala Ala Tyr Ser Ser Gly Lys Pro Ala Tyr Gly Val Gly 195 200 205 Pro Gly Asn Val Pro Cys Tyr Ile Glu Lys Thr Ala Lys Val Ala Gln 210 215 220 Ser Val Lys Met Ile Ile Asp Ser Lys Ser Phe Asp Asn Gly Thr Ile 225 230 235 240 Cys Ala Thr Glu Gln Ser Ile Val Ala Asp Arg Asn Ile Lys Glu Met 245 250 255 Ala Met Arg Glu Leu Lys Asn Asn Gly Ala Tyr Ile Leu Asn Ser Asp 260 265 270 Glu Lys Ala Ala Leu Glu Lys Ile Ile Ser Pro Ser Pro Gly Lys Leu 275 280 285 Asn Pro Asp Ile Val Gly Gln Ser Ala Val Lys Ile Ala Ala Met Ala 290 295 300 Gly Ile Gln Val Pro Asn Asp Thr Arg Val Leu Ile Ala Glu Glu Thr 305 310 315 320 Lys Val Gly Lys Asp Ile Pro Phe Ser Ile Glu Lys Leu Ser Pro Ile 325 330 335 Phe Ala Phe Tyr Thr Ala Glu Ser Tyr Gln Asp Ala Lys Glu Ile Cys 340 345 350 Leu Gln Leu Leu Asn Leu Gly Gly Arg Gly His Ser Leu Ser Leu His 355 360 365 Thr Asn Asp Asp Ala Val Ala Lys Asp Phe Ala Leu Glu Met Pro Val 370 375 380 Ser Arg Ile Leu Val Asn Thr Leu Ser Ser Ile Gly Ala Val Gly Ala 385 390 395 400 Thr Thr Gly Leu Met Pro Ser Leu Thr Leu Gly Cys Gly Ser Phe Gly 405 410 415 Gly Asn Ile Thr Ser Asp Asn Val Thr Ala Arg His Leu Ile Asn Thr 420 425 430 Lys Arg Met Ala Tyr Gly Thr Lys Glu Val Thr Val Pro Lys Pro Ala 435 440 445 Ala Ser Ser Ser Ile Ala Glu Lys Glu Gln Ala Gly Ser Gln Asp Val 450 455 460 Asp His Ile Val Ser Gln Val Leu Gln Gln Val Ser Pro Gly Gly Glu 465 470 475 480 Val Asp Ala Lys Met Ile Ala Asp Met Val Asn Gln Val Met Lys Lys 485 490 495 Tyr Gln Thr Asn 500 <210> 321 <211> 528 <212> PRT <213> Artificial Sequence <220> <223> Rhodobacter aestuarii <400> 321 Met Lys Asp Ile Asp Ile Glu Asn Ala Val Ala Arg Val Leu Ser Gly 1 5 10 15 Tyr Thr Gly Pro Ala Glu Thr Pro Ala Pro Ala Pro Thr Ser Lys Pro 20 25 30 Gly Thr Thr Gly Cys Val Trp Glu Pro Val Lys Ala Val Asp Pro Val 35 40 45 Asp Asp Ile Ile Gly Gly Met Leu Thr Arg Ala Leu Gly Glu Arg Asn 50 55 60 Cys Ser Asn Cys Lys Ala Gly Asp Cys Gln Gly Lys Ala Gly Cys Leu 65 70 75 80 Ser Ile Ser Asp Ala Glu Ala Leu Glu Leu Gly Asp Gly Val Phe Ala 85 90 95 Thr Met Asp Glu Ala Val Asn Ala Ala Ala Glu Ala Gln Arg Lys Tyr 100 105 110 Leu Phe Cys Thr Met Gly Asp Arg Lys Arg Phe Val Glu Gly Ile Arg 115 120 125 Ala Ile Phe Thr Asp Glu Ala Val Leu Glu Arg Ile Ser Arg Leu Thr 130 135 140 Val Glu Gln Thr Gly Met Gly Asn Leu Ala His Lys Ile Ile Lys Asn 145 150 155 160 Arg Leu Ala Ala Glu Lys Thr Pro Gly Val Glu Asp Leu Thr Thr Glu 165 170 175 Ala Gln Ser Gly Asp Asp Gly Leu Thr Leu Val Glu Leu Ser Pro Phe 180 185 190 Gly Val Ile Gly Ala Ile Thr Pro Thr Thr Asn Pro Thr Glu Thr Val 195 200 205 Ile Cys Asn Ser Ile Gly Met Leu Ala Ala Gly Asn Ala Ala Val Phe 210 215 220 Ser Pro His Pro Arg Ala Lys Gly Val Ser Leu Leu Ala Ile Lys Leu 225 230 235 240 Ile Asn Arg Lys Leu Ala Ala Leu Gly Ala Pro Ala Asn Leu Val Val 245 250 255 Thr Val Gln Ala Pro Ser Ile Asp Asn Thr Asn Ala Met Met Ala His 260 265 270 Pro Gln Val Arg Met Leu Val Ala Thr Gly Gly Pro Gly Ile Val Arg 275 280 285 Thr Val Met Ser Thr Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn 290 295 300 Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Pro Lys Ala Ala Gln 305 310 315 320 Asp Ile Val Asn Gly Ala Ser Phe Asp Asn Asn Met Pro Cys Ile Ala 325 330 335 Glu Lys Glu Val Ile Val Val Asp Gln Val Ala Asp Phe Leu Ile Ser 340 345 350 Glu Met Gln Arg Asn Gly Ala Trp Leu Ala Ser Asp Pro Ser Val Val 355 360 365 Glu Arg Leu Ala Gln Leu Val Leu Thr Glu Lys Gly Gly Pro Gln Thr 370 375 380 Gly Cys Val Gly Lys Ser Ala Ala Trp Leu Leu Gly Gln Ile Gly Ile 385 390 395 400 Gln Val Gly Pro Asp Val Arg Leu Ile Ile Leu Glu Thr Thr Lys Asp 405 410 415 His Pro Phe Val Gln Glu Glu Leu Met Met Pro Ile Leu Pro Val Val 420 425 430 Arg Val Pro Asp Val Asp Thr Ala Ile Asp Leu Ala Val Asp Leu Glu 435 440 445 His Gly Asn Arg His Thr Ala Met Met His Ser Thr Asn Val Arg Lys 450 455 460 Leu Thr Lys Met Ala Lys Leu Ile Gln Thr Thr Ile Phe Val Lys Asn 465 470 475 480 Gly Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Tyr Thr Thr 485 490 495 Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Pro Arg Ser 500 505 510 Phe Ala Arg Arg Arg Lys Cys Val Met Val Glu Ala Leu Asn Val Arg 515 520 525 <210> 322 <211> 468 <212> PRT <213> Artificial Sequence <220> <223> Clostridium grantii <400> 322 Met Ala Ile Asn Glu Ser Gln Ile Glu Glu Ile Val Lys Gln Val Leu 1 5 10 15 Leu Asn Val Ser Gly Thr Thr Lys Val Lys Asn Glu Asn Lys Ala Ile 20 25 30 Gly Ile Phe Glu Asp Ile Glu Glu Ala Ile Asp Ala Ala Lys Ile Ala 35 40 45 Gln Lys Lys Ile Lys Lys Met Ser Met Glu Gln Arg Glu Lys Ile Ile 50 55 60 Thr Arg Ile Arg Glu Lys Thr Arg Glu Asn Ala Lys Ile Met Ser Glu 65 70 75 80 Met Ala Val Glu Glu Thr Gly Met Gly Arg Val Asp His Lys Ile Leu 85 90 95 Lys His Leu Leu Val Ala Asp Lys Thr Pro Gly Thr Glu Asp Ile Thr 100 105 110 Thr Thr Ala Trp Ser Gly Asp Asn Gly Leu Thr Leu Ile Glu Met Gly 115 120 125 Ala Phe Gly Val Ile Gly Gly Ile Thr Pro Ser Thr Asn Pro Ser Cys 130 135 140 Thr Val Leu Cys Asn Ser Ile Gly Met Ile Ala Gly Gly Asn Thr Val 145 150 155 160 Val Phe Asn Pro His Pro Gly Ala Val Lys Val Ser Asn Tyr Ala Val 165 170 175 Thr Leu Val Asn Glu Ala Ser Val Glu Cys Gly Gly Pro Glu Asn Ile 180 185 190 Ala Cys Ser Val Thr Lys Pro Thr Leu Asp Ser Gly Lys Ile Leu Met 195 200 205 Thr His Lys Asp Ile Ala Leu Leu Ala Val Thr Gly Gly Pro Gly Val 210 215 220 Val Thr Ala Ala Leu Lys Ser Gly Lys Arg Ala Leu Gly Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Leu Gln Ser Ala 245 250 255 Ala Lys His Ile Val Asp Gly Ala Thr Phe Asp Asn Asn Leu Pro Cys 260 265 270 Ile Ala Glu Lys Glu Val Val Ala Val Glu Ser Ile Val Glu Glu Leu 275 280 285 Lys Tyr His Met Ile Asn Asn Gly Cys Tyr Glu Leu Lys Gly Ser Asp 290 295 300 Ile Asp Lys Leu Val Asn Thr Val Leu Ile Asn Asn Asn Gly Ile Ile 305 310 315 320 Gly Leu Asn Arg Asp Cys Val Gly Lys Asp Ala Lys Val Ile Leu Lys 325 330 335 Lys Leu Gly Ile Glu Val Asp Asp Ser Ile Arg Cys Ile Ile Phe Asp 340 345 350 Ala Asp Glu Asp His Ile Leu Val Leu Glu Glu Leu Met Met Pro Ile 355 360 365 Leu Gly Ile Val Lys Val Glu Asn Val Asp Glu Ala Ile Lys Leu Ala 370 375 380 Val Arg Tyr Glu His Gly Asn Arg His Ser Ala His Met His Ser Lys 385 390 395 400 Asn Ile Asp Asn Leu Thr Lys Tyr Gly Arg Glu Ile Asp Thr Ala Ile 405 410 415 Phe Val Lys Asn Ala Pro Ser Tyr Ser Ala Leu Gly Phe Asn Gly Glu 420 425 430 Gly Tyr Cys Thr Phe Thr Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr 435 440 445 Ser Gly Lys Thr Phe Thr Lys Ser Arg Arg Cys Val Leu Ser Asp Gly 450 455 460 Leu Ser Ile Arg 465 <210> 323 <211> 449 <212> PRT <213> Artificial Sequence <220> <223> Collinsella sp. GD7 <400> 323 Val Ala Glu Phe Ile Glu Arg Ala Arg Val Ala Gln Ala Glu Phe Glu 1 5 10 15 Thr Tyr Ser Gln Glu Glu Val Asp Arg Ala Val Arg Ala Ile Gly Lys 20 25 30 Ala Val Phe Asp Ala Ala Glu Pro Leu Ala Lys Leu Ala Val Glu Glu 35 40 45 Thr Arg Met Gly Arg Tyr Glu Asp Lys Ile Ala Lys Asn Ser Gly Lys 50 55 60 Thr Lys Ile Thr Trp Asp Arg Leu Lys Gly Val Lys Ser Arg Gly Ile 65 70 75 80 Ile Ala Arg His Glu Asp Glu Gly Ile Val Glu Val Ala Lys Pro Met 85 90 95 Gly Val Ile Gly Cys Ile Pro Pro Thr Thr Asn Pro Thr Met Thr Pro 100 105 110 Ala His Asn Ala Met Cys Ala Leu Lys Gly Gly Asn Ala Leu Leu Ile 115 120 125 Ser Pro His Pro Arg Ala Lys Lys Thr Gly Val Glu Thr Val Arg Ile 130 135 140 Met Arg Glu Ala Leu Glu Ala Met Gly Ala Pro Ala Asp Leu Ile Gln 145 150 155 160 Ile Ile Pro Asp Pro Thr Leu Glu Ile Ser Ser Leu Val Met Ser Met 165 170 175 Cys Asp Cys Thr Ile Ala Thr Gly Gly Pro Gly Met Val Lys Ala Val 180 185 190 Tyr Ser Ser Gly Lys Pro Ala Phe Gly Val Gly Ala Gly Asn Val Gln 195 200 205 Thr Ile Val Asp Thr Asp Ala Asp Leu Glu Leu Ser Ala Gln Gln Ile 210 215 220 Val Arg Ser Arg Thr Tyr Asp Asn Gly Val Leu Cys Thr Cys Glu Gln 225 230 235 240 Cys Ile His Val Gln Glu Asp Ile Tyr Gly Glu Met Val Arg Leu Phe 245 250 255 Gln Gln Glu Gly Ala Phe Tyr Ile Ser Glu Gln Ala Asp Val Asp Ala 260 265 270 Leu Arg Ala Ala Leu Phe Pro Asn Gly Ala Ile Asn Lys Asp Ala Val 275 280 285 Gly Ala Ser Pro Gln Phe Ile Gly Ser Leu Ala Gly Leu Asp Val Pro 290 295 300 Glu Asp Ala Lys Leu Leu Met Val Lys Val Asp Ala Tyr Gly Ala Asp 305 310 315 320 Glu Leu Leu Cys Lys Glu Lys Leu Cys Pro Val Met Cys Val Ala Ser 325 330 335 Tyr Gly Thr Trp Glu Glu Gly Val Ala Asn Ala Lys Thr Asn Leu Leu 340 345 350 His Glu Gly Ala Gly His Ser Ala Ile Val Arg Ser His Thr Ala Glu 355 360 365 His Val Asp Tyr Ala Gly Glu Gln Leu Pro Val Ser Arg Ile Gly Val 370 375 380 Asn Met Ile Gly Ser Ser Gly Leu Gly Gly Ala Phe Asp Asn Gly Leu 385 390 395 400 Asn Pro Thr Ala Thr Leu Gly Cys Gly Ser Trp Gly Asn Asn Ser Ile 405 410 415 Ser Glu Asn Leu Trp Trp His His Leu Val Asn Ile Ala Arg Ile Ala 420 425 430 Val Ala Leu Pro Asp Val Gln Val Pro Ser Asp Glu Glu Val Trp Gly 435 440 445 Glu <210> 324 <211> 471 <212> PRT <213> Artificial Sequence <220> <223> Clostridium estertheticum <400> 324 Met Glu Ile Lys Asn Asp Glu Ile Ser Ala Met Val Glu Lys Val Leu 1 5 10 15 Gln Glu Met Asn Arg Arg Asp Leu Asn Val Ser Glu Ser Asp Gly Val 20 25 30 Phe Asp Asp Met Asp Glu Ala Ile Glu Ala Ala Ser Ile Ala Gln Lys 35 40 45 Glu Leu Ile Cys Met Ser Ile Ser Gln Arg Glu Glu Leu Ile Ser Ala 50 55 60 Met Arg Lys Ala Ile Leu Asp Asn Ala Thr Lys Ile Ala Asp Ile Cys 65 70 75 80 Val Glu Asp Thr Gly Met Gly Arg Lys Asp His Lys Tyr Leu Lys Leu 85 90 95 Lys Leu Val Ala Asn Lys Thr Pro Gly Thr Glu Val Leu Lys Thr Met 100 105 110 Ala Ile Ser Gly Asp Lys Gly Leu Thr Leu Ile Glu Met Gly Pro Phe 115 120 125 Gly Val Ile Gly Gly Ile Thr Pro Ser Thr Asn Pro Ser Ala Thr Val 130 135 140 Met Cys Asn Ser Ile Gly Met Ile Ala Ser Gly Asn Ala Ala Val Phe 145 150 155 160 Ser Pro His Pro Gly Ala Ile Glu Ser Cys Leu Ile Ser Val Arg Val 165 170 175 Leu Asn Lys Ala Ile Thr Asp Ala Gly Gly Pro Arg Asn Leu Ile Thr 180 185 190 Thr Leu Arg Lys Pro Ser Leu Glu Ser Thr Asp Thr Met Ile Asn Asn 195 200 205 Pro Lys Ile Arg Leu Val Val Ala Thr Gly Gly Pro Phe Ile Val Lys 210 215 220 Lys Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Val Lys Ala Ala Arg 245 250 255 Asp Ile Ile Ala Gly Cys Cys Phe Asp Asn Asn Leu Pro Cys Ile Ala 260 265 270 Glu Lys Glu Ala Ile Val Val Glu Ser Val Tyr Glu Lys Leu Ile Ala 275 280 285 Glu Met Leu Lys Asn Gly Asn Val Tyr Glu Leu Asp Glu Gln Gln Lys 290 295 300 Gln Lys Val Leu Asp Val Val Met Asn Lys Thr Glu Lys Gly Gly Lys 305 310 315 320 Ile Lys Tyr Gly Val Asn Lys Asn Phe Val Gly Lys Asp Ala Ser Val 325 330 335 Ile Leu Ala Ala Ala Gly Ile Glu Ala Pro Lys Gly Val Glu Cys Leu 340 345 350 Ile Cys Arg Ala Glu Asn Leu His Pro Phe Val Gln Glu Glu Leu Met 355 360 365 Met Pro Ile Leu Ala Ile Val Lys Val Lys Asp Val Asp Glu Ala Ile 370 375 380 Asn Thr Ala Val Leu Asp Glu His Gly Asn Arg His Thr Ala Met Met 385 390 395 400 His Ser Lys Asn Ile Asp Asn Leu Thr Lys Met Ser Arg Leu Ile Asp 405 410 415 Thr Thr Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Gly Ile Gly Phe 420 425 430 Gly Gly Glu Gly Trp Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu 435 440 445 Gly Ile Thr Asn Ala Thr Ser Phe Thr Arg Gln Arg Arg Cys Thr Met 450 455 460 Val Asp Ser Phe Arg Ile Ile 465 470 <210> 325 <211> 483 <212> PRT <213> Artificial Sequence <220> <223> bacterium MS4 <400> 325 Met Asp Ile Asp Ala Asn Leu Ile Glu Lys Met Val Lys Gln Val Leu 1 5 10 15 Asn Glu Ile Asp Ala Gly Lys Ala Glu Lys Thr Ala Ala Ala Glu Ile 20 25 30 Lys Lys Glu Glu Lys Gly Gly Ala Tyr Gly Ile Phe Asn Thr Met Glu 35 40 45 Glu Ala Ile Asp Ala Cys Asp Ile Ala Gln Lys Gln Tyr Leu Phe Cys 50 55 60 Ser Met Ala Glu Arg Gln Lys Tyr Val Gln Thr Leu Arg Asp Val Val 65 70 75 80 Leu Lys Gln Glu Asn Leu Glu Leu Ile Ser Arg Leu Ala Val Glu Glu 85 90 95 Thr Gly Met Gly Asn Tyr Pro His Lys Leu Ile Lys Asn Arg Leu Ala 100 105 110 Ala Glu Lys Ser Pro Gly Ile Glu Asp Leu Glu Thr Thr Ala Leu Ser 115 120 125 Gly Asp Asp Gly Leu Thr Leu Val Glu Tyr Cys Pro Phe Gly Val Ile 130 135 140 Gly Ala Ile Thr Pro Ala Thr Asn Pro Thr Glu Thr Ile Ile Cys Asn 145 150 155 160 Ser Ile Gly Met Leu Ala Ala Gly Asn Ser Ile Val Phe Ser Pro His 165 170 175 Pro Arg Ala Lys Asp Val Thr Ile Arg Leu Val Thr Met Ile Asn Arg 180 185 190 Ala Leu Glu Glu Thr Gly Ala Pro Lys Asn Leu Ile Val Thr Val Met 195 200 205 Glu Pro Ser Ile Glu Asn Thr Asn Val Met Met Lys His Pro Lys Ile 210 215 220 Arg Met Leu Val Ala Thr Gly Gly Pro Gly Ile Val Lys Leu Val Met 225 230 235 240 Ser Thr Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val 245 250 255 Val Val Asp Glu Thr Ala Asp Ile Lys Lys Ala Ala Ile Asp Ile Val 260 265 270 Asn Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu 275 280 285 Val Ile Ala Val Asp Arg Ile Thr Asp Glu Leu Ile Arg Ser Met Arg 290 295 300 Glu Asn Gly Ala Tyr Gln Val Thr Asp Pro Ala Val Ile Gln Lys Leu 305 310 315 320 Ala Asp Leu Val Arg Lys Glu Gly Gly Gly Pro Lys Thr Ser Phe Val 325 330 335 Gly Lys Ser Ala Ile Tyr Ile Leu Asp Lys Ile Gly Ile Gln Ala Gly 340 345 350 Pro Glu Val Lys Val Ile Ile Met Glu Thr Pro Lys Asp His Pro Phe 355 360 365 Val Met Glu Glu Leu Met Met Pro Ile Leu Pro Ile Val Arg Thr Arg 370 375 380 Asn Val Asp Glu Ala Ile Asp Leu Ala Leu Ile Ala Glu Arg Gly Asn 385 390 395 400 Arg His Thr Ala Met Met His Ser Lys Asn Val Asp Lys Leu Thr Lys 405 410 415 Met Ala Lys Leu Leu Gln Thr Thr Ile Phe Val Lys Asn Ala Pro Ser 420 425 430 Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly His Thr Thr Phe Thr Ile 435 440 445 Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys Ser Phe Cys Arg 450 455 460 Lys Arg Arg Cys Val Leu Ser Asp Ala Phe His Ile Arg Asp Phe Ser 465 470 475 480 Lys Gly Leu <210> 326 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Clostridium glycyrrhizinilyticum <400> 326 Val Ser Val Asn Glu Gln Met Val Gln Asp Ile Val Gln Glu Val Met 1 5 10 15 Ala Lys Met Gln Ile Thr Ser Asp Val Ser Gly Ser His Gly Val Phe 20 25 30 Lys Asp Met Asn Glu Ala Ile Ala Ala Ala Lys Lys Thr Gln Lys Ile 35 40 45 Val Gly Lys Met Ser Met Asp Gln Arg Glu Lys Ile Ile Ser Asn Ile 50 55 60 Arg Thr Lys Ile Lys Glu Asn Ala Glu Ile Met Ala Arg Met Gly Val 65 70 75 80 Gln Glu Thr Gly Met Gly Asn Val Gly His Lys Ile Leu Lys His Val 85 90 95 Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Val Leu 130 135 140 Cys Asn Thr Ile Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Phe Ala Ile Asn Leu Leu 165 170 175 Asn Glu Ala Ser Leu Glu Ala Gly Gly Pro Asp Asn Ile Ala Cys Thr 180 185 190 Val Glu Lys Pro Thr Leu Ala Ser Ser Asp Ile Met Met Lys His Lys 195 200 205 Asp Ile Pro Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Glu Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Asp Ser Ile Ala Asp Glu Leu Met Tyr Tyr 275 280 285 Met Val Ser Glu Gln Gly Cys Tyr Lys Ile Thr Lys Glu Glu Gln Asp 290 295 300 Ala Leu Thr Ala Val Val Leu Lys Asp Gly Lys Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Lys Thr Leu Leu Gly Met Ile Gly Val Thr Val 325 330 335 Pro Asp Asn Ile Arg Cys Ile Thr Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Ala Glu Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Lys Asp Phe Asp Asp Ala Val Glu Gln Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Val Asp Asn Ile Thr 385 390 395 400 Thr Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Gly Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Tyr Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Thr Asp Ser Leu Cys Ile Arg 450 455 460 <210> 327 <211> 482 <212> PRT <213> Artificial Sequence <220> <223> Thermincola ferriacetica <400> 327 Met Ala Ile Glu Ala Tyr Gln Ile Glu Lys Ile Val Glu Glu Val Met 1 5 10 15 Lys Lys Met Val Ser Gly Gly Ser Gly Asp Ser Phe Ala Gly Lys Ala 20 25 30 Lys Gly Ile Phe Glu Ser Val Asp Glu Ala Val Lys Ala Ala Lys Ala 35 40 45 Ala Gln Lys Glu Leu Val Ala Met Arg Ile Glu Lys Arg Glu Met Leu 50 55 60 Leu Lys Ala Met Arg Glu Ala Ala Ile Ala His Ala Glu Glu Leu Ala 65 70 75 80 Arg Leu Ala Val Glu Glu Thr Gly Met Gly Arg Val Thr Asp Lys Ile 85 90 95 Ile Lys Asn Arg Val Ala Ala Glu Lys Thr Pro Gly Thr Glu Asn Leu 100 105 110 Gln Pro Ser Ala Val Thr Gly Asp Arg Gly Leu Thr Leu Ile Glu Arg 115 120 125 Ala Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro Cys 130 135 140 Ala Thr Val Ile Asn Asn Ser Ile Ser Met Val Ala Ala Gly Asn Ser 145 150 155 160 Val Val Phe Ser Val His Pro Gly Ala Lys Lys Ala Ser Leu Leu Thr 165 170 175 Val Glu Ile Leu Asn Glu Ala Ile Glu Lys Ala Gly Gly Pro Ala Asn 180 185 190 Val Leu Thr Ala Val Ala Ser Pro Ser Leu Glu Asn Thr Asn Ala Leu 195 200 205 Met Lys His Pro Asp Ile Lys Leu Leu Val Ala Thr Gly Gly Pro Gly 210 215 220 Leu Val Lys Ala Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly 225 230 235 240 Ala Gly Asn Pro Pro Ala Leu Val Asp Glu Thr Ala Asp Leu Glu Arg 245 250 255 Ala Ala Lys Ser Ile Val Ala Gly Ala Ser Phe Asp Asn Asn Leu Pro 260 265 270 Cys Ile Ala Glu Lys Glu Val Ile Val Val Asp Tyr Val Ala Asn Gln 275 280 285 Leu Ile Ser Tyr Met Lys Gln Asn Gly Ala Tyr Leu Ala Asn Asp Arg 290 295 300 Glu Ile Lys Ala Leu Met Asp Leu Val Leu Thr Lys Asn Glu Asn Leu 305 310 315 320 Lys Ala Glu Gly Cys Thr Val Lys Pro Glu Lys Leu Tyr Gly Gly Ile 325 330 335 Asn Lys Glu Tyr Val Gly Lys Asp Ala Ala Tyr Ile Met Lys Lys Ile 340 345 350 Gly Val Asp Ile Pro Glu Asp Thr Lys Leu Ile Ile Cys Glu Val Asp 355 360 365 Glu Asp His Pro Phe Val Leu Glu Glu Leu Met Met Pro Ile Leu Pro 370 375 380 Ile Val Arg Val Pro Asn Val Gln Lys Ala Ile Glu Val Gly Val Arg 385 390 395 400 Val Glu His Gly Asn Arg His Thr Ala Val Met His Ser Gln Asn Ile 405 410 415 Asp Asn Leu Ser Ala Phe Ala Arg Ala Ile Gln Thr Thr Ile Phe Val 420 425 430 Lys Asn Gly Pro Ser Tyr Ala Gly Ile Gly Ile Gly Gly Glu Gly Tyr 435 440 445 Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ala Ala 450 455 460 Ser Ser Phe Thr Arg Gln Arg Arg Cys Val Leu Val Asp Gly Phe Ser 465 470 475 480 Ile Val <210> 328 <211> 461 <212> PRT <213> Artificial Sequence <220> <223> Lachnospiraceae bacterium AC3007 <400> 328 Met Asn Glu Lys Leu Val Gln Glu Ile Val Arg Arg Val Met Ala Asp 1 5 10 15 Ile Asn Asp Glu Gly Gly Ala Asp Gly Met His Gly Val Phe Ser Asp 20 25 30 Met Asn Asp Ala Ile Glu His Ala Leu Lys Ala Gln Glu Lys Val Arg 35 40 45 Val Met Thr Leu Asp Gln Arg Glu Lys Ile Ile Ser Ala Ile Arg Arg 50 55 60 Lys Thr Asn Glu Asn Val Glu Thr Ile Ala Arg Met Gly Val Glu Glu 65 70 75 80 Thr Gly Met Gly Asn Val Gly Asp Lys Ile Leu Lys His Lys Leu Thr 85 90 95 Ala Asp Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala Trp Ser 100 105 110 Gly Asp Arg Gly Leu Thr Leu Val Glu Met Gly Pro Phe Gly Val Ile 115 120 125 Gly Ala Ile Thr Pro Ala Thr Asn Pro Ser Glu Thr Val Ile Cys Asn 130 135 140 Ser Ile Gly Met Ile Ala Gly Gly Asn Thr Val Val Phe Asn Pro His 145 150 155 160 Pro Asn Ala Lys Lys Thr Thr Ile Tyr Thr Ile Asn Met Ile Asn Glu 165 170 175 Ala Ser Leu Glu Ala Gly Gly Pro Asp Asn Ile Ala Cys Thr Val Gln 180 185 190 Glu Pro Thr Met Glu Thr Ser Ala Ile Met Met Lys His Pro Lys Ile 195 200 205 Pro Leu Leu Val Ala Thr Gly Gly Pro Gly Val Val Thr Ala Val Leu 210 215 220 Ser Ser Gly Lys Arg Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Ala 225 230 235 240 Leu Val Asp Glu Thr Ala Asp Ile Glu Lys Ala Ala Arg Asp Ile Ile 245 250 255 Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu 260 265 270 Val Val Ala Val Asp Ala Ile Phe Asp Glu Leu Met Arg His Phe Glu 275 280 285 Glu Glu Asn Gly Cys Tyr Arg Ala Ser Arg Glu Ile Gln Asp Lys Leu 290 295 300 Ile Ala Thr Val Ile Thr Pro Lys Gly Ala Leu Asn Arg Lys Cys Val 305 310 315 320 Gly Arg Asp Ala Lys Thr Leu Leu Lys Met Val Gly Val Asp Ala Pro 325 330 335 Ala Asp Thr Arg Cys Ile Ile Phe Glu Gly Glu Lys Glu His Pro Leu 340 345 350 Ile Ala Thr Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Val Lys 355 360 365 Asp Phe Arg Glu Gly Val Glu Thr Ala Val Trp Leu Glu His Gly Asn 370 375 380 Arg His Ser Ala His Ile His Ser Lys Asn Val Asp Arg Ile Thr Glu 385 390 395 400 Tyr Ala Arg Ala Leu Asp Thr Ala Ile Leu Val Lys Asn Gly Pro Ser 405 410 415 Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Tyr Pro Thr Phe Thr Ile 420 425 430 Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr Lys 435 440 445 Arg Arg Arg Cys Val Met Thr Asp Ser Leu Cys Ile Arg 450 455 460 <210> 329 <211> 471 <212> PRT <213> Artificial Sequence <220> <223> Eubacterium sp. 14-2 <400> 329 Met Asn Ile Asp Glu Arg Val Val Ala Ser Ile Val Asn Ala Val Leu 1 5 10 15 Gly Arg Leu Asp Asp Val Ser Ser Pro Ala Ala Glu Ala Gly Gly Gly 20 25 30 Asn Trp Gly Ile Phe Glu Ser Met Asn Asp Ala Val Glu Ala Ala Ala 35 40 45 Ala Ala Gln Lys Lys Tyr Ile Asn Cys Thr Met His Asp Arg Ala Ala 50 55 60 Tyr Val Gln Ala Ile Arg Asp Val Val Leu Lys Gln Glu Asn Leu Glu 65 70 75 80 Tyr Ile Ser Arg Gln Ser Ala Glu Glu Thr Gly Met Gly Asn Tyr Glu 85 90 95 His Lys Leu Ile Lys Asn Arg Leu Ala Ala Thr Lys Thr Pro Gly Thr 100 105 110 Glu Asp Leu Thr Thr Asp Ala Met Ser Gly Asp Asp Gly Leu Thr Leu 115 120 125 Val Glu Tyr Ser Pro Phe Gly Val Ile Gly Ala Ile Thr Pro Thr Thr 130 135 140 Asn Pro Thr Glu Thr Ile Ile Cys Asn Ser Ile Gly Met Leu Ala Ala 145 150 155 160 Gly Asn Ser Val Val Phe Ser Pro His Pro Arg Ala Lys Asn Val Ser 165 170 175 Leu His Leu Ile Arg Leu Ile Asn Arg Ala Leu Ala Glu Ala Gly Ala 180 185 190 Pro Ala Asn Leu Val Val Thr Val Ser Gln Pro Ser Ile Glu Asn Thr 195 200 205 Asn Ala Met Met Ser His Pro Met Val Arg Met Leu Val Ala Thr Gly 210 215 220 Gly Pro Gly Ile Val Lys Thr Val Leu Ser Ser Gly Lys Lys Ala Ile 225 230 235 240 Gly Ala Gly Ala Gly Asn Pro Pro Val Val Val Asp Glu Thr Ala Asn 245 250 255 Ile Glu Lys Ala Gly Lys Asp Ile Ile Asp Gly Cys Cys Phe Asp Asn 260 265 270 Asn Leu Pro Cys Ile Ala Glu Lys Glu Val Ile Val Val Asp Ser Ala 275 280 285 Ala Asp Tyr Leu Ile Phe Asn Met Lys Lys Asn Gly Ala Tyr Glu Val 290 295 300 Lys Asp Pro Glu Ile Ile Asp Arg Ile Val Lys Leu Val Val Gln Glu 305 310 315 320 Asn Gly Lys Ser Pro Val Thr Ser Phe Val Gly Lys Ser Ala Lys Tyr 325 330 335 Ile Leu Glu Gln Ala Gly Val His Val Asp Asp Asp Val Arg Val Ile 340 345 350 Ile Ala Gln Thr Gly Glu Asp His Pro Phe Val Gln Val Glu Leu Met 355 360 365 Met Pro Ile Leu Pro Ile Val Arg Val Pro Asp Val Asp Ala Gly Ile 370 375 380 Glu Met Ala Val Arg Val Glu His Gly Asn Arg His Thr Ala Met Met 385 390 395 400 His Ser Arg Asn Val Asp Lys Leu Thr Lys Met Ala Lys Leu Ile Gln 405 410 415 Thr Thr Ile Phe Val Lys Asn Gly Pro Ser Tyr Ala Gly Ile Gly Val 420 425 430 Gly Gly Glu Gly Tyr Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu 435 440 445 Gly Leu Thr Ser Ala Lys Ser Phe Ala Arg Arg Arg Arg Cys Val Leu 450 455 460 Val Gly Gly Met Asp Val Arg 465 470 <210> 330 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Anaerosalibacter massiliensis <400> 330 Met Glu Leu Asp Lys Met Asp Leu Glu Gln Ile Val Asn Leu Val Val 1 5 10 15 Glu Gln Leu Lys Gly Glu Asp Thr Ser Ser Tyr Cys Lys Glu Glu Ser 20 25 30 Lys Asn Gly Val Phe Asn Asn Met Asn Glu Ala Ile Glu Lys Ala Tyr 35 40 45 Ile Ala Gln Lys Asp Phe Phe Lys Asn Tyr Asn Leu Glu Asp Arg Arg 50 55 60 Arg Ile Ile Lys Thr Ile Arg Lys Glu Leu Met Glu Asp Val Glu Leu 65 70 75 80 Leu Ala Lys Leu Gly Val Glu Asp Thr Gly Met Gly Arg Tyr Glu Asp 85 90 95 Lys Leu Lys Lys Asn Lys Leu Val Ile Glu Lys Thr Pro Gly Val Glu 100 105 110 Asp Leu Asn Ser Glu Val Phe Thr Gly Asp Asn Gly Leu Thr Leu Val 115 120 125 Glu Leu Ser Pro Tyr Gly Val Ile Gly Ala Ile Ala Pro Ser Thr Asn 130 135 140 Pro Ser Glu Thr Val Ile Cys Asn Ser Ile Gly Met Ile Ala Ala Gly 145 150 155 160 Asn Ser Val Val Phe Ser Pro His Pro Gly Ala Lys Asn Ile Ser Met 165 170 175 Lys Thr Val Glu Leu Ile Asn Lys Ala Ile Glu Lys Ala Gly Gly Pro 180 185 190 Lys Asn Leu Val Val Thr Thr Ser Asn Pro Ser Ile Glu Asn Ala Glu 195 200 205 Ile Met Met Lys His Glu Lys Ile Lys Met Ile Val Ala Thr Gly Gly 210 215 220 Pro Gly Val Val Lys Ser Ala Leu Ser Gln Gly Lys Lys Ala Ile Gly 225 230 235 240 Ala Gly Ala Gly Asn Pro Pro Ala Val Ile Asp Glu Thr Ala Asp Ile 245 250 255 Glu Lys Ala Ala Arg Asp Ile Ile Ala Gly Cys Ser Phe Asp Asn Asn 260 265 270 Leu Pro Cys Ile Ala Glu Lys Glu Val Ile Val Val Asp Ser Val Ala 275 280 285 Asp Tyr Leu Ile Phe Ser Met Asn Lys Asn Asn Val Tyr His Leu Lys 290 295 300 Asp Glu Glu Lys Ile Asp Lys Leu Ala Ser Met Val Ile Asp Lys Asn 305 310 315 320 Gly Arg Ile Asn Arg Lys Phe Val Gly Lys Asp Ala Lys Val Ile Leu 325 330 335 Lys Ala Val Asp Ile Glu Cys Glu His Asp Val Arg Ala Ile Ile Val 340 345 350 Glu Thr Glu Lys Asp His Pro Phe Val Val Thr Glu Leu Met Met Pro 355 360 365 Ile Leu Pro Ile Val Arg Val Lys Asp Ile Asp Glu Ala Ile Lys Leu 370 375 380 Ala Val Glu Val Glu Gln Gly Asn Arg His Thr Ala Ile Met His Ser 385 390 395 400 Lys Asn Val Asp Asn Leu Ser Arg Phe Ala Arg Glu Ile Glu Thr Thr 405 410 415 Ile Phe Val Lys Asn Ala Pro Ser Phe Ala Gly Leu Gly Phe Gly Gly 420 425 430 Glu Gly Tyr Pro Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu 435 440 445 Thr Ser Ala Arg Ser Phe Ala Arg Lys Arg Arg Cys Ser Leu Val Gly 450 455 460 Ser Phe Ser Ile Lys 465 <210> 331 <211> 473 <212> PRT <213> Artificial Sequence <220> <223> Clostridium indolis DSM 755 <400> 331 Met Glu Ile Gly Ala Lys Glu Ile Glu Leu Ile Val Arg Glu Val Leu 1 5 10 15 Ala Gly Ile Glu Ser Arg Gly Ile Lys Pro Ser Tyr Thr Pro Ser Arg 20 25 30 Ser Glu Asp Gly Val Phe Glu Arg Val Glu Asp Ala Ile Glu Ala Ala 35 40 45 Tyr Ala Ala Gln Arg Glu Trp Val Glu His Tyr Arg Val Glu Asp Arg 50 55 60 Arg Arg Ile Ile Glu Ala Ile Arg Val Thr Ala Lys Ser His Ala Glu 65 70 75 80 Ser Leu Ala Lys Met Val Trp Glu Glu Thr Gly Met Gly Arg Phe Glu 85 90 95 Asp Lys Ile Gln Lys His Met Ala Val Ile Glu Lys Thr Pro Gly Val 100 105 110 Glu Cys Leu Thr Thr Glu Ala Ile Ser Gly Asp Gly Gly Leu Met Ile 115 120 125 Glu Glu Tyr Ala Pro Phe Gly Val Ile Gly Ala Ile Thr Pro Ser Thr 130 135 140 Asn Pro Thr Glu Thr Ile Ile Asn Asn Thr Ile Ser Met Ile Ala Gly 145 150 155 160 Gly Asn Ser Val Val Phe Asn Val His Pro Gly Ala Lys Arg Cys Cys 165 170 175 Ala His Cys Leu Lys Ile Leu His Gln Ala Ile Val Glu Asn Gly Gly 180 185 190 Pro Ala Ser Leu Ile Thr Met Gln Lys Glu Pro Asp Met Glu Ala Val 195 200 205 Ser Lys Leu Thr Ser Asp Pro Arg Ile Arg Leu Met Val Gly Thr Gly 210 215 220 Gly Met Pro Met Val Asn Ala Leu Leu Arg Ser Gly Lys Lys Thr Ile 225 230 235 240 Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val Asp Asp Thr Ala Asp 245 250 255 Val Ser Leu Ala Ala Arg Glu Ile Tyr Arg Gly Ala Ser Phe Asp Asn 260 265 270 Asn Ile Leu Cys Leu Ala Glu Lys Glu Val Phe Val Met Glu Arg Ala 275 280 285 Ala Asp Glu Leu Val Asn Lys Leu Ile Lys Glu Gly Ala Tyr Leu Leu 290 295 300 Ser Ser Leu Glu Leu Ser Glu Ile Leu Lys Phe Ala Met Val Glu Lys 305 310 315 320 Asn Gly Ser Tyr Glu Val Asn Lys Lys Trp Val Gly Lys Asp Ala Gly 325 330 335 Gln Phe Leu Glu Ala Ile Gly Val Ser Gly His Lys Asp Val Arg Leu 340 345 350 Leu Ile Cys Glu Thr Asp Arg Ser His Pro Phe Val Met Val Glu Gln 355 360 365 Leu Met Pro Ile Leu Pro Ile Val Arg Leu Arg Thr Phe Glu Glu Cys 370 375 380 Val Glu Ser Ala Leu Ala Ala Glu Ser Gly Asn Arg His Thr Ala Ser 385 390 395 400 Met Phe Ser Arg Asn Val Glu Asn Met Thr Lys Phe Gly Lys Ile Ile 405 410 415 Glu Thr Thr Ile Phe Thr Lys Asn Gly Ser Thr Leu Lys Gly Val Gly 420 425 430 Ile Gly Gly Glu Gly His Thr Thr Met Thr Ile Ala Gly Pro Thr Gly 435 440 445 Glu Gly Leu Thr Cys Ala Arg Ser Phe Thr Arg Arg Arg Arg Cys Met 450 455 460 Leu Ala Glu Gly Gly Leu Arg Ile Ile 465 470 <210> 332 <211> 467 <212> PRT <213> Artificial Sequence <220> <223> Catabacter hongkongensis <400> 332 Met Gly Leu Ser Glu Gln Gln Ile Lys Gln Ile Val Glu Glu Thr Val 1 5 10 15 Arg Asn Ile Gly Thr Gly Thr Ala Gly Ala Ala Cys Ser Gly Ser Trp 20 25 30 Met Cys Asp Asp Ala Asn Asp Ala Val Glu Asn Ala Lys Arg Ala Gln 35 40 45 Lys Gln Leu Met Thr Met Thr Leu Glu Gln Arg Gly Arg Leu Val Ser 50 55 60 Ala Met Arg Glu Ala Ala Leu Ala Asn Ser Val Lys Leu Ala Glu Met 65 70 75 80 Ala His Glu Glu Thr Gly Tyr Gly Ser Val Glu His Lys Ile Met Lys 85 90 95 Asn Glu Leu Ala Ala Lys Lys Thr Pro Gly Ile Glu Asp Leu His Thr 100 105 110 Gln Ala Phe Ser Gly Asp Asp Gly Leu Thr Ile Val Glu Gln Ala Pro 115 120 125 Phe Gly Val Ile Gly Ser Ile Thr Pro Ser Thr Asn Pro Thr Ser Thr 130 135 140 Val Ile Asn Asn Ser Ile Ser Met Val Ala Ala Gly Asn Ala Val Val 145 150 155 160 Tyr Asn Pro His Pro Ala Ala Lys Arg Ala Ser Gln Glu Ala Met Arg 165 170 175 Ile Leu Asn Glu Ala Ile Val Ser Ala Gly Gly Pro Ala Thr Leu Ile 180 185 190 Thr Thr Val Lys Glu Pro Thr Leu Glu Ser Gly Gln Val Ile Met Asn 195 200 205 His Arg Asp Ile Lys Met Leu Ser Ile Thr Gly Gly Glu Ala Val Val 210 215 220 Ala Val Ala Met Lys Thr Gly Lys Lys Val Val Ala Ala Gly Pro Gly 225 230 235 240 Asn Pro Pro Val Ile Val Asp Asp Thr Ala Val Ile Pro Lys Ala Ala 245 250 255 Lys Asp Ile Val Asp Gly Ala Ser Phe Asp Asn Asn Val Leu Cys Val 260 265 270 Ala Glu Lys Glu Val Phe Ala Phe Asp Asn Ile Thr Asp Gln Leu Met 275 280 285 Ser Glu Met Glu Lys Asn Gly Ala Tyr Arg Val Ser Gly Glu Asp Ile 290 295 300 Asn Lys Ile Val Asn Thr Val Leu Val Leu Lys Asp Gly His Tyr Val 305 310 315 320 Ile Asn Arg Lys Phe Val Gly Arg Asp Ala Thr Tyr Ile Met Gln Glu 325 330 335 Ser Gly Val Ser Tyr Thr Gly Asn Pro Arg Leu Val Ile Ala Glu Val 340 345 350 Ser Ala Asn His Pro Phe Val Thr Val Glu Met Leu Met Pro Val Leu 355 360 365 Gly Val Val Arg Val Arg Asn Ile Asp Glu Ala Val Asp Glu Ala Phe 370 375 380 Arg Ala Glu Arg Gly Cys Gln His Ser Ala Leu Ile His Ser Thr Asn 385 390 395 400 Ile Arg Asn Met Ser Lys Ala Ala Ser Thr Met Asn Thr Thr Ile Phe 405 410 415 Val Lys Asn Ala Pro Ser Tyr Ser Gly Leu Gly Phe Gly Gly Glu Gly 420 425 430 Tyr Ala Thr Leu Thr Ile Ala Thr Pro Thr Gly Glu Gly Leu Thr Ser 435 440 445 Ala Lys Thr Phe Thr Arg Ala Arg Arg Cys Val Leu Lys Gly Asp Leu 450 455 460 Arg Ile Ile 465 <210> 333 <211> 463 <212> PRT <213> Artificial Sequence <220> <223> Bacillus thermotolerans <400> 333 Met Ala Val Gln Glu Arg Asp Leu Glu Ser Ile Val Lys Lys Val Leu 1 5 10 15 Glu Glu Leu Ser Arg Lys Glu Glu Thr Pro Glu Ala Gly Gln Gly Val 20 25 30 Phe Glu Asp Met Asn Asp Ala Ile Glu Ala Ala Glu Gln Ala Gln Lys 35 40 45 Glu Leu Ile Lys Leu Ser Leu Glu Glu Arg Gly Ala Ile Ile Glu Ala 50 55 60 Ile Arg Glu Ala Ser Arg Lys His Val Glu Thr Phe Ala Arg Met Ala 65 70 75 80 Val Glu Glu Thr Gly Met Gly Asn Tyr Glu Asp Lys Val Arg Lys Asn 85 90 95 Val Leu Val Ile Asp Lys Thr Pro Gly Ile Glu Asp Leu Lys Thr Glu 100 105 110 Ala Val Ser Gly Asp Asn Gly Leu Thr Val Val Glu Leu Ser Pro Tyr 115 120 125 Gly Val Ile Gly Ser Ile Thr Pro Thr Thr Asn Pro Thr Glu Thr Ile 130 135 140 Ile Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn Ser Val Val Phe 145 150 155 160 Ser Pro His Pro Gly Ala Lys Asp Thr Ser Leu Lys Ala Val Glu Ile 165 170 175 Ile Asn Gln Ala Ile Val Glu Ala Gly Gly Pro Lys Asn Leu Ile Thr 180 185 190 Ser Ile Ala Glu Pro Ser Ile Asp Gln Ala Asn Ile Met Met Arg His 195 200 205 Lys Lys Val Arg Met Leu Val Ala Thr Gly Gly Pro Gly Val Val Lys 210 215 220 Ala Val Leu Thr Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Val Val Val Asp Glu Thr Ala Asp Leu Glu Lys Ala Ala Lys 245 250 255 Asp Ile Val Asp Gly Cys Ser Phe Asp Asn Asn Ile Pro Cys Val Ala 260 265 270 Glu Lys Glu Leu Phe Val Val Glu Ala Val Ala Asp Tyr Leu Val Phe 275 280 285 His Met Lys Lys His Gly Ala Phe Gln Leu Asn Asp Pro Lys His Val 290 295 300 Glu Lys Leu Thr Glu Leu Val Val Asp Asn Gly His Ala Asn Lys Glu 305 310 315 320 Phe Val Gly Lys Asp Ile Gln Tyr Ile Leu Lys Gln Ile Gly Val Asp 325 330 335 Ala Pro Gln Asp Ala Arg Ile Ala Ile Met Asp Val Gly Ala Asp His 340 345 350 Pro Leu Val Ser Ala Glu Leu Met Met Pro Ile Leu Pro Val Val Arg 355 360 365 Thr Ala Asn Val Asp Glu Ala Ile Glu Leu Ala Val Glu Ala Glu His 370 375 380 Gly Phe Arg His Thr Ser Ile Met His Ser Lys Asn Ile Asp Asn Leu 385 390 395 400 Thr Lys Phe Ala Lys Ala Ile Gln Thr Thr Ile Phe Val Lys Asn Gly 405 410 415 Pro Ser Tyr Ala Gly Leu Gly Val Gly Gly Glu Gly Tyr Thr Ser Phe 420 425 430 Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys Asp Phe 435 440 445 Ala Arg Lys Arg Lys Cys Val Leu Val Asp Ser Leu Ser Val Arg 450 455 460 <210> 334 <211> 511 <212> PRT <213> Artificial Sequence <220> <223> Gracilibacillus kekensis <400> 334 Met Gln Leu Asn Glu Lys Asp Ile Gln Thr Ile Ile Asp Ser Val Leu 1 5 10 15 Lys Asn Val Glu Ala Ala Val Glu Asn Arg Gln Pro Thr Gln Ala Ser 20 25 30 Gly Gln Ser Ser Glu Gln Gln Pro Ile Lys Met Lys Gln Leu Ser Pro 35 40 45 Ser Ala Pro Ser Asn Thr Phe Asn Met Ser Ser Asn Lys Asp Gly Val 50 55 60 Phe Glu Arg Val Thr Asp Ala Ile Glu Ala Ala Ser Lys Ala Gln Glu 65 70 75 80 Val Trp Met Lys Gln Tyr Thr Leu Glu Glu Lys Glu Asn Leu Ile Asn 85 90 95 Ser Ile Arg Gln Ala Val Ala Gln Gln Val Asn His Phe Ala Lys Ser 100 105 110 Ala Leu Glu Glu Thr Gly Leu Gly Asn Tyr Glu Asp Lys Val Leu Lys 115 120 125 Leu Ser Leu Thr Val Glu Lys Thr Pro Gly Thr Glu Leu Leu Gln Thr 130 135 140 Glu Thr Phe Ser Gly Asp Asp Gly Leu Ser Phe Val Glu Gln Thr Pro 145 150 155 160 Phe Gly Val Ile Gly Ala Val Thr Pro Val Thr Asn Pro Ile Asp Thr 165 170 175 Ile Val Asn Asn Gly Ile Gly Met Ile Ala Ala Gly Asn Ala Val Val 180 185 190 Phe Asn Val His Pro Ser Ala Lys Lys Thr Ser Arg Glu Met Ile Gln 195 200 205 Leu Leu Asn Gln Thr Ile Val Asn Ala Gly Gly Pro Glu Asn Leu Leu 210 215 220 Thr Met Val Gln Glu Pro Thr Ile Glu Thr Val Gln Glu Ile Ala Asn 225 230 235 240 His Pro Ser Val Lys Leu Leu Val Gly Thr Gly Gly Pro Gly Met Val 245 250 255 Lys Ser Leu Leu Lys Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly 260 265 270 Asn Pro Pro Val Ile Val Asp Glu Thr Ala Asp Leu Lys Gln Ala Ala 275 280 285 Lys Asp Ile Ile Glu Gly Ala Ser Phe Asp Asn Asn Leu Leu Cys Ile 290 295 300 Ala Glu Lys Glu Val Phe Val Leu Asp Gln Val Ala Asp Asp Leu Ile 305 310 315 320 Phe Glu Leu Leu Asn Gln Gln Val His Met Leu Asp His Gln Gln Leu 325 330 335 Glu Lys Val Met Lys Leu Thr Leu Lys Glu Asn Thr Glu Gly Ile Pro 340 345 350 Gly Gly Cys Ser Tyr Leu Ser Arg Asp Tyr Leu Val Ser Lys Asp Trp 355 360 365 Val Gly Lys Asp Ala Thr Gln Ile Leu Glu Gln Ile Gly Val Ser Asn 370 375 380 Val Gln Thr Lys Leu Leu Ile Cys Glu Val Asp Ala Glu His Pro Tyr 385 390 395 400 Val Gln Leu Glu Gln Leu Met Pro Ile Leu Pro Ile Val Arg Val Lys 405 410 415 Ser Val Asp Glu Ala Ile Glu Lys Ala Val Lys Ala Glu His Gly Asn 420 425 430 Arg His Thr Ala Val Met His Ser Asn His Ile Lys Asn Val Thr Lys 435 440 445 Phe Ala Lys Ala Ile Gly Thr Thr Ile Phe Val Asn Asn Gly Ser Ser 450 455 460 Leu Ser Gly Val Gly Tyr Arg Gly Glu Gly Phe Thr Thr Met Thr Ile 465 470 475 480 Ala Gly Pro Thr Gly Glu Gly Val Thr Ser Ala Arg Thr Phe Thr Arg 485 490 495 Gln Arg Arg Thr Val Ile Ala Asn Gly Gly Phe Asn Ile Arg Gly 500 505 510 <210> 335 <211> 479 <212> PRT <213> Artificial Sequence <220> <223> Propionispora sp. 2/2-37 <400> 335 Met Ile Gln Glu Gln Glu Leu Ile Ala Lys Ile Thr Ala Gln Val Ile 1 5 10 15 Ala Gln Met Gln Gln Gly Gln Ala Ala Ala Val Pro Glu His Tyr Gly 20 25 30 Val Phe Asp Ser Ile Asp Gly Ala Val Ala Ala Ala Arg Lys Ala Tyr 35 40 45 Gln Ser Leu Arg Ala Leu Pro Leu Glu Lys Arg Glu Gln Leu Val Gly 50 55 60 Ala Met Arg Lys Thr Ala Tyr Asp His Ala Glu Ile Met Ala Glu Met 65 70 75 80 Ala Val Thr Glu Ser Gly Met Gly Arg Tyr Ser Asp Lys Val Ile Lys 85 90 95 Asn Arg Thr Ala Ala Leu Lys Thr Pro Gly Thr Glu Asp Leu Lys Thr 100 105 110 Arg Ala Trp Ser Gly Asp Cys Gly Leu Thr Leu Val Glu Met Gly Pro 115 120 125 Tyr Gly Val Ile Gly Ala Ile Thr Pro Thr Thr Asn Pro Thr Glu Thr 130 135 140 Leu Ile Cys Asn Gly Ile Gly Met Ile Ala Ala Gly Asn Ala Val Phe 145 150 155 160 Phe Ser Pro His Pro Thr Ala Lys Asn Thr Ser Ile Trp Thr Ile Gln 165 170 175 Leu Leu Asn Lys Ala Leu Val Glu Ala Gly Gly Pro Pro Asn Leu Leu 180 185 190 Thr Thr Val Tyr Asn Pro Ser Ile Ala Val Ala Asn Ala Met Met Lys 195 200 205 His Pro Asp Val Asn Met Leu Val Ala Thr Gly Gly Pro Gly Val Val 210 215 220 Lys Ala Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly 225 230 235 240 Asn Pro Pro Ala Val Val Asp Glu Thr Ala Asp Leu Glu Lys Ala Ala 245 250 255 Lys Asp Ile Val Ala Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys Ile 260 265 270 Ala Glu Lys Glu Val Ile Ala Val Gly Ser Ile Ala Asp Arg Leu Met 275 280 285 Asp Tyr Met Val Arg Asn Gly Ala Tyr Lys Ile Thr Pro Gln Gln Thr 290 295 300 Ala Glu Leu Val Asn Leu Leu Leu Thr Val Lys Glu Glu Lys Met Ala 305 310 315 320 Glu Gly Cys Thr Ala Lys Thr Lys Arg Thr Tyr Gly Ile Asn Lys Asp 325 330 335 Tyr Val Gly Lys Ser Ala Gln Cys Ile Leu Ser Lys Ile Gly Val Thr 340 345 350 Val Lys Asp Asp Ile Arg Val Ile Leu Cys Glu Ala Glu Ala Asp His 355 360 365 Pro Phe Val Leu Glu Glu Leu Met Met Pro Val Leu Pro Val Val Gln 370 375 380 Val Lys Asp Val Asp Ala Ala Ile Glu Leu Ala Val Arg Val Glu His 385 390 395 400 Gly Asn Arg His Thr Ala Val Met His Ser Lys Asn Val Asp His Leu 405 410 415 Thr Arg Met Ala Arg Ala Ile Asp Thr Thr Ile Phe Val Lys Asn Ala 420 425 430 Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Tyr Cys Thr Phe 435 440 445 Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Pro Arg Ser Phe 450 455 460 Thr Arg Ala Arg Arg Cys Val Leu Val Asp Gly Phe Ser Ile Val 465 470 475 <210> 336 <211> 478 <212> PRT <213> Artificial Sequence <220> <223> Clostridium chauvoei <400> 336 Val Phe Ser Asp Glu Lys Ser Ile Glu Glu Ile Val Ile Lys Val Leu 1 5 10 15 Glu Glu Ile His Thr Asp Arg Lys Thr Lys Cys Asn Lys Asn Cys Asn 20 25 30 Ser Asn Cys Gly Cys Asn Lys Asp Lys Phe Ile Phe Ser Ser Val Asp 35 40 45 Asp Ala Val Ala Ala Ala Lys Lys Ser Phe Phe Glu Leu Lys Lys Leu 50 55 60 Thr Ile Arg Glu Arg Glu Glu Ile Ile Lys Asn Ile Arg Lys Lys Cys 65 70 75 80 Leu Asp Tyr Ala Asp Lys Leu Ser Ile Met Ala Val Glu Glu Thr Gly 85 90 95 Met Gly Lys Val Glu Asp Lys Val Thr Lys His Ile Leu Ile Ala Glu 100 105 110 Lys Thr Pro Gly Thr Glu Asp Leu Lys Thr Thr Ala Trp Ser Gly Asp 115 120 125 Gly Gly Leu Thr Leu Ile Glu Gln Gly Ala Phe Gly Val Ile Ala Ala 130 135 140 Ile Thr Pro Ser Thr Asn Pro Thr Ala Thr Val Leu Cys Asn Ala Ile 145 150 155 160 Gly Met Ile Ser Ala Gly Asn Thr Ile Val Phe Ala Pro His Pro Asn 165 170 175 Ala Val Lys Cys Ser Asn Leu Ala Val Lys Leu Ile Asn Glu Ala Ser 180 185 190 Lys Glu Ala Gly Gly Pro Glu Asn Ile Ala Val Ser Phe Arg Lys Pro 195 200 205 Ser Ile Asp Ile Thr Thr Glu Leu Met Lys His Lys Asp Ile Ala Leu 210 215 220 Ile Ser Ala Thr Gly Gly Pro Gly Val Val Asn Gln Ala Leu Ser Ser 225 230 235 240 Gly Lys Arg Ala Leu Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val 245 250 255 Asp Glu Thr Ala Asn Ile Glu Lys Ala Ala Lys Asp Ile Ile Asp Gly 260 265 270 Ala Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu Val Ile 275 280 285 Val Ile Asp Ser Val Ser Asn Lys Leu Ile Glu Tyr Met Ile Lys Phe 290 295 300 Gly Ala Tyr Leu Leu Lys Asp Lys Glu Gln Ile Lys Arg Leu Glu Asp 305 310 315 320 Lys Leu Leu Ile Lys Asn Gly Lys Lys Val Thr Leu Asn Arg Asp Phe 325 330 335 Val Gly Lys Asp Ala Lys Val Ile Leu Asp Ser Ile Asp Ile Leu Val 340 345 350 Asp Asp Ser Ile Lys Cys Ile Ile Phe Glu Gly Asp Lys Asp Ser Leu 355 360 365 Leu Ile Lys Glu Glu Leu Met Met Pro Ile Leu Gly Ile Val Lys Val 370 375 380 Asn Asn Phe Asp Glu Ala Val Glu Cys Ala Leu Glu Leu Glu His Gly 385 390 395 400 Asn Arg His Ser Ala His Met His Ser Lys Asn Ile Asp Asn Leu Thr 405 410 415 Thr Phe Ala Arg Val Ile Asp Thr Ala Ile Phe Val Lys Asn Ala Pro 420 425 430 Ser Tyr Ser Ala Leu Gly Val Asn Ala Glu Gly Phe Ala Thr Phe Thr 435 440 445 Ile Ala Ser Lys Thr Gly Glu Gly Leu Ser Ser Thr Lys Thr Phe Thr 450 455 460 Lys Asn Arg Arg Cys Val Leu Ser Asp Gly Leu Ser Ile Arg 465 470 475 <210> 337 <211> 467 <212> PRT <213> Artificial Sequence <220> <223> 10500A -Thermoanaerobacterium aotearoense <400> 337 Met Lys Val Lys Glu Glu Asp Ile Glu Ala Ile Val Lys Lys Val Leu 1 5 10 15 Ser Glu Phe Asn Phe Glu Lys Asn Thr Lys Ser Phe Arg Asp Phe Gly 20 25 30 Val Phe Gln Asp Met Asn Asp Ala Ile Arg Ala Ala Lys Asp Ala Gln 35 40 45 Lys Lys Leu Arg Asn Met Ser Met Glu Ser Arg Glu Lys Ile Ile Gln 50 55 60 Asn Ile Arg Lys Lys Ile Met Glu Asn Lys Lys Ile Leu Ala Glu Met 65 70 75 80 Gly Val Ser Glu Thr Gly Met Gly Lys Val Glu His Lys Ile Ile Lys 85 90 95 His Glu Leu Val Ala Leu Lys Thr Pro Gly Thr Glu Asp Ile Val Thr 100 105 110 Thr Ala Trp Ser Gly Asp Lys Gly Leu Thr Leu Val Glu Met Gly Pro 115 120 125 Phe Gly Val Ile Gly Thr Ile Thr Pro Ser Thr Asn Pro Ser Glu Thr 130 135 140 Val Leu Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn Ser Val Val 145 150 155 160 Phe Asn Pro His Pro Gly Ala Val Asn Val Ser Asn Tyr Ala Val Lys 165 170 175 Leu Val Asn Glu Ala Val Met Glu Ala Gly Gly Pro Glu Asn Leu Val 180 185 190 Ala Ser Val Glu Lys Pro Thr Leu Glu Thr Gly Asn Ile Met Phe Lys 195 200 205 Ser Pro Asp Val Ser Leu Leu Val Ala Thr Gly Gly Pro Gly Val Val 210 215 220 Thr Ser Val Leu Ser Ser Gly Lys Arg Ala Ile Gly Ala Gly Ala Gly 225 230 235 240 Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Lys Lys Ala Ala 245 250 255 Lys Asp Ile Val Asp Gly Ala Thr Phe Asp Asn Asn Leu Pro Cys Ile 260 265 270 Ala Glu Lys Glu Val Val Ser Val Asp Lys Ile Thr Asp Glu Leu Ile 275 280 285 Tyr Tyr Met Gln Gln Asn Gly Cys Tyr Lys Ile Glu Gly Arg Glu Ile 290 295 300 Glu Lys Leu Ile Glu Leu Val Leu Asp His Lys Gly Gly Lys Ile Thr 305 310 315 320 Leu Asn Arg Lys Trp Val Gly Lys Asp Ala His Leu Ile Leu Lys Ala 325 330 335 Ile Gly Ile Asp Ala Asp Glu Ser Val Arg Cys Ile Ile Phe Glu Ala 340 345 350 Glu Lys Asp Asn Pro Leu Val Val Glu Glu Leu Met Met Pro Ile Leu 355 360 365 Gly Ile Val Arg Ala Lys Asn Val Asp Glu Ala Ile Met Ile Ala Thr 370 375 380 Glu Leu Glu His Gly Asn Arg His Ser Ala His Met His Ser Lys Asn 385 390 395 400 Val Asp Asn Leu Thr Lys Phe Gly Lys Ile Ile Asp Thr Ala Ile Phe 405 410 415 Val Lys Asn Ala Pro Ser Tyr Ala Ala Leu Gly Tyr Gly Gly Glu Gly 420 425 430 Tyr Cys Thr Phe Thr Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser 435 440 445 Ala Arg Thr Phe Thr Lys Ser Arg Arg Cys Val Leu Ala Asp Gly Leu 450 455 460 Ser Ile Arg 465 <210> 338 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Ruminococcus sp. AT10 <400> 338 Val Ser Val Asn Glu Gln Met Val Gln Asp Ile Val Gln Glu Val Leu 1 5 10 15 Ala Lys Met Gln Ile Ala Ser Asp Val Ser Gly Asn Arg Gly Val Phe 20 25 30 Ala Asp Met Asn Glu Ala Ile Ala Ala Ala Gln Lys Ala Gln Lys Val 35 40 45 Val Ala Arg Met Thr Leu Asp His Arg Glu Lys Val Ile Ser Asn Ile 50 55 60 Arg Lys Lys Ile Asn Glu Asn Ala Glu Ile Leu Ala Arg Met Gly Val 65 70 75 80 Glu Glu Thr Gly Met Gly Asn Val Gly His Lys Ile Leu Lys His Gln 85 90 95 Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Val Leu 130 135 140 Cys Asn Thr Ile Gly Met Phe Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Tyr Ala Val Asn Leu Leu 165 170 175 Asn Glu Ala Ser Val Glu Ala Gly Gly Pro Asp Asn Ile Ala Cys Thr 180 185 190 Val Glu His Pro Thr Leu Glu Thr Ser Asn Ile Met Met Lys His Lys 195 200 205 Ala Ile Gln Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Arg Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Glu Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Glu Ser Val Ala Asp Glu Leu Leu His Tyr 275 280 285 Met Ile Gln Glu Gln Gly Cys Tyr Leu Ala Ser Lys Glu Glu Gln Asp 290 295 300 Ala Leu Thr Ala Val Val Leu Lys Asp Gly Arg Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Lys Thr Leu Leu Gly Met Ile Gly Val Thr Val 325 330 335 Pro Asp Asn Ile Arg Cys Ile Thr Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Ala Thr Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Lys Asp Phe Asn Asp Ala Val Glu Gln Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Val Asp His Ile Thr 385 390 395 400 Lys Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Gly Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Phe Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Ser Asp Ser Leu Cys Ile Arg 450 455 460 <210> 339 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Acetobacterium dehalogenans <400> 339 Met Asn Ile Asp Thr Thr Gly Ile Glu Tyr Ile Val Lys Lys Val Met 1 5 10 15 Ala Glu Ile Asp Cys Ala Asp Ala Gly Gly Lys Pro Leu Lys Asp Gly 20 25 30 Glu Leu Gly Val Phe Asn Asp Met Glu Asn Ala Ile Asp Ala Ala Phe 35 40 45 Thr Ala Gln Lys Thr Phe Met Arg Glu Ser Leu Ala Tyr Arg Ser Lys 50 55 60 Leu Ile Ala Ala Met Arg Ala Glu Met Leu Lys Lys Glu Asn Met Glu 65 70 75 80 Met Ile Cys Gln Met Ala Val Glu Glu Thr Gly Met Gly Asn Tyr Glu 85 90 95 His Lys Leu Leu Lys His Glu Leu Ala Thr Val Lys Thr Pro Gly Val 100 105 110 Glu Asp Leu Val Ala Glu Ala Phe Thr Gly Asp Asp Gly Leu Thr Leu 115 120 125 Ile Glu Gln Ser Pro Phe Gly Val Ile Gly Ser Val Ser Pro Ser Thr 130 135 140 Asn Pro Ser Glu Thr Val Ile Cys Asn Ser Ile Gly Met Leu Ala Ala 145 150 155 160 Gly Asn Thr Val Val Phe Ala Pro His Pro Ser Ala Lys Asn Thr Ser 165 170 175 Ala Leu Thr Val Lys Leu Leu Asn Lys Ala Ile Leu Glu Ala Gly Gly 180 185 190 Pro Glu Asn Leu Ile Val Thr Thr Ala Glu Pro Thr Ile Asp Ser Ala 195 200 205 Asn Thr Met Phe Ala Ser Pro Lys Ile Thr Leu Leu Cys Ala Thr Gly 210 215 220 Gly Pro Gly Val Val Lys Thr Val Leu Gln Ser Gly Lys Lys Ala Ile 225 230 235 240 Gly Ala Gly Ala Gly Asn Pro Pro Ala Leu Val Asp Glu Thr Ala Asp 245 250 255 Ile Glu Lys Ala Gly Lys Asp Ile Ile Asp Gly Cys Cys Phe Asp Asn 260 265 270 Asn Leu Pro Cys Ile Ala Glu Lys Glu Val Val Val Val Glu Gln Val 275 280 285 Ala Asp Tyr Leu Ile Phe Asn Met Lys Lys Asn Gly Ala Tyr Glu Leu 290 295 300 Lys Asp Ala Lys Lys Ile Ala Glu Leu Glu Glu Leu Val Ile Pro Gly 305 310 315 320 Gly Arg Leu Ser Arg Asp Tyr Val Gly Arg Ser Ala Lys Val Ile Leu 325 330 335 Lys Gly Ile Gly Ile Asp Val Asp Asp Ser Ile Arg Val Ile Ile Met 340 345 350 Glu Thr Ser Lys Asp His Ile Phe Ala Val Glu Glu Leu Met Met Pro 355 360 365 Ile Leu Pro Ile Val Arg Val Lys Asn Ile Ala Glu Gly Ile Asp Leu 370 375 380 Ala Val Ala Leu Glu His Gly Asn Arg His Thr Ala Ile Met His Ser 385 390 395 400 Thr Asn Ile Asn Asn Leu Thr Glu Met Ala Lys Arg Val Gln Thr Thr 405 410 415 Ile Phe Val Lys Asn Gly Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly 420 425 430 Glu Gly Tyr Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu 435 440 445 Thr Ser Ala Lys Thr Phe Thr Arg Lys Arg Arg Cys Val Leu Val Gly 450 455 460 Gly Phe Thr Ile Lys 465 <210> 340 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Spirochaeta alkalica <400> 340 Ile Ala Thr Leu Leu Glu Arg Ala Arg Ala Ala Gln Glu Lys Ile Ala 1 5 10 15 Thr Cys Thr Gln Arg Glu Ile Asp Asp Leu Cys Leu Ser Val Gly Trp 20 25 30 Glu Val Tyr Thr Asp Glu Asn Ile Ala Lys Leu Ala Glu Cys Ala Val 35 40 45 Gln Thr Thr Gly Met Gly Asn Val Pro Asp Lys Ile Thr Lys His Lys 50 55 60 Val Lys Val Leu Gly Val Leu Lys Asp Leu Arg Lys Ala Arg Thr Val 65 70 75 80 Gly Leu Ile Glu Arg Asp Glu Ala Arg Gly Leu Ser Lys Tyr Ala Lys 85 90 95 Pro Val Gly Val Val Gly Ala Leu Leu Pro Val Thr Asn Pro Thr Ala 100 105 110 Thr Pro Ala Ser Asn Gly Leu Ser Ile Leu Lys Gly Arg Asn Ala Val 115 120 125 Ile Phe Ala Pro His Pro Arg Gly Ala Ala Ala Ser Ala Leu Ala Val 130 135 140 Glu Phe Met Arg Arg Gly Leu Arg Arg Val Gly Ala Pro Glu Asp Leu 145 150 155 160 Ile Gln Ile Val Glu Asp Pro Ser Leu Gly Gln Thr Gly Glu Leu Met 165 170 175 Lys Gln Val Asp Leu Val Val Ala Thr Gly Gly Gly Ala Met Val Lys 180 185 190 Ala Ala Tyr Ser Ser Gly Thr Pro Ala Tyr Gly Val Gly Pro Gly Asn 195 200 205 Ser Val Gln Ile Ile Ala Glu Asp Ala Asp Leu Ala Asp Ala Ala Ala 210 215 220 Lys Ile Ala Leu Ser Lys Ala Phe Asp His Ala Thr Ser Cys Ser Ser 225 230 235 240 Glu Asn Ser Ile Ile Val Glu Asp Ser Val Tyr Glu Gly Met Ile Thr 245 250 255 Glu Leu Val Gln Asn Gln Gly Cys Tyr Leu Thr Thr Pro Arg Glu Arg 260 265 270 Ser Gln Leu Glu Ala Leu Leu Trp Arg Pro Gly Lys Thr Gly Gln Leu 275 280 285 Ala Leu Asn Pro Gly Ile Ile Ala Arg Ser Ala Ala Thr Ile Ala Ala 290 295 300 Glu Ala Gly Ile Thr Leu Pro Glu Gly Thr Arg Val Ile Leu Val Glu 305 310 315 320 Gly Gln His Pro Leu Glu Gln Asp Pro Phe Ser Gln Glu Lys Leu Cys 325 330 335 Pro Val Leu Thr Val Tyr Arg Tyr Thr Arg Trp Glu Glu Ala Val Asp 340 345 350 Leu Leu Val Arg Leu Thr Asp Gln Ala Gly Thr Gly His Ser Cys Gly 355 360 365 Ile His Thr Phe Arg Glu Asp Tyr Ile Arg His Leu Gly Glu Thr Met 370 375 380 Arg Thr Ser Arg Ile Met Val Arg Gln Ala Gln Ala Pro Ala Asn Gly 385 390 395 400 Gly Asn Phe Phe Asn Ala Met Pro Ser Thr Val Thr Leu Gly Cys Gly 405 410 415 Thr Trp Gly Gly Asn Ile Thr Thr Glu Asn Ile His Trp Lys His Phe 420 425 430 Ile Asn Val Thr Trp Val Ser Glu Pro Ile Pro Pro Asp Arg Pro Asp 435 440 445 Asp Glu Glu Ile Trp Gly Ser Phe Trp Ser Arg Tyr Ala Glu 450 455 460 <210> 341 <211> 494 <212> PRT <213> Artificial Sequence <220> <223> Clostridium caminithermale DSM 15212 <400> 341 Met Gln Ile Asn Glu Leu Gln Ile Glu Lys Leu Val Ala Glu Val Leu 1 5 10 15 Ala Lys Thr Leu Gly Ala Glu Gly Asn Ser Ser Leu Val Asn Asn Asn 20 25 30 Ser Ile Gly Asn Ser Asn Glu Tyr Glu Tyr Asn Gln Ser Leu Glu Val 35 40 45 Gly Val Phe Glu Lys Met Glu Asp Ala Ile Asn Glu Ala His Arg Ala 50 55 60 Tyr Gln Gln Leu Lys Asn Tyr Ser Ile Lys Asp Arg Gln Arg Phe Ile 65 70 75 80 Asp Gly Ile Lys Glu Trp Thr Leu Arg Glu Lys Asn Ile Leu Ala Lys 85 90 95 Lys Val Val Glu Glu Thr Gly Leu Gly Asn Tyr Glu Asp Lys Ile Ile 100 105 110 Lys His Glu Leu Ala Ala Arg Thr Ala Gly Thr Glu Val Leu Ser Ser 115 120 125 Lys Val Gln Ser Gly Asp Thr Gly Leu Ala Leu Ile Glu Gln Ala Pro 130 135 140 Tyr Gly Val Val Gly Ala Thr Thr Pro Ser Thr Asn Pro Ser Glu Thr 145 150 155 160 Val Ile Ser Asn Thr Ile Ala Met Leu Ala Ala Gly Asn Thr Val Val 165 170 175 Phe Asn Val His Pro Ser Ser Lys His Val Cys Ala Tyr Thr Val Ala 180 185 190 Lys Ile Asn Glu Cys Ile Met Asp Leu Gly Gly Pro Ala Asn Ile Ile 195 200 205 Thr Met Val Lys Asp Pro Thr Met Glu Ser Leu Gln Val Met Ala Asn 210 215 220 Cys Pro Lys Ile Asn Leu Leu Val Gly Thr Gly Gly Pro Gly Leu Val 225 230 235 240 Arg Ala Leu Leu Lys Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly 245 250 255 Asn Pro Pro Val Val Val Asp Ser Thr Ala Asn Ile Lys Lys Ala Ala 260 265 270 Ala Asp Ile Ile Lys Gly His Ser Phe Asp Asn Asn Ile Val Cys Ile 275 280 285 Leu Glu Lys Glu Val Phe Val Val Asp Glu Val Ala Asn Glu Leu Ile 290 295 300 Glu Asn Met Lys Ser Glu Gly Ala Phe Tyr Leu Asp Ser Ser Tyr Ile 305 310 315 320 Ser Ala Leu Thr Asp Leu Ile Ile Glu Ala Thr Asp Lys Lys Phe Phe 325 330 335 Leu Gly Asn Ser Ser Lys Thr Thr Asn Leu His Thr Lys Lys Glu Trp 340 345 350 Val Gly Lys Asp Ala Tyr Lys Ile Leu Asp Ala Leu Gly Ile Arg Tyr 355 360 365 Ser Thr Arg Pro Lys Cys Ile Ile Cys Glu Val Pro Phe Glu His Pro 370 375 380 Phe Val Gln Leu Glu Leu Leu Met Pro Val Leu Pro Ile Val Arg Val 385 390 395 400 Glu Asn Phe Val Lys Gly Val Glu Tyr Ala Val Glu Ala Glu His Gly 405 410 415 Asn Arg His Thr Ala Ile Val His Ser Gln Asn Ile Asp Asn Ile Thr 420 425 430 Tyr Tyr Ala Lys Ala Ile Asp Thr Thr Ile Phe Val Lys Asn Ala Pro 435 440 445 Ser Val Ala Gly Ile Gly Val Asp Ser Glu Ser Val Val Ser Phe Ser 450 455 460 Ile Ala Gly Pro Thr Gly Glu Gly Ile Thr Thr Ala Lys Asp Phe Thr 465 470 475 480 Arg Ala Arg His Cys Val Leu Val Asp Gly Phe Arg Ile Ile 485 490 <210> 342 <211> 464 <212> PRT <213> Artificial Sequence <220> <223> Caldanaerobius fijiensis <400> 342 Val Val Lys Glu Glu Gln Ile Glu Ala Ile Val Arg Glu Val Leu Arg 1 5 10 15 Arg Ile Asp Arg Glu Asp Ile Lys Leu Asn Glu Asp Lys His Gln Leu 20 25 30 Gly Val Phe Asp Lys Met Glu Asp Ala Ile Glu Ala Ala Lys Asp Ala 35 40 45 Phe Glu Lys Phe Ser Asn Met Thr Leu Glu Asp Arg Glu Arg Phe Ile 50 55 60 Ser Glu Ile Arg Lys Ala Thr Leu Glu Asn Ala Arg Val Leu Ala Glu 65 70 75 80 Met Gly Val Lys Glu Thr Gly Met Gly Lys Val Glu His Lys Val Leu 85 90 95 Lys His Gln Leu Val Ala Lys Lys Thr Pro Gly Thr Glu Asp Leu Lys 100 105 110 Thr Gln Ala Trp Ser Gly Asp Lys Gly Leu Thr Leu Val Glu Met Ala 115 120 125 Pro Phe Gly Val Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro Ser Glu 130 135 140 Thr Ile Ile Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn Ala Val 145 150 155 160 Val Phe Ser Pro His Pro Gly Ala Lys Arg Val Ser Asn Phe Ala Val 165 170 175 Asp Met Ile Asn Arg Ala Ile Ile Arg Ala Gly Gly Pro Glu Asn Leu 180 185 190 Val Val Ser Ile Lys Glu Pro Ser Ile Asn Thr Thr Asn Ala Met Ile 195 200 205 Lys His Pro Asp Val Lys Leu Leu Val Ala Thr Gly Gly Pro Glu Ile 210 215 220 Val Lys Ile Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Lys Lys Ala 245 250 255 Ala Lys Asp Ile Ile Asp Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys 260 265 270 Ile Ala Glu Lys Glu Val Ile Ala Val Glu Lys Ile Tyr Arg Asp Leu 275 280 285 Leu Asp Glu Ile Leu Lys Gln Gly Val Tyr Lys Leu Asn Ala Leu Gln 290 295 300 Ile Ser Lys Leu Glu Asn Leu Val Leu Met Asp Gly Lys Leu Asn Lys 305 310 315 320 Lys Leu Val Gly Lys Asp Ala Lys Val Ile Leu Asp Gln Ile Gly Ile 325 330 335 Asn Val Ser Asp Asp Ile Arg Cys Ile Ile Cys Glu Thr Asp Glu Asp 340 345 350 His Pro Phe Val Met Glu Glu Leu Met Met Pro Ile Leu Pro Ile Val 355 360 365 Lys Ala Lys Asn Ile Asp Asp Ala Ile Arg Ile Ala Val Lys Ala Glu 370 375 380 Lys Asn Asn Arg His Thr Ala His Ile His Ser Lys Asn Ile Asp Asn 385 390 395 400 Ile Thr Arg Tyr Ala Lys Ala Ile Asn Thr Thr Ile Leu Val Lys Asn 405 410 415 Ala Pro Ser Tyr Ala Gly Ile Gly Phe Gly Gly Glu Gly Phe Thr Thr 420 425 430 Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Gln Thr 435 440 445 Phe Thr Arg Met Arg Arg Cys Val Leu Ala Asp Gly Leu Arg Ile Ile 450 455 460 <210> 343 <211> 480 <212> PRT <213> Artificial Sequence <220> <223> Pelosinus fermentans <400> 343 Met Ser Ile Asp Gln Ala Leu Ile Glu Lys Ile Thr Leu Glu Ile Leu 1 5 10 15 Thr Lys Met Gln Thr Gly Ala Lys Ala Ala Pro Ala Gly Tyr Gly Asp 20 25 30 Gly Ile Phe Glu Thr Val Asp Glu Ala Val Ala Ala Ala Arg Lys Ala 35 40 45 Tyr Gln Glu Leu Lys Thr Leu Ser Leu Glu Lys Arg Glu Val Leu Ile 50 55 60 Lys Ala Met Arg Asp Val Ala Tyr Glu Asn Ala Thr Ile Leu Ala Gln 65 70 75 80 Met Ala Val Asp Glu Ser Gly Met Gly Arg Val Ser Asp Lys Ile Ile 85 90 95 Lys Asn Gln Val Ala Ala Leu Lys Thr Pro Gly Thr Glu Asp Leu Thr 100 105 110 Thr Gln Ala Trp Ser Gly Asp Asn Gly Leu Thr Leu Ile Glu Met Gly 115 120 125 Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro Thr Thr Asn Pro Thr Glu 130 135 140 Thr Val Ile Cys Asn Gly Ile Gly Met Ile Ala Ala Gly Asn Thr Val 145 150 155 160 Phe Phe Ser Pro His Pro Thr Ala Lys Asn Thr Ser Met Lys Ile Ile 165 170 175 Thr Leu Leu Asn Gln Ala Ile Val Lys Ala Gly Gly Pro Asn Asn Leu 180 185 190 Leu Thr Ser Val Ala Asn Pro Ser Ile Lys Ala Ala Asn Glu Met Met 195 200 205 Lys His Pro Gly Ile Asn Met Leu Val Ala Thr Gly Gly Pro Gly Val 210 215 220 Val Lys Ala Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Val Ile Val Asp Glu Thr Ala Asp Ile Glu Lys Ala 245 250 255 Ala Arg Asp Ile Val Ala Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys 260 265 270 Ile Ala Glu Lys Glu Val Ile Ala Ile Gly Ser Ile Ala Asp Arg Leu 275 280 285 Ile Thr Tyr Met Gln Lys Tyr Gly Ala Tyr Leu Ile Ser Gly Ser Asn 290 295 300 Ile Asp Arg Leu Leu Asn Val Ile Met Thr Val Gln Glu Glu Lys Ile 305 310 315 320 Ala Glu Gly Cys Thr Asp Lys Pro Lys Arg Ser Tyr Gly Ile Asn Lys 325 330 335 Asp Tyr Val Gly Lys Asp Ala Lys Tyr Leu Leu Ser Lys Ile Gly Ile 340 345 350 Asp Val Pro Asp Ser Val Arg Val Val Leu Cys Glu Thr Pro Ala Asp 355 360 365 His Pro Phe Val Ile Glu Glu Leu Met Met Pro Val Leu Pro Val Val 370 375 380 Gln Val Lys Asp Ile Asp Glu Ala Ile Glu Val Ala Val Arg Val Glu 385 390 395 400 His Gly Asn Arg His Thr Ala Ala Met His Ser Lys Asn Val Asp His 405 410 415 Leu Thr Arg Phe Ala Arg Ala Val Glu Thr Thr Ile Phe Val Lys Asn 420 425 430 Ala Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Phe Thr Ser 435 440 445 Phe Thr Leu Ala Gly Pro Thr Gly Glu Gly Ile Thr Ser Pro Arg Ser 450 455 460 Phe Thr Arg Gln Arg Arg Cys Val Leu Val Asp Ala Phe Ser Ile Val 465 470 475 480 <210> 344 <211> 463 <212> PRT <213> Artificial Sequence <220> <223> Blautia wexlerae <400> 344 Met Pro Val Ser Glu Ser Met Val Gln Glu Ile Val Gln Gln Val Met 1 5 10 15 Ala Lys Met Gln Ile Ala Asp Ala Pro Ala Glu Lys Gln His Gly Val 20 25 30 Phe Lys Asp Met Asn Asp Ala Ile Glu Ala Ala Lys Lys Ser Gln Glu 35 40 45 Ile Val His Lys Met Ser Met Asp Gln Arg Glu Lys Ile Ile Ser Cys 50 55 60 Ile Arg Lys Lys Ile Lys Glu Asn Ala Glu Ile Met Ala Arg Met Gly 65 70 75 80 Val Glu Glu Thr Lys Met Gly Asn Val Gly Asp Lys Ile Leu Lys His 85 90 95 His Leu Val Ala Asp Lys Thr Pro Gly Thr Glu Ala Ile Thr Thr Thr 100 105 110 Ala Trp Ser Gly Asp Arg Gly Leu Thr Leu Val Glu Met Gly Pro Phe 115 120 125 Gly Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Val 130 135 140 Leu Cys Asn Thr Met Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe 145 150 155 160 Asn Pro His Pro Ala Ala Val Lys Thr Ser Leu Tyr Ala Val Asn Leu 165 170 175 Val Asn Glu Ala Ser Leu Glu Gln Gly Gly Pro Asp Asn Ile Ala Val 180 185 190 Ser Val Glu Asn Pro Thr Leu Asp Thr Ser Ser Val Met Met Lys His 195 200 205 Lys Asp Ile His Leu Leu Val Ala Thr Gly Gly Pro Gly Val Val Thr 210 215 220 Ala Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Arg 245 250 255 Asp Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala 260 265 270 Glu Lys Glu Val Val Ala Val Ser Ser Ile Met Asp Glu Leu Met His 275 280 285 Tyr Met Leu Thr Glu Asn Asp Cys Tyr Leu Ala Ser Lys Glu Glu Gln 290 295 300 Asp Lys Leu Val Glu Val Val Leu Ala Gly Gly Lys Leu Asn Arg Lys 305 310 315 320 Cys Val Gly Arg Asp Ala Arg Thr Leu Leu Ser Met Ile Gly Val Asp 325 330 335 Ala Pro Ala Asn Ile Arg Cys Ile Ile Phe Glu Gly Pro Lys Glu His 340 345 350 Pro Leu Ile Thr Thr Glu Leu Met Met Pro Ile Leu Gly Ile Val Arg 355 360 365 Ala Arg Asp Phe Glu Asp Ala Val Glu Gln Ala Val Trp Leu Glu His 370 375 380 Gly Asn Arg His Ser Ala His Ile His Ser Lys Asn Val Asp Arg Ile 385 390 395 400 Thr Thr Tyr Ala Lys Ala Ile Asp Thr Ala Ile Val Val Lys Asn Gly 405 410 415 Pro Ser Tyr Ala Ser Leu Gly Phe Gly Ser Glu Gly Tyr Thr Thr Phe 420 425 430 Thr Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Cys Ala Ser Thr Phe 435 440 445 Thr Lys Arg Arg Arg Cys Ile Met Glu Asp Ser Leu Cys Ile Arg 450 455 460 <210> 345 <211> 500 <212> PRT <213> Artificial Sequence <220> <223> Paenibacillus sp. OSY-SE <400> 345 Ile Lys Leu Thr Glu Thr Asp Ile Gln Asn Ile Ile Gln Gly Val Leu 1 5 10 15 Lys Asn Ile Glu Gln Asn Leu Pro Gly Ala Gln Ala Ala Asp Asp Ala 20 25 30 Ala Thr Gly Gln Ala Lys Pro Glu Ser Ala Pro Val Ala Ala Ala Pro 35 40 45 Val Arg Ser Asn Gly Asp Tyr Gly Val Phe Asp Glu Ala Glu Ala Ala 50 55 60 Ile Ala Ala Ala Tyr Gln Ala Gln Arg Ala Tyr Ala His His Phe Ser 65 70 75 80 Met Gln Asp Arg Glu Arg Phe Ile Ala Ala Ile Arg Lys Ala Thr Leu 85 90 95 Glu His Lys Glu Thr Leu Ala Ser Met Val Leu Lys Glu Thr Lys Leu 100 105 110 Gly Arg Tyr Glu Asp Lys Ile Ala Lys Leu Glu Leu Thr Ala Leu Lys 115 120 125 Thr Pro Gly Thr Glu Asp Leu Glu Thr Lys Ala Phe Ser Gly Asp Asn 130 135 140 Gly Leu Thr Leu Val Lys Asp Gly Pro Phe Gly Val Ile Gly Ala Val 145 150 155 160 Thr Pro Val Thr Asn Ser Val Glu Thr Val Ile Asn Asn Ala Ile Gly 165 170 175 Met Leu Ala Ala Gly Asn Ala Val Val Tyr Asn Val His Pro Ser Ser 180 185 190 Lys Ala Cys Cys Ala Tyr Ala Val Lys Met Ile Asn Arg Ala Val Gln 195 200 205 Glu Ala Gly Gly Pro Glu His Leu Val Thr Met Val Lys Glu Pro Thr 210 215 220 Lys Glu Thr Leu Asp Ala Ile Thr Gln Ser Pro Lys Val Gln Leu Leu 225 230 235 240 Val Gly Thr Gly Gly Pro Gly Leu Val Arg Ala Leu Leu Arg Ser Gly 245 250 255 Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val Asp 260 265 270 Glu Thr Ala Asn Ile Glu Arg Ala Ala Lys Glu Ile Ile Ala Gly Ala 275 280 285 Ser Phe Glu Asn Asn Ile Leu Cys Ile Ala Glu Lys Glu Val Phe Val 290 295 300 Val Asp Lys Val Ala Asp Asp Leu Leu Phe His Met Leu Asn His Gly 305 310 315 320 Ala Tyr Arg Leu Asp Asp Arg Glu Leu Glu Gln Val Met Ser Phe Ala 325 330 335 Leu Glu Ala Asn Val Asn Glu Thr Ala Gly Gly Cys Ser Leu Asp Met 340 345 350 Lys Arg Glu Tyr His Thr Val Lys Glu Trp Ile Gly Lys Asp Ala Ala 355 360 365 Leu Phe Leu Glu Lys Ile Gly Val Thr Pro Glu Lys Glu Val Lys Leu 370 375 380 Leu Ile Cys Glu Val Asp Phe Asp His Pro Phe Val Gln Leu Glu Gln 385 390 395 400 Met Met Pro Val Leu Pro Ile Val Arg Val Ser Asp Leu Asp Glu Ala 405 410 415 Ile Arg Leu Ala Val Glu Ala Glu His Gly Asn Arg His Thr Ala Leu 420 425 430 Met His Ser Thr Asn Val Ala Asn Phe Ala Ala Phe Glu Arg Ala Ile 435 440 445 Gly Thr Thr Ile Phe Val Lys Asn Ala Ser Ser Leu Ala Gly Val Gly 450 455 460 Ala Gly Gly Glu Gly Cys Thr Thr Met Thr Ile Ala Gly Pro Thr Gly 465 470 475 480 Glu Gly Leu Thr Ser Ala Arg Thr Phe Thr Arg Lys Lys Arg Cys Val 485 490 495 Leu Ala Glu Arg 500 <210> 346 <211> 476 <212> PRT <213> Artificial Sequence <220> <223> Spirochaetes bacterium GWC2_52_13 <400> 346 Val Ser Gln Ser Ile Glu Asp Thr Val Arg Thr Leu Val Glu Lys Leu 1 5 10 15 Val Leu Glu Tyr Ser Ala Ser Ser Val Gly Val Asp His Ile Ala Pro 20 25 30 Ser Gln Tyr Ala Ser Gly Ile Phe Pro Thr Met Asp Leu Ala Val Lys 35 40 45 Ala Ala Tyr Glu Ala Gln Arg His Leu Val Gly Leu Pro Leu Glu Lys 50 55 60 Arg Lys Glu Ile Val Gln Ala Met Arg Glu Thr Ala Met Asp His Ala 65 70 75 80 Gln Glu Phe Ala Glu Met Ala Val Gln Glu Ser Gly Arg Gly Asn Val 85 90 95 Ala Asp Lys Ile Ala Lys Asn Ile Leu Ala Ala Lys Lys Thr Pro Gly 100 105 110 Val Glu Asp Val Glu Thr Ser Ala Tyr Ser Asp Glu His Gly Leu Ser 115 120 125 Leu Val Glu Arg Ala Pro Tyr Gly Val Ile Gly Ser Ile Thr Pro Val 130 135 140 Thr Asn Pro Thr Ala Thr Ile Ile Asn Asn Gly Ile Ser Met Ile Ser 145 150 155 160 Gly Gly Asn Ser Val Val Phe Asn Pro His Pro Gly Ala Lys Asn Val 165 170 175 Ser Cys Phe Ala Ile Glu Val Leu Asn Ala Ala Ile Glu Arg Val Gly 180 185 190 Gly Pro Arg Asn Leu Leu Val Ser Leu Ala Gln Pro Thr Ile Glu Ser 195 200 205 Ala Asn Glu Met Met Gly His Gln Lys Ile Ser Leu Leu Val Val Thr 210 215 220 Gly Gly Pro Gly Val Val Lys Ala Ala Met Asn Ser Gly Lys Lys Val 225 230 235 240 Ile Ala Ala Gly Pro Gly Asn Pro Pro Cys Val Val Asp Glu Thr Ala 245 250 255 Lys Ile Gln Lys Ala Ala Lys Asp Ile Val Asp Gly Ala Ser Phe Asp 260 265 270 Asn Asn Leu Val Cys Ile Cys Glu Lys Glu Val Leu Val Val Lys Ser 275 280 285 Val Ala Asn Glu Leu Ile Gly Glu Met Gln Lys Val Gly Ala Tyr Leu 290 295 300 Leu Ser Asp Gln Gln Ala Lys Ser Leu Leu Asp Gln Ile Ile Glu Val 305 310 315 320 Pro Gly Met Met Asn Ser Glu Gly Val Val Lys Arg Glu Tyr Val Gly 325 330 335 Lys Ser Pro Ser Phe Leu Ala Ser Leu Ile Gly Val Thr Val Pro Glu 340 345 350 Ser Thr Arg Leu Leu Ile Cys Asp Val Asp Ala Gly Asn Pro Leu Val 355 360 365 Trp Thr Glu Gln Leu Met Pro Phe Leu Pro Ile Val Arg Met Glu Asn 370 375 380 Val Asp Gln Cys Ile Asp Leu Ala Val Gln Cys Glu His Gly Phe Arg 385 390 395 400 His Thr Ala Ile Met His Ser Leu Asn Val Glu Lys Leu Ser Lys Met 405 410 415 Ala Arg Gln Met Asn Cys Ser Leu Phe Val Lys Asn Gly Pro Cys Tyr 420 425 430 Ala Gly Leu Gly Asn Gly Gly Ala Gly Tyr Thr Ser Phe Thr Ile Ala 435 440 445 Ser Pro Thr Gly Glu Gly Leu Thr Arg Ala Arg Thr Phe Thr Arg Glu 450 455 460 Arg Arg Cys Thr Leu Val Asp Tyr Phe Arg Ile Ile 465 470 475 <210> 347 <211> 454 <212> PRT <213> Artificial Sequence <220> <223> Romboutsia lituseburensis DSM <400> 347 Met Glu Ala Arg Asp Tyr Val Leu Gln Leu Ile Asn Lys Ala Arg Ile 1 5 10 15 Ala Gln Lys Glu Phe Glu Lys Tyr Ser Gln Glu Gln Val Asp Glu Ala 20 25 30 Val Arg Ala Ile Gly Lys Ser Ile Tyr Asp Asn Gly Glu Met Leu Ala 35 40 45 Arg Met Ala Val Asp Glu Thr Lys Met Gly Val Tyr Glu Asp Lys Ile 50 55 60 Val Lys Asn Lys Gly Lys Ser Lys Ala Val Trp Asn Lys Leu Lys Gly 65 70 75 80 Val Lys Ser Arg Gly Ile Ile Lys Tyr Ile Ala Glu Glu Gly Leu Val 85 90 95 Glu Val Ala Lys Pro Ile Gly Val Val Gly Ala Val Thr Pro Thr Thr 100 105 110 Asn Pro Thr Met Thr Pro Met His Asn Ala Met Ile Ala Leu Lys Gly 115 120 125 Gly Asn Ala Ile Ile Ile Cys Pro His Pro Arg Ala Lys Asn Thr Gly 130 135 140 Val Lys Thr Val Asp Leu Met Arg Glu Ala Leu Asp Lys Val Gly Ala 145 150 155 160 Pro Lys Asp Leu Ile Gln Ile Val Asn Glu Pro Thr Val Glu Ile Ser 165 170 175 Asn Leu Val Met Gln Leu Ser Asp Val Cys Val Ser Thr Gly Gly Pro 180 185 190 Gly Met Val Lys Val Ala Tyr Ser Ser Gly Lys Pro Ala Phe Gly Val 195 200 205 Gly Ala Gly Asn Val Gln Cys Leu Ile Asp Lys Asp Ala Asn Leu Glu 210 215 220 Glu Val Val Pro Lys Val Ile Lys Gly Arg Ile Tyr Asp Asn Gly Ile 225 230 235 240 Leu Cys Thr Cys Glu Gln Ser Ala Ile Cys Pro Asp Glu Met Tyr Asn 245 250 255 Glu Phe Ile Asp Arg Leu Val Gln Ser Gly Ala Tyr Tyr Ile Glu Lys 260 265 270 Glu Glu Glu Val Lys Ser Leu Arg Lys Ala Leu Phe Pro Asp Gly Asn 275 280 285 Ile Ser Lys Asp Cys Val Gly Ala Ser Pro Tyr Glu Ile Ala Lys Met 290 295 300 Ala Ser Ile Ala Ile Pro Lys Asp Thr Lys Leu Leu Val Val Lys Val 305 310 315 320 Glu Lys Tyr Gly Thr Glu Glu Tyr Phe Ala Lys Glu Lys Met Cys Pro 325 330 335 Val Leu Ser Ala Tyr Lys Tyr Glu Lys Trp Glu Asp Ala Val Asn Ile 340 345 350 Ala Asn Gln Asn Leu Glu Tyr Glu Gly Lys Gly His Ser Ala Ile Ile 355 360 365 His Ser Tyr Thr Lys Glu Asn Ile Glu Tyr Ala Ala Asn Ile Leu Pro 370 375 380 Val Ser Arg Phe Gly Val Asn Gln Ile Gly Ser Ser Gly Leu Gly Gly 385 390 395 400 Ser Phe Leu Asn Gly Leu Asn Pro Thr Ala Thr Leu Gly Cys Gly Ser 405 410 415 Trp Gly Asn Asn Ser Ile Ser Glu Asn Leu Trp Phe Asn His Leu Ile 420 425 430 Asn Val Ser Lys Ile Ala Tyr Glu Val Pro Ser Lys Lys Ile Pro Thr 435 440 445 Asp Asp Glu Ile Trp Asn 450 <210> 348 <211> 485 <212> PRT <213> Artificial Sequence <220> <223> Clostridium sp. CAG:448 <400> 348 Met Ala Ile Asn Trp Thr Glu Ala Gln Ile Ala Asp Ile Val Ser Lys 1 5 10 15 Val Ile Ala Gly Met Gly Glu Gln Thr Leu Val Asn Asp Lys Glu Trp 20 25 30 Asp Ala Thr Gln Tyr His Gly Arg Lys Leu Ile Gly Ile Phe Glu Thr 35 40 45 Met Glu Glu Ala Ile Asp Ala Ala Ser Ala Gly Tyr Ala Ala Ile Arg 50 55 60 Ala Met Ser Val Ala Gln Arg Glu Thr Leu Ile Ser Ser Ile Arg Thr 65 70 75 80 Tyr Cys Arg Asn Glu Ala Arg Ile Met Ala Glu Leu Gly Val Ala Glu 85 90 95 Thr His Met Gly Arg Val Asp His Lys Thr Ala Lys His Ile Leu Val 100 105 110 Ala Asp Lys Thr Pro Gly Thr Glu Asp Ile Val Ala Glu Ala Lys Thr 115 120 125 Gly Asp Cys Gly Leu Thr Leu Thr Glu Arg Ala Pro Phe Gly Val Val 130 135 140 Gly Ala Ile Thr Pro Ser Thr Asn Pro Ser Glu Thr Val Ile Cys Asn 145 150 155 160 Ser Met Gly Met Ile Ala Ala Gly Asn Gly Val Val Phe Asn Pro His 165 170 175 Pro Gly Ala Ile Ala Thr Ser Asn Tyr Ala Val Asp Leu Val Asn Arg 180 185 190 Ala Val Phe Ala Ala Gly Gly Pro Lys Val Leu Val Ala Ser Val Arg 195 200 205 Lys Pro Thr Met Asp Thr Ala Gln Val Met Tyr Lys His Pro Ala Ile 210 215 220 Arg Leu Leu Val Cys Thr Gly Gly Pro Gly Val Val Lys Ala Val Leu 225 230 235 240 Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val 245 250 255 Ile Val Asp Asp Thr Ala Asp Ile Glu Lys Ala Ala Lys Asp Ile Ile 260 265 270 Asp Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu 275 280 285 Val Phe Val Phe Asp Asn Val Ala Asp Arg Leu Ile Ala Gly Met Leu 290 295 300 Arg Asn Gly Cys Ile Lys Leu Thr Arg Glu Gln Ala Asp Glu Leu Ala 305 310 315 320 Lys Val Val Val Val Glu Lys Thr Asp Ser Lys Thr Gly Lys Val Thr 325 330 335 Arg Ser Val Asn Arg Asp Cys Val Gly Arg Asp Cys Arg Val Ile Leu 340 345 350 Lys Lys Ile Gly Ile Glu Val Gly Pro Glu Ile Arg Cys Ala Ile Ala 355 360 365 Glu Val Pro Phe Glu His Thr Phe Val Gln Thr Glu Leu Met Met Pro 370 375 380 Ile Leu Gly Ile Val Arg Val Lys Asp Ile Asp Glu Ala Ile Asp Leu 385 390 395 400 Ala Val Lys Ala Glu His Gly Asn Arg His Thr Ala His Met His Ser 405 410 415 Lys Asn Ile Asp Asn Leu Ser Arg Phe Ala Lys Ala Ile Glu Thr Thr 420 425 430 Ile Phe Val Lys Asn Ala Pro Ser Tyr Ala Gly Ile Gly Phe Gly Gly 435 440 445 Glu Gly His Thr Thr Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Ile 450 455 460 Thr Ser Ala Lys Ser Tyr Thr Arg Leu Arg Arg Cys Val Met Ala Asp 465 470 475 480 His Phe Arg Ile Ile 485 <210> 349 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Yersinia bercovieri ATCC 43970 <400> 349 Met Asn Thr Asn Asp Leu Glu Ser Leu Ile Arg Thr Ile Leu Thr Glu 1 5 10 15 Gln Leu Thr Pro Ala Thr Ala Ser Ala Ser Asn Ala Ile Phe Ala Ser 20 25 30 Val Asp Glu Ala Val Asn Ala Ala His Ser Ala Phe Leu Arg Tyr Gln 35 40 45 Gln Ser Pro Met Lys Thr Arg Ser Ala Ile Ile Ser Ala Leu Arg Gln 50 55 60 Gln Leu Lys Pro Gln Leu Ala Ser Leu Ser Glu Arg Gly Ala Ser Glu 65 70 75 80 Thr Gly Met Gly Asn Lys Glu Asp Lys Phe Leu Lys Asn Lys Ala Ala 85 90 95 Leu Glu Asn Thr Pro Gly Ile Glu Asp Leu Ser Thr Thr Ala Leu Thr 100 105 110 Gly Asp Gly Gly Met Val Leu Phe Glu Tyr Ser Pro Phe Gly Val Ile 115 120 125 Gly Ser Val Ala Pro Ser Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn 130 135 140 Ser Ile Ser Met Leu Ala Ala Gly Asn Ala Val Tyr Phe Ser Pro His 145 150 155 160 Pro Gly Ala Lys Ala Val Ser Leu Asp Leu Ile Ala Gln Ile Glu Ala 165 170 175 Ile Ile Phe Asn Ser Cys Gly Ile Arg Asn Leu Val Val Thr Val Gln 180 185 190 Glu Pro Ser Phe Glu Ala Thr Gln Gln Met Met Ala His Asp Lys Ile 195 200 205 Ala Leu Leu Ala Ile Thr Gly Gly Pro Ala Ile Val Ala Met Gly Met 210 215 220 Lys Ser Gly Lys Lys Val Ile Gly Ala Gly Ala Gly Asn Pro Pro Cys 225 230 235 240 Leu Val Asp Glu Thr Ala Glu Leu Ala Lys Ala Ala Gln Asp Ile Val 245 250 255 Ser Gly Ala Ser Phe Asp Tyr Asn Leu Pro Cys Ile Ala Glu Lys Ser 260 265 270 Leu Ile Val Val Glu Ser Val Ala Asp Arg Leu Leu Gln Gln Met Gln 275 280 285 Ala Phe Asp Ala Leu Leu Ile Ser Asn Pro Gln Asp Val Asp Ser Leu 290 295 300 Arg Lys Ala Cys Leu Thr Pro Gln Gly His Ala Asn Lys Asn Leu Val 305 310 315 320 Gly Lys Ser Pro Leu Glu Leu Leu Lys Ala Ala Gly Leu Thr Cys Pro 325 330 335 Ala Lys Ala Pro Arg Leu Leu Leu Val Glu Val Ala Gly Asp Asp Pro 340 345 350 Leu Val Thr Thr Glu Gln Leu Met Pro Leu Leu Pro Val Val Arg Val 355 360 365 Lys Asp Phe Asp Ala Ala Leu Thr Leu Ala Leu Gln Val Glu Gly Gly 370 375 380 Leu His His Thr Ala Thr Met His Ser Gln Asn Val Ser Arg Leu Asn 385 390 395 400 Leu Ala Ala Arg Leu Leu Gln Thr Ser Ile Phe Val Lys Asn Gly Pro 405 410 415 Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Phe Thr Thr Phe Thr 420 425 430 Ile Ala Thr Pro Thr Gly Glu Gly Thr Thr Ser Ala Arg Thr Phe Ala 435 440 445 Arg Gln Arg Arg Cys Val Leu Thr Asn Gly Phe Ser Ile Arg 450 455 460 <210> 350 <211> 511 <212> PRT <213> Artificial Sequence <220> <223> Proteocatella sphenisci <400> 350 Val Asp Ile Gly Gln Lys Asp Ile Glu Leu Ile Val Gln Gln Val Leu 1 5 10 15 Lys Asn Val Val Ser Gln Ser Ala Ala Ala Gln Ser Asn Ser Gln Pro 20 25 30 Glu Val Lys Thr Tyr Arg Pro Gly Val Pro Val Gln Glu Phe Ser Met 35 40 45 Lys Ser Gln Tyr Ala Pro Ser Ser Pro Tyr Pro Ser Ser Ser Gln Ser 50 55 60 Ser Ala Gly Asp Tyr Gly Val Phe Glu Thr Met Asp Gln Ala Val Glu 65 70 75 80 Ala Ala Tyr Gln Ala Gln Lys Ile Tyr Gln Ala Lys Phe Gln Leu Lys 85 90 95 Asp Arg Glu Arg Leu Ile Lys Ser Ile Arg Glu Thr Gly Met Lys Asn 100 105 110 Val Glu Lys Leu Ala Arg Met Ser Val Asp Glu Thr Gly Leu Gly Arg 115 120 125 Tyr Glu Asp Lys Ile Leu Lys Asn Thr Leu Val Leu Glu Arg Thr Pro 130 135 140 Gly Thr Glu Cys Leu Lys Thr Glu Ala Ile Ser Gly Asp Asp Gly Leu 145 150 155 160 Thr Ile Ile Glu His Ala Pro Tyr Gly Val Ile Gly Ser Ile Thr Pro 165 170 175 Val Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn Val Ile Ser Met Ile 180 185 190 Ala Gly Gly Asn Ser Val Val Phe Asn Val His Pro Ser Ala Lys Glu 195 200 205 Ser Cys Arg Phe Ala Val Gln Met Ile Asn Lys Ala Ile Glu Glu Val 210 215 220 Gly Gly Pro Lys Asn Leu Val Ser Met Val Lys Gln Pro Thr Leu Asp 225 230 235 240 Thr Val Ser Gln Leu Ser Lys Asn Asp Lys Val Arg Leu Met Ala Gly 245 250 255 Thr Gly Gly Met Pro Met Val Arg Ser Leu Leu Gln Ser Gly Lys Lys 260 265 270 Val Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val Asp Glu Thr 275 280 285 Ala Asp Ile Lys Arg Ala Ala Ala Glu Ile Phe Lys Gly Ala Ser Phe 290 295 300 Asp Asn Asn Val Leu Cys Leu Ala Glu Lys Glu Val Phe Ile Val Glu 305 310 315 320 Ser Val Ala Thr Asp Phe Val Tyr Asn Met Ile Gln Glu Gly Ala Phe 325 330 335 Leu Leu Asn Glu Ser Gln Leu Glu Lys Ile Met Asn Leu Val Leu Thr 340 345 350 Tyr Glu Glu Thr Pro Asn Gly Arg Glu Tyr His Thr Ser Lys Asn Trp 355 360 365 Val Gly Lys Asp Ala Gly Lys Met Leu Asp Ala Ile Gly Ile Asn Gly 370 375 380 Lys Ser Asp Cys Arg Leu Leu Ile Cys Glu Val Gly Pro Asn His Pro 385 390 395 400 Phe Val Leu Leu Glu Gln Leu Met Pro Val Leu Pro Ile Val Lys Cys 405 410 415 Lys Asn Leu Asp Glu Ala Ile Lys Phe Ala Met Ile Ala Glu His Gly 420 425 430 Asn Arg His Thr Ala Ser Met Phe Ser Gln Ser Ile Asn Asn Leu Thr 435 440 445 Arg Phe Ala Arg Glu Val Glu Thr Thr Ile Phe Val Lys Asn Ala Ala 450 455 460 Thr Leu Ala Gly Val Gly Phe Gly Gly Glu Gly His Thr Thr Met Thr 465 470 475 480 Ile Ala Gly Pro Thr Gly Glu Gly Ile Thr Asn Ala Val Ser Phe Thr 485 490 495 Arg Gln Arg Arg Cys Ala Leu Ser Glu Gly Gly Phe Arg Ile Ile 500 505 510 <210> 351 <211> 480 <212> PRT <213> Artificial Sequence <220> <223> Pelosinus propionicus DSM <400> 351 Met Ser Ile Asp Gln Ala Leu Ile Glu Lys Ile Thr Leu Glu Ile Leu 1 5 10 15 Ser Lys Met Gln Thr Gly Ala Lys Ala Ala Pro Thr Gly Tyr Gly Ser 20 25 30 Gly Ile Phe Glu Thr Val Asp Glu Ala Val Ala Ala Ala Arg Lys Ala 35 40 45 Tyr Gln Glu Leu Lys Thr Leu Ser Leu Glu Lys Arg Glu Val Leu Ile 50 55 60 Lys Ala Met Arg Asp Val Ala Tyr Glu Asn Ala Thr Ile Leu Ala Gln 65 70 75 80 Met Ala Val Asp Glu Ser Gly Met Gly Arg Val Ser Asp Lys Ile Ile 85 90 95 Lys Asn Gln Val Ala Ala Leu Lys Thr Pro Gly Thr Glu Asp Leu Thr 100 105 110 Thr Gln Ala Trp Ser Gly Asp Asn Gly Leu Thr Leu Ile Glu Met Gly 115 120 125 Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro Thr Thr Asn Pro Thr Glu 130 135 140 Thr Val Ile Cys Asn Gly Ile Gly Met Ile Ala Ala Gly Asn Thr Val 145 150 155 160 Phe Phe Ser Pro His Pro Thr Ala Lys Asn Thr Ser Ile Lys Ile Ile 165 170 175 Thr Leu Leu Asn Asp Ala Ile Val Lys Ala Gly Gly Pro Asn Asn Leu 180 185 190 Leu Thr Ser Val Ala Asn Pro Ser Ile Lys Ala Ala Asn Glu Met Met 195 200 205 Lys His Pro Gly Ile Asn Met Leu Val Ala Thr Gly Gly Pro Gly Val 210 215 220 Val Lys Ala Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala 225 230 235 240 Gly Asn Pro Pro Val Ile Val Asp Glu Thr Ala Asp Ile Glu Lys Ala 245 250 255 Ala Arg Asp Ile Val Ala Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys 260 265 270 Ile Ala Glu Lys Glu Val Ile Ala Val Gly Ser Ile Ala Asp Arg Leu 275 280 285 Ile Thr Tyr Met Gln Lys Tyr Gly Ala Tyr Leu Ile Ser Gly Ser Asn 290 295 300 Ile Asp Arg Leu Leu Asp Val Ile Met Thr Val Gln Glu Glu Lys Ile 305 310 315 320 Ala Glu Gly Cys Thr Asp Lys Pro Lys Arg Ser Tyr Gly Ile Asn Lys 325 330 335 Asp Tyr Val Gly Lys Asp Ala Lys Tyr Leu Leu Ser Lys Ile Gly Ile 340 345 350 Asp Val Pro Asp Ser Val Lys Val Val Leu Cys Glu Thr Pro Ala Asp 355 360 365 His Pro Phe Val Ile Glu Glu Leu Met Met Pro Val Leu Pro Val Val 370 375 380 Gln Val Lys Asp Ile Asp Glu Ala Ile Glu Val Ala Val Arg Val Glu 385 390 395 400 His Gly Asn Arg His Thr Ala Ala Met His Ser Lys Asn Val Asp His 405 410 415 Leu Thr Arg Phe Ala Arg Ala Val Glu Thr Thr Ile Phe Val Lys Asn 420 425 430 Ala Pro Ser Tyr Ala Gly Ile Gly Val Gly Gly Glu Gly Phe Thr Ser 435 440 445 Phe Thr Leu Ala Gly Pro Thr Gly Glu Gly Ile Thr Ser Pro Arg Ser 450 455 460 Phe Thr Arg Gln Arg Arg Cys Val Leu Val Asp Ala Phe Ser Ile Val 465 470 475 480 <210> 352 <211> 457 <212> PRT <213> Artificial Sequence <220> <223> Clostridium sp. KLE <400> 352 Met Val Gln Asp Ile Val Lys Glu Val Val Ala Arg Met Gln Leu Ser 1 5 10 15 Gly Thr Ala Gln Ser Ala Gln His Gly Val Phe Asn Asp Met Asn Gln 20 25 30 Ala Ile Glu Ala Ala Lys Glu Ala Glu Lys Thr Val Arg Arg Met Thr 35 40 45 Met Asp Gln Arg Glu Gln Ile Val Ser Asn Ile Arg Lys Lys Thr His 50 55 60 Glu Ala Ala Glu Ile Leu Ala Arg Met Gly Val Glu Glu Thr Gly Met 65 70 75 80 Gly Asn Val Gly Asp Lys Ile Leu Lys His His Leu Leu Ala Asp Lys 85 90 95 Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala Trp Ser Gly Asp Arg 100 105 110 Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly Val Ile Gly Ala Ile 115 120 125 Thr Pro Cys Thr Asn Pro Ser Glu Thr Val Leu Cys Asn Ser Ile Gly 130 135 140 Met Ile Ala Ala Gly Asn Thr Val Val Phe Asn Pro His Pro Gln Ala 145 150 155 160 Ile Arg Thr Ser Ile Phe Ala Ile Asn Leu Val Asn Glu Ala Ser Leu 165 170 175 Glu Ala Gly Gly Pro Asp Asn Val Ala Cys Thr Val Phe Lys Pro Thr 180 185 190 Leu Glu Thr Ser Asn Ile Met Met Lys His Lys Asp Ile Pro Leu Ile 195 200 205 Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala Val Leu Ser Ser Gly 210 215 220 Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro Pro Ala Leu Val Asp 225 230 235 240 Glu Thr Ala Asp Ile Arg Lys Ala Ala Ala Asp Ile Val Asn Gly Cys 245 250 255 Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu Lys Glu Ile Val Ala 260 265 270 Val Asp Ser Ile Ala Asp Glu Leu Met Asn Tyr Met Ile Ser Glu Gln 275 280 285 Gly Cys Tyr Leu Ile Ser Lys Glu Glu Gln Asp Lys Leu Thr Ala Thr 290 295 300 Val Leu Thr Pro Lys Gly Leu Asn Arg Lys Cys Val Gly Arg Asp Ala 305 310 315 320 Arg Thr Leu Leu Ser Met Ile Gly Ile Gln Ala Pro Glu Asn Ile Arg 325 330 335 Cys Ile Val Phe Glu Gly Glu Lys Glu His Pro Leu Ile Ser Glu Glu 340 345 350 Leu Met Met Pro Ile Leu Gly Leu Val Arg Ala Lys Asp Phe Asp Asp 355 360 365 Ala Val Glu Lys Ala Val Trp Leu Glu His Gly Asn Arg His Ser Ala 370 375 380 His Ile His Ser Lys Asn Ile Asp Asn Ile Thr Lys Tyr Ala Arg Ala 385 390 395 400 Ile Asp Thr Ala Ile Leu Val Lys Asn Ala Pro Ser Tyr Ala Ala Leu 405 410 415 Gly Phe Gly Gly Glu Gly Phe Cys Thr Phe Thr Ile Ala Ser Arg Thr 420 425 430 Gly Glu Gly Leu Thr Ser Thr Ser Thr Phe Thr Lys Arg Arg Arg Cys 435 440 445 Val Met Ser Asp Ser Leu Cys Ile Arg 450 455 <210> 353 <211> 527 <212> PRT <213> Artificial Sequence <220> <223> Caldalkalibacillus thermarum TA2.A1 <400> 353 Met Asn Met Thr Glu Lys Asp Ile Glu Lys Ile Val Gln Ser Val Leu 1 5 10 15 His Asn Val Glu Ser Ala Leu Gly Lys Ser Ala Ser Ala Ser Pro Ser 20 25 30 Val Ser Ala Val Ser Val Ala Ser Gly Glu Gly Ile Lys Pro Val Gln 35 40 45 Phe Lys Gln Val Pro Val Phe Gln Gln Glu Thr Val Lys Ser Pro Asn 50 55 60 Arg Asn Arg Asn Leu Gly Gly Ala Glu Glu Lys Trp Gly Val Phe Asn 65 70 75 80 His Met Glu Asp Ala Ile Glu Ala Ser Tyr Arg Ala Gln Met Glu Phe 85 90 95 Val Lys His Phe Gln Leu Lys Asp Arg Glu Lys Ile Ile Thr Ala Ile 100 105 110 Arg Glu Ala Val Leu Arg Glu Lys Glu Val Leu Ala Arg Lys Val Tyr 115 120 125 Glu Glu Thr Lys Ile Gly Arg Tyr Glu Asp Lys Val Ala Lys His Glu 130 135 140 Leu Ala Ala Leu Lys Thr Pro Gly Thr Glu Asp Leu Lys Thr Glu Ala 145 150 155 160 Phe Ser Gly Asp Asn Gly Leu Thr Ile Val Glu Arg Ala Pro Tyr Gly 165 170 175 Leu Ile Gly Ala Val Thr Pro Val Thr Asn Pro Thr Glu Thr Ile Ile 180 185 190 Asn Asn Ala Ile Gly Met Leu Ala Ala Gly Asn Ala Val Val Phe Asn 195 200 205 Val His Pro Ser Ser Lys Arg Ser Cys Ala Tyr Ala Val Gln Leu Ile 210 215 220 Asn Lys Ala Ile Thr Glu Ala Gly Gly Pro His His Leu Val Thr Met 225 230 235 240 Val Lys Glu Pro Thr Leu Asp Thr Leu Gln Thr Leu Ile Asp Ser Pro 245 250 255 Lys Val Lys Leu Leu Val Gly Thr Gly Gly Pro Gly Leu Val Gln Thr 260 265 270 Leu Leu Lys Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro 275 280 285 Pro Val Ile Val Asp Asp Thr Ala Asp Leu Glu His Ala Ala Arg Ser 290 295 300 Ile Ile Glu Gly Ala Ala Phe Asp Asn Asn Leu Leu Cys Ile Ala Glu 305 310 315 320 Lys Glu Val Phe Val Leu Glu Ser Val Ala Asp Asp Leu Ile Phe His 325 330 335 Met Leu Asn His Gly Ala Tyr Met Leu Gly Gln His Glu Val Glu Gln 340 345 350 Val Met Ala Phe Ala Leu Glu Glu Gln Gly Asn Glu Gln Asn Arg Gly 355 360 365 Cys Gly Phe Asn Pro Gln Arg His Tyr Gln Val Ser Lys Asp Trp Ile 370 375 380 Gly Gln Asp Ala Arg Leu Phe Leu Glu His Ile Gly Val Gln Pro Pro 385 390 395 400 Thr Glu Val Lys Leu Leu Ile Cys Asp Val Glu Phe Asp His Pro Phe 405 410 415 Val Gln Leu Glu Gln Met Met Pro Val Leu Pro Ile Val Arg Val Lys 420 425 430 Thr Leu Asp Glu Ala Ile Glu Lys Ala Val Met Ala Glu His Gly Asn 435 440 445 Arg His Thr Ala Ile Met His Ser Lys Asn Val Asp His Leu Thr Lys 450 455 460 Phe Ala Arg Ala Ile Gln Thr Thr Leu Phe Val Lys Asn Ala Ser Ser 465 470 475 480 Leu Ala Gly Val Gly Tyr Gly Gly Glu Gly His Thr Thr Met Thr Ile 485 490 495 Ala Gly Pro Thr Gly Glu Gly Val Thr Ser Ala Lys Thr Phe Thr Arg 500 505 510 Glu Arg Arg Cys Val Leu Ala Glu Gly Gly Phe Arg Ile Ile Gly 515 520 525 <210> 354 <211> 476 <212> PRT <213> Artificial Sequence <220> <223> Caldalkalibacillus thermarum TA2.A1 <400> 354 Val Pro Val Phe Gln Gln Glu Thr Val Lys Ser Pro Asn Arg Asn Arg 1 5 10 15 Asn Leu Gly Gly Ala Glu Glu Lys Trp Gly Val Phe Asn His Met Glu 20 25 30 Asp Ala Ile Glu Ala Ser Tyr Arg Ala Gln Met Glu Phe Val Lys His 35 40 45 Phe Gln Leu Lys Asp Arg Glu Lys Ile Ile Thr Ala Ile Arg Glu Ala 50 55 60 Val Leu Arg Glu Lys Glu Val Leu Ala Arg Lys Val Tyr Glu Glu Thr 65 70 75 80 Lys Ile Gly Arg Tyr Glu Asp Lys Val Ala Lys His Glu Leu Ala Ala 85 90 95 Leu Lys Thr Pro Gly Thr Glu Asp Leu Lys Thr Glu Ala Phe Ser Gly 100 105 110 Asp Asn Gly Leu Thr Ile Val Glu Arg Ala Pro Tyr Gly Leu Ile Gly 115 120 125 Ala Val Thr Pro Val Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn Ala 130 135 140 Ile Gly Met Leu Ala Ala Gly Asn Ala Val Val Phe Asn Val His Pro 145 150 155 160 Ser Ser Lys Arg Ser Cys Ala Tyr Ala Val Gln Leu Ile Asn Lys Ala 165 170 175 Ile Thr Glu Ala Gly Gly Pro His His Leu Val Thr Met Val Lys Glu 180 185 190 Pro Thr Leu Asp Thr Leu Gln Thr Leu Ile Asp Ser Pro Lys Val Lys 195 200 205 Leu Leu Val Gly Thr Gly Gly Pro Gly Leu Val Gln Thr Leu Leu Lys 210 215 220 Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile 225 230 235 240 Val Asp Asp Thr Ala Asp Leu Glu His Ala Ala Arg Ser Ile Ile Glu 245 250 255 Gly Ala Ala Phe Asp Asn Asn Leu Leu Cys Ile Ala Glu Lys Glu Val 260 265 270 Phe Val Leu Glu Ser Val Ala Asp Asp Leu Ile Phe His Met Leu Asn 275 280 285 His Gly Ala Tyr Met Leu Gly Gln His Glu Val Glu Gln Val Met Ala 290 295 300 Phe Ala Leu Glu Glu Gln Gly Asn Glu Gln Asn Arg Gly Cys Gly Phe 305 310 315 320 Asn Pro Gln Arg His Tyr Gln Val Ser Lys Asp Trp Ile Gly Gln Asp 325 330 335 Ala Arg Leu Phe Leu Glu His Ile Gly Val Gln Pro Pro Thr Glu Val 340 345 350 Lys Leu Leu Ile Cys Asp Val Glu Phe Asp His Pro Phe Val Gln Leu 355 360 365 Glu Gln Met Met Pro Val Leu Pro Ile Val Arg Val Lys Thr Leu Asp 370 375 380 Glu Ala Ile Glu Lys Ala Val Met Ala Glu His Gly Asn Arg His Thr 385 390 395 400 Ala Ile Met His Ser Lys Asn Val Asp His Leu Thr Lys Phe Ala Arg 405 410 415 Ala Ile Gln Thr Thr Leu Phe Val Lys Asn Ala Ser Ser Leu Ala Gly 420 425 430 Val Gly Tyr Gly Gly Glu Gly His Thr Thr Met Thr Ile Ala Gly Pro 435 440 445 Thr Gly Glu Gly Val Thr Ser Ala Lys Thr Phe Thr Arg Glu Arg Arg 450 455 460 Cys Val Leu Ala Glu Gly Gly Phe Arg Ile Ile Gly 465 470 475 <210> 355 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Blautia sp. CAG:257 <400> 355 Met Pro Ile Ser Glu Asn Met Val Gln Glu Ile Val Gln Glu Val Met 1 5 10 15 Ala Lys Met Gln Ile Ala Glu Ala Pro Ala Gly Lys His Gly Ile Phe 20 25 30 Lys Asp Met Asn Asp Ala Ile Glu Ala Ala Lys Lys Ala Glu Leu Ile 35 40 45 Val Lys Arg Met Ser Met Asp Gln Arg Glu Lys Ile Ile Thr Cys Ile 50 55 60 Arg Lys Lys Ile Lys Glu Asn Ala Glu Val Leu Ala Arg Met Gly Val 65 70 75 80 Glu Glu Thr Gly Met Gly Asn Val Gly Asp Lys Ile Leu Lys His His 85 90 95 Leu Val Ala Asp Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Ile Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Val Leu 130 135 140 Cys Asn Thr Met Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Tyr Ala Ile Asn Leu Leu 165 170 175 Asn Glu Ala Ser Leu Glu Ser Gly Gly Pro Asp Asn Ile Ala Val Thr 180 185 190 Val Glu Lys Pro Thr Leu Glu Thr Ser Asp Ile Met Met Lys His Lys 195 200 205 Asp Ile His Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Gln Asp 245 250 255 Ile Val Asn Gly Cys Thr Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Ser Ser Ile Ala Asp Glu Leu Met His Tyr 275 280 285 Leu Ile Thr Glu Asn Asp Cys Tyr Leu Ala Ser Lys Glu Glu Gln Asp 290 295 300 Lys Leu Thr Glu Val Val Leu Ala Gly Gly Lys Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Arg Thr Leu Leu Ser Met Ile Gly Val Asp Ala 325 330 335 Pro Ala Asn Ile Arg Cys Ile Val Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Ala Glu Glu Leu Met Met Pro Ile Leu Gly Met Val Arg Ala 355 360 365 Arg Asp Phe Asp Asp Ala Val Glu Gln Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Val Asp Asn Ile Thr 385 390 395 400 Lys Tyr Ala Arg Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Gly Pro 405 410 415 Ser Tyr Ser Ala Leu Gly Phe Gly Gly Glu Gly Phe Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Ser Asp Ser Leu Cys Ile Arg 450 455 460 <210> 356 <211> 469 <212> PRT <213> Artificial Sequence <220> <223> Listeria marthii FSL <400> 356 Met Glu Ser Leu Glu Leu Glu Gln Leu Val Lys Lys Val Leu Leu Glu 1 5 10 15 Lys Leu Ala Glu Gln Lys Glu Ala Pro Ala Lys Pro Ile Thr Gln Gly 20 25 30 Ala Lys Ser Gly Ile Phe Asp Thr Val Asp Glu Ala Val Gln Ala Ala 35 40 45 Val Ile Ala Gln Asn Cys Tyr Lys Glu Lys Ser Leu Glu Glu Arg Arg 50 55 60 Asn Val Val Lys Ala Ile Arg Glu Thr Leu Tyr Pro Glu Ile Glu Thr 65 70 75 80 Ile Ala Thr Lys Ala Val Ala Glu Thr Gly Met Gly Asn Val Ala Asp 85 90 95 Lys Ile Leu Lys Asn Thr Leu Ala Ile Glu Lys Thr Pro Gly Val Glu 100 105 110 Asp Leu Tyr Thr Glu Val Ala Thr Gly Asp Asn Gly Met Thr Leu Tyr 115 120 125 Glu Leu Ser Pro Tyr Gly Val Ile Gly Ala Val Ala Pro Ser Thr Asn 130 135 140 Pro Thr Glu Thr Leu Ile Cys Asn Thr Ile Gly Met Leu Ala Ala Gly 145 150 155 160 Asn Ala Val Phe Tyr Ser Pro His Pro Gly Ala Lys Asn Ile Ser Leu 165 170 175 Trp Leu Ile Glu Lys Leu Asn Thr Ile Val Arg Glu Ser Cys Gly Ile 180 185 190 Asp Asn Leu Val Val Thr Val Glu Lys Pro Ser Ile Gln Ala Ala Gln 195 200 205 Glu Met Met Asn His Pro Lys Val Pro Leu Leu Val Ile Thr Gly Gly 210 215 220 Pro Gly Val Val Leu Gln Ala Met Gln Ser Gly Lys Lys Val Ile Gly 225 230 235 240 Ala Gly Ala Gly Asn Pro Pro Ser Ile Val Asp Glu Thr Ala Asn Ile 245 250 255 Glu Lys Ala Ala Ala Asp Ile Val Asp Gly Ala Ser Phe Asp His Asn 260 265 270 Ile Leu Cys Ile Ala Glu Lys Ser Ile Val Ala Val Glu Ser Ile Ala 275 280 285 Asp Phe Leu Leu Phe Gln Met Glu Lys Asn Gly Ala Leu His Val Thr 290 295 300 Asn Pro Ser Asp Ile Gln Lys Leu Glu Lys Val Ala Val Thr Asp Lys 305 310 315 320 Gly Val Thr Asn Lys Lys Leu Val Gly Lys Ser Ala Ala Glu Ile Leu 325 330 335 Lys Glu Ala Gly Ile Thr Cys Asp Phe Thr Pro Arg Leu Ile Ile Val 340 345 350 Glu Thr Thr Lys Thr His Pro Phe Ala Thr Val Glu Leu Leu Met Pro 355 360 365 Ile Val Pro Leu Val Arg Val Pro Asp Phe Asp Glu Ala Leu Glu Val 370 375 380 Ala Ile Glu Leu Glu Gln Gly Leu His His Thr Ala Thr Met His Ser 385 390 395 400 Gln Asn Ile Ser Arg Leu Asn Lys Ala Ala Arg Asp Met Gln Thr Ser 405 410 415 Ile Phe Val Lys Asn Gly Pro Ser Phe Ala Gly Leu Gly Phe Arg Gly 420 425 430 Glu Gly Ser Thr Thr Phe Thr Ile Ala Thr Pro Thr Gly Glu Gly Thr 435 440 445 Thr Thr Ala Arg His Phe Ala Arg Arg Arg Arg Cys Val Leu Thr Asp 450 455 460 Gly Phe Ser Ile Arg 465 <210> 357 <211> 473 <212> PRT <213> Artificial Sequence <220> <223> Clostridium methoxybenzovorans <400> 357 Met Glu Ile Gly Ala Lys Glu Ile Glu Leu Ile Val Arg Glu Val Leu 1 5 10 15 Ala Gly Ile Glu Ser Arg Gly Ile Lys Pro Ser Tyr Thr Pro Ser Arg 20 25 30 Ser Glu Asp Gly Val Phe Glu Arg Val Glu Asp Ala Ile Glu Ala Ala 35 40 45 Tyr Ala Ala Gln Arg Glu Trp Val Glu His Tyr Arg Val Glu Asp Arg 50 55 60 Arg Arg Ile Ile Glu Ala Ile Arg Val Thr Ala Lys Ser His Ala Glu 65 70 75 80 Ser Leu Ala Lys Met Val Trp Glu Glu Thr Gly Met Gly Arg Phe Glu 85 90 95 Asp Lys Ile Gln Lys His Met Ala Val Ile Glu Lys Thr Pro Gly Val 100 105 110 Glu Cys Leu Thr Thr Glu Ala Ile Ser Gly Asp Gly Gly Leu Met Ile 115 120 125 Glu Glu Tyr Ala Pro Phe Gly Val Ile Gly Ala Ile Thr Pro Ser Thr 130 135 140 Asn Pro Thr Glu Thr Ile Ile Asn Asn Thr Ile Ser Met Ile Ala Gly 145 150 155 160 Gly Asn Ser Val Val Phe Asn Val His Pro Gly Ala Lys Arg Cys Cys 165 170 175 Ala His Cys Leu Lys Ile Leu His Gln Ala Ile Val Glu Asn Gly Gly 180 185 190 Pro Ala Ser Leu Ile Thr Met Gln Lys Glu Pro Asp Met Glu Ala Val 195 200 205 Ser Lys Leu Thr Ser Asp Pro Arg Ile Arg Leu Met Val Gly Thr Gly 210 215 220 Gly Met Pro Met Val Asn Ala Leu Leu Arg Ser Gly Lys Lys Thr Ile 225 230 235 240 Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val Asp Asp Thr Ala Asp 245 250 255 Val Ser Leu Ala Ala Arg Glu Ile Tyr Arg Gly Ala Ser Phe Asp Asn 260 265 270 Asn Ile Leu Cys Leu Ala Glu Lys Glu Val Phe Val Met Glu Arg Ala 275 280 285 Ala Asp Glu Leu Val Asn Lys Leu Ile Lys Glu Gly Ala Tyr Leu Leu 290 295 300 Ser Ser Met Glu Leu Ser Glu Ile Leu Lys Phe Ala Met Val Glu Lys 305 310 315 320 Asn Gly Ser Tyr Glu Val Asn Lys Lys Trp Val Gly Lys Asp Ala Gly 325 330 335 Gln Phe Leu Glu Ala Ile Gly Val Ser Gly His Lys Asp Val Arg Leu 340 345 350 Leu Ile Cys Glu Thr Asp Arg Ser His Pro Phe Val Met Val Glu Gln 355 360 365 Leu Met Pro Ile Leu Pro Ile Val Arg Leu Arg Thr Phe Glu Glu Cys 370 375 380 Val Glu Ser Ala Leu Ala Ala Glu Ser Gly Asn Arg His Thr Ala Ser 385 390 395 400 Met Phe Ser Arg Asn Val Glu Asn Met Thr Lys Phe Gly Lys Ile Ile 405 410 415 Glu Thr Thr Ile Phe Thr Lys Asn Gly Ser Thr Leu Lys Gly Val Gly 420 425 430 Ile Gly Gly Glu Gly His Thr Thr Met Thr Ile Ala Gly Pro Thr Gly 435 440 445 Glu Gly Leu Thr Cys Ala Arg Ser Phe Thr Arg Arg Arg Arg Cys Met 450 455 460 Leu Ala Glu Gly Gly Leu Arg Ile Ile 465 470 <210> 358 <211> 477 <212> PRT <213> Artificial Sequence <220> <223> Bacillus sp. m3-13 <400> 358 Val Gln Ile Lys Glu Ser Asp Ile Lys Glu Met Val Ala Gln Val Leu 1 5 10 15 Ala Gln Leu Gly Asp Glu Ser Lys Gln Pro Ser Pro Ala Ser Glu Gln 20 25 30 Gly Ser Asn Glu Val Pro Leu Gly Asn Gly Val Phe Thr Thr Val Asp 35 40 45 Gln Ala Thr Glu Ala Ala Thr Glu Ala Trp Asp Lys Leu Arg Ala Thr 50 55 60 Ser Leu Glu Thr Arg Lys Asn Met Ile Glu Lys Met Arg Glu Val Ser 65 70 75 80 Arg Glu His Ala Lys Ala Leu Ala Glu Leu Ala Val Lys Glu Thr Gly 85 90 95 Leu Gly Arg Val Glu Asp Lys Val Ala Lys Asn Leu Leu Ala Ala Asp 100 105 110 Lys Thr Pro Gly Val Glu Asp Ile Val Ala Thr Thr Tyr Ser Gly Asp 115 120 125 Gly Gly Leu Thr Leu Val Glu Tyr Ser Pro Val Gly Val Tyr Gly Ala 130 135 140 Ile Thr Pro Ser Thr Asn Pro Ala Ala Thr Ile Ile Asn Asn Ser Ile 145 150 155 160 Ser Leu Val Ala Ala Gly Asn Ala Val Val Phe Asn Pro His Pro Ser 165 170 175 Ala Lys Gln Val Ser Ile Lys Thr Met Gln Leu Leu Asn Glu Ala Ile 180 185 190 Val Ala Ala Gly Gly Pro Ala Asn Thr Leu Thr Ser Val Ala Ser Pro 195 200 205 Asn Ile Glu Thr Ser Asn Glu Val Met Lys His Pro Lys Val Arg Ala 210 215 220 Leu Val Val Thr Gly Gly Gly Ile Val Val Gln Ala Ala Met Ser Ala 225 230 235 240 Gly Lys Lys Val Ile Ala Ala Gly Pro Gly Asn Pro Pro Val Val Val 245 250 255 Asp Glu Thr Ala Ile Ile Ser Lys Ala Ala Lys Asp Ile Val Thr Gly 260 265 270 Ala Ser Phe Asp Asn Asn Val Leu Cys Thr Ala Glu Lys Glu Val Phe 275 280 285 Val Val Glu Lys Val Ala Asn Thr Leu Lys Ser Glu Met Thr Lys Asn 290 295 300 Gly Ala Val Glu Leu Lys Gly Tyr Gln Leu Glu Lys Leu Leu Gly Lys 305 310 315 320 Ile Leu Val Lys Lys Gly Glu Lys Tyr Tyr Pro Asn Arg Asp Phe Ile 325 330 335 Gly Lys Asp Ala Ser Val Leu Leu Glu Ala Ala Gly Ile Arg Ser Asp 340 345 350 Ser Asn Val Lys Leu Ile Ile Ala Glu Thr Lys Glu Asp His Pro Leu 355 360 365 Val His Thr Glu Met Leu Met Pro Ile Leu Pro Ile Val Arg Val Ser 370 375 380 Asp Val Asp Lys Ala Ile Ser Leu Ala Val Lys Ala Glu Lys Gly Asn 385 390 395 400 Arg His Thr Ala Ile Met His Ser Gln Asn Val Thr Asn Leu Thr Lys 405 410 415 Met Ala Lys Glu Ile Gln Ala Thr Ile Phe Val Lys Asn Gly Pro Ser 420 425 430 Val Ala Gly Leu Gly Tyr Gln Ser Glu Gly Phe Thr Thr Leu Thr Ile 435 440 445 Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys Thr Phe Thr Arg 450 455 460 Gln Arg Arg Cys Val Leu Val Asp Gly Phe Arg Ile Ile 465 470 475 <210> 359 <211> 472 <212> PRT <213> Artificial Sequence <220> <223> bacterium CG2_30_54_10 <400> 359 Met Ser Val Ser Lys Asp Glu Ile Asn Val Ile Val Gln Glu Val Leu 1 5 10 15 Lys Ala Ile Glu Thr Ser Gly Gly Leu Pro Ser Ala Ala Ser Ser Val 20 25 30 Gly Arg Ile Ser Gln Lys Gly Val Phe Glu Asn Leu Asp Asp Ala Ile 35 40 45 Lys Ala Ala Gly Gln Ala Gln Lys Lys Leu Val Glu Leu Pro Leu Lys 50 55 60 Thr Arg Gly Glu Ile Ile Ala Asn Met Arg Arg Arg Ala Ala Glu Asn 65 70 75 80 Val Glu Glu Ile Ser Arg Leu Gly His Glu Glu Thr Gly Tyr Gly Arg 85 90 95 Ile Ala Asp Lys Ile Gln Lys Asn Met Leu Ala Ile Thr Lys Thr Pro 100 105 110 Gly Ile Glu Asp Leu Gln Pro Val Ala Tyr Ser Gly Asp His Gly Leu 115 120 125 Thr Ile Val Glu Gln Ala Pro Tyr Gly Val Ile Gly Ala Ile Thr Pro 130 135 140 Ser Thr Asn Pro Ser Glu Thr Val Ile Cys Asn Ser Ile Gly Met Ile 145 150 155 160 Ala Ala Gly Asn Ala Val Val Phe Gly Pro His Pro Ser Ala Ala Gln 165 170 175 Val Cys Leu Leu Ala Ile Ser Val Leu Asn Asp Ala Val Val Glu Ala 180 185 190 Gly Gly Pro Glu Asn Leu Met Val Ser Val Ser Lys Pro Ser Ile Gln 195 200 205 Thr Ala Gln Ala Leu Met Ala His Pro Asp Ile Arg Leu Leu Val Val 210 215 220 Thr Gly Gly Pro Ala Val Val Ala Ala Ala Ala Lys Ser Gly Lys Lys 225 230 235 240 Phe Ile Ala Ala Gly Pro Gly Asn Pro Pro Ala Val Val Asp Glu Thr 245 250 255 Ala Asp Leu Lys Lys Ala Ala Arg Asp Ile Ile Ser Gly Ala Thr Leu 260 265 270 Asp Asn Asn Ile Leu Cys Ile Ala Glu Lys Glu Ile Ile Val Val Glu 275 280 285 Ser Val Ala Asp Glu Leu Lys Arg His Leu Cys Asn Ser Gly Ala Tyr 290 295 300 Glu Ala Ser Ala Arg Glu Ile Leu Gln Leu Glu Lys Leu Val Ile Asp 305 310 315 320 Pro Arg Thr His Gly Pro Asn Arg Ser Phe Ile Gly Lys Asn Ala Ser 325 330 335 Val Ile Leu Asp Ala Ile Gly Val Lys Val Ser Asp Glu Val Arg Met 340 345 350 Val Leu Cys Glu Val Gly Pro Asp His Pro Phe Val Val Glu Glu Met 355 360 365 Met Met Pro Val Val Pro Leu Val Arg Val Arg Asp Val His Thr Ala 370 375 380 Val Asp Phe Ala Val Lys Ile Glu His Gly Cys Arg His Thr Ala Ile 385 390 395 400 Met His Ser Lys Asn Leu Asp Asn Leu His Leu Met Ala Thr Arg Cys 405 410 415 Asn Cys Ser Ile Phe Val Lys Asn Gly Pro Ser Tyr Ala Gly Leu Gly 420 425 430 Leu Gly Gly Glu Gly Phe Thr Thr Phe Thr Ile Ala Ser Pro Thr Gly 435 440 445 Glu Gly Leu Thr Ser Ala Arg Thr Phe Thr Arg Gln Arg Arg Cys Val 450 455 460 Leu Val Asp Tyr Phe Arg Ile Val 465 470 <210> 360 <211> 475 <212> PRT <213> Artificial Sequence <220> <223> Candidatus Izimaplasma sp. <400> 360 Met Ser Thr Asn Asp Leu Ile Lys Gln Leu Thr Glu Glu Met Glu Arg 1 5 10 15 Lys Tyr Gly Asn Asp Val Val Thr Lys Pro Asn Thr Pro Thr Asn Ser 20 25 30 Tyr Asn Thr Gly Tyr Val Gly Ile Phe Glu Asn Val Glu Asp Ala Ile 35 40 45 Leu Ala Ala Lys Glu Ser Gln Lys Gln Leu Met Glu Leu Ser Met Lys 50 55 60 Lys Arg Lys Glu Ile Ile Glu Ala Met Arg Lys Ala Ser Leu Glu Asn 65 70 75 80 Ala Glu Lys Leu Ala Ile Met Ala His Glu Glu Thr Gly Phe Gly Arg 85 90 95 Val Ala Asp Lys Ile Ile Lys Asn Val Leu Ala Ala Glu Lys Thr Pro 100 105 110 Gly Thr Glu Asp Leu Ser Ser Ser Thr Phe Thr Gly Asp Asp Gly Met 115 120 125 Thr Leu Val Glu Leu Ala Pro Tyr Gly Val Ile Gly Ser Ile Thr Pro 130 135 140 Ser Thr Asn Pro Ser Ser Thr Ile Ile Asn Asn Ser Ile Ser Met Val 145 150 155 160 Ala Ala Gly Asn Gly Val Val Tyr Asn Pro His Pro Ser Ala Lys Lys 165 170 175 Val Thr Ser Glu Thr Ile Ser Ile Leu Asn Lys Ala Ile Ser Ser Val 180 185 190 Gly Gly Pro Arg Glu Leu Leu Thr Ala Pro Leu Thr Pro Thr Met Asp 195 200 205 Thr Ser Lys Val Ile Met Thr His Lys Asp Val Arg Ile Leu Val Val 210 215 220 Thr Gly Gly Glu Ala Val Val Gly Val Ala Met Lys Ser Gly Lys Lys 225 230 235 240 Val Ile Ala Ala Gly Pro Gly Asn Pro Pro Val Ile Val Asp Glu Thr 245 250 255 Ala Asn Ile Lys Lys Ala Ala Asn Asp Val Phe Arg Gly Ala Ser Phe 260 265 270 Asp Asn Asn Ile Leu Cys Ile Ala Glu Lys Glu Ala Phe Val Ile Asn 275 280 285 Ser Val Ile Asn Glu Phe Lys Gln Glu Met Val Ser Asn Gly Ala Tyr 290 295 300 Glu Leu Lys Arg His Glu Ile Asp Leu Val Thr Glu Glu Val Phe Thr 305 310 315 320 Lys Asn Lys Asn Gly Asp Thr Val Val Asn Arg Lys His Val Gly Lys 325 330 335 Ser Ala Val Glu Ile Leu Lys Ala Cys Asn Ile Met Val His Gln Asp 340 345 350 Ile Arg Leu Ile Thr Ala Glu Val Ser Glu Asn His Pro Phe Ile Thr 355 360 365 Val Glu Met Leu Met Pro Val Leu Gly Ile Val Arg Val Tyr Ser Ile 370 375 380 Asp Glu Ala Ile Glu Lys Ala Val Ile Ala Glu Asp Gly Cys Leu His 385 390 395 400 Thr Ala Ile Met His Ser Glu Ser Val Ser Asn Leu Thr Lys Ala Ala 405 410 415 Arg Ala Leu Asn Thr Ser Ile Phe Val Lys Asn Ala Pro Ser Phe Ala 420 425 430 Gly Leu Gly Ile Glu Gly Glu Gly Phe Thr Thr Leu Thr Ile Ala Thr 435 440 445 Pro Thr Gly Glu Gly Leu Thr Ser Ala Arg Ser Phe Thr Arg Ile Arg 450 455 460 Arg Cys Thr Leu Ser Gly Gly Phe Arg Ile Val 465 470 475 <210> 361 <211> 462 <212> PRT <213> Artificial Sequence <220> <223> Firmicutes bacterium CAG:41 <400> 361 Val Pro Ile Asn Glu Asn Met Val Gln Asp Ile Val Gln Glu Val Leu 1 5 10 15 Ala Lys Met Gln Ile Gln Glu Ala Pro Thr Gly Lys His Gly Val Phe 20 25 30 Lys Asp Met Asn Glu Ala Ile Glu Ala Ala Lys Lys Ala Gln Gln Thr 35 40 45 Val Lys Lys Met Ser Met Asp Gln Arg Glu Lys Ile Leu Ser Ile Ile 50 55 60 Arg Lys Lys Ile Cys Glu Asn Ala Glu Thr Met Ala Arg Met Gly Val 65 70 75 80 Glu Glu Thr Gly Met Gly Asn Val Gly Asp Lys Ile Leu Lys His Arg 85 90 95 Leu Val Ala Glu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr Thr Ala 100 105 110 Trp Ser Gly Asp Arg Gly Leu Thr Leu Val Glu Met Gly Pro Phe Gly 115 120 125 Val Ile Gly Ala Ile Thr Pro Cys Thr Asn Pro Ser Glu Thr Val Leu 130 135 140 Cys Asn Thr Met Gly Met Leu Ala Gly Gly Asn Thr Val Val Phe Asn 145 150 155 160 Pro His Pro Ala Ala Ile Lys Thr Ser Ile Phe Ala Ile Asn Leu Leu 165 170 175 Asn Glu Ala Ser Leu Glu Gly Gly Gly Pro Asp Asn Ile Ala Cys Thr 180 185 190 Val Glu Asn Pro Thr Leu Glu Thr Ser Asn Ile Met Met Lys His Lys 195 200 205 Asp Ile Pro Leu Ile Ala Ala Thr Gly Gly Pro Gly Val Val Thr Ala 210 215 220 Val Leu Ser Ser Gly Lys Arg Gly Ile Gly Ala Gly Ala Gly Asn Pro 225 230 235 240 Pro Ala Leu Val Asp Glu Thr Ala Asp Ile Arg Lys Ala Ala Gln Asp 245 250 255 Ile Val Asn Gly Cys Val Phe Asp Asn Asn Leu Pro Cys Ile Ala Glu 260 265 270 Lys Glu Ile Val Ala Val Ser Ser Val Val Asp Glu Leu Met His Tyr 275 280 285 Met Val Thr Glu Gln Gly Cys Tyr Leu Ala Ser Lys Glu Glu Gln Asp 290 295 300 Ala Leu Thr Ala Val Val Leu Ala Gly Gly Arg Leu Asn Arg Lys Cys 305 310 315 320 Val Gly Arg Asp Ala Arg Thr Leu Leu Ser Met Ile Gly Val Asp Ala 325 330 335 Pro Ala Asn Ile Arg Cys Ile Thr Phe Glu Gly Pro Lys Glu His Pro 340 345 350 Leu Ile Ala Glu Glu Leu Met Met Pro Ile Leu Gly Val Val Arg Ala 355 360 365 Lys Asp Phe Glu Asp Ala Val Glu Gln Ala Val Trp Leu Glu His Gly 370 375 380 Asn Arg His Ser Ala His Ile His Ser Lys Asn Ile Asp Asn Ile Thr 385 390 395 400 Thr Tyr Ala Lys Ala Ile Asp Thr Ala Ile Leu Val Lys Asn Ala Pro 405 410 415 Ser Tyr Ala Ala Leu Gly Phe Gly Gly Glu Gly Tyr Cys Thr Phe Thr 420 425 430 Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser Ala Ser Thr Phe Thr 435 440 445 Lys Arg Arg Arg Cys Val Met Ser Asp Ser Leu Cys Ile Arg 450 455 460 <210> 362 <211> 467 <212> PRT <213> Artificial Sequence <220> <223> Thermoanaerobacterium xylanolyticum LX-11 <400> 362 Met Lys Val Lys Glu Glu Asp Ile Glu Ala Ile Val Lys Lys Val Leu 1 5 10 15 Ser Glu Phe Asn Leu Glu Lys Thr Thr Ser Lys Tyr Gly Asp Val Gly 20 25 30 Ile Phe Gln Asp Met Asn Asp Ala Ile Ser Ala Ala Lys Asp Ala Gln 35 40 45 Lys Lys Leu Arg Asn Met Pro Met Glu Ser Arg Glu Lys Ile Ile Gln 50 55 60 Asn Ile Arg Lys Lys Ile Met Glu Asn Lys Lys Ile Leu Ala Glu Met 65 70 75 80 Gly Val Arg Glu Thr Gly Met Gly Arg Val Glu His Lys Ile Val Lys 85 90 95 His Glu Leu Val Ala Leu Lys Thr Pro Gly Thr Glu Asp Ile Thr Thr 100 105 110 Thr Ala Trp Ser Gly Asp Lys Gly Leu Thr Leu Val Glu Met Gly Pro 115 120 125 Phe Gly Val Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro Ser Glu Thr 130 135 140 Val Leu Cys Asn Ser Ile Gly Met Ile Ala Ala Gly Asn Ser Val Val 145 150 155 160 Phe Asn Pro His Pro Gly Ala Val Asn Val Ser Asn Tyr Ala Val Lys 165 170 175 Leu Val Asn Glu Ala Ala Met Glu Ala Gly Gly Pro Glu Asn Leu Val 180 185 190 Val Ser Val Glu Lys Pro Thr Leu Glu Thr Gly Asn Val Met Phe Lys 195 200 205 Ser Ser Asp Val Ser Leu Leu Val Ala Thr Gly Gly Pro Gly Val Val 210 215 220 Thr Ala Val Leu Ser Ser Gly Lys Arg Ala Ile Gly Ala Gly Ala Gly 225 230 235 240 Asn Pro Pro Val Val Val Asp Glu Thr Ala Asp Ile Lys Lys Ala Ala 245 250 255 Lys Asp Ile Ile Asp Gly Ala Thr Phe Asp Asn Asn Leu Pro Cys Ile 260 265 270 Ala Glu Lys Glu Val Val Ser Val Asp Lys Ile Thr Asp Glu Leu Ile 275 280 285 Tyr Tyr Met Gln Lys Asn Gly Cys Tyr Lys Ile Glu Gly Arg Glu Ile 290 295 300 Glu Lys Leu Ile Glu Leu Val Leu Asp His Glu Gly Gly Lys Thr Thr 305 310 315 320 Leu Asn Arg Lys Trp Val Gly Lys Asp Ala His Leu Ile Leu Lys Ala 325 330 335 Ile Gly Ile Asp Ala Asp Glu Ser Val Arg Cys Ile Ile Phe Glu Ala 340 345 350 Glu Lys Asp Asn Pro Leu Val Val Glu Glu Leu Met Met Pro Ile Leu 355 360 365 Gly Ile Val Arg Ala Lys Asn Val Asp Glu Ala Ile Met Ile Ala Thr 370 375 380 Glu Leu Glu His Gly Asn Arg His Ser Ala His Met His Ser Lys Asn 385 390 395 400 Ile Asp Asn Leu Thr Lys Phe Gly Lys Ile Ile Asp Thr Ala Ile Phe 405 410 415 Val Lys Asn Ala Pro Ser Tyr Ala Ala Leu Gly Tyr Gly Gly Glu Gly 420 425 430 Tyr Cys Thr Phe Thr Ile Ala Ser Arg Thr Gly Glu Gly Leu Thr Ser 435 440 445 Ala Arg Thr Phe Thr Lys Ser Arg Arg Cys Val Leu Ala Asp Gly Leu 450 455 460 Ser Ile Arg 465 <210> 363 <211> 441 <212> PRT <213> Artificial Sequence <220> <223> Listeria monocytogenes <400> 363 Met Thr Lys Gly Ala Lys Ser Gly Val Phe Asp Thr Val Asp Glu Ala 1 5 10 15 Val Gln Ala Ala Val Ile Ala Gln Asn Ser Tyr Lys Glu Lys Ser Leu 20 25 30 Glu Glu Arg Arg Asn Val Val Lys Ala Ile Arg Glu Ala Leu Tyr Pro 35 40 45 Glu Ile Glu Ser Ile Ala Ala Arg Ala Val Ala Glu Thr Gly Met Gly 50 55 60 Asn Val Ala Asp Lys Ile Leu Lys Asn Thr Leu Ala Ile Glu Lys Thr 65 70 75 80 Pro Gly Val Glu Asp Leu Tyr Thr Glu Val Ala Thr Gly Asp Asn Gly 85 90 95 Met Thr Leu Tyr Glu Leu Ser Pro Tyr Gly Val Ile Gly Ala Val Ala 100 105 110 Pro Ser Thr Asn Pro Thr Glu Thr Leu Ile Cys Asn Thr Ile Gly Met 115 120 125 Leu Ala Ala Gly Asn Ala Val Phe Tyr Ser Pro His Pro Gly Ala Lys 130 135 140 Asn Ile Ser Leu Trp Leu Ile Glu Lys Leu Asn Thr Ile Val Arg Glu 145 150 155 160 Ser Cys Gly Val Asp Asn Leu Val Val Thr Val Glu Lys Pro Ser Ile 165 170 175 Gln Ala Ala Gln Glu Met Met Asn His Pro Lys Val Pro Leu Leu Val 180 185 190 Ile Thr Gly Gly Pro Gly Val Val Leu Gln Ala Met Gln Ser Gly Lys 195 200 205 Lys Val Ile Gly Ala Gly Ala Gly Asn Pro Pro Ser Ile Val Asp Glu 210 215 220 Thr Ala Asn Ile Glu Lys Ala Ala Ala Asp Ile Val Asp Gly Ala Ser 225 230 235 240 Phe Asp His Asn Ile Leu Cys Ile Ala Glu Lys Ser Val Val Ala Val 245 250 255 Asp Ser Ile Ala Asp Phe Leu Met Phe Gln Met Glu Lys Asn Gly Ala 260 265 270 Leu His Val Thr Asn Pro Ser Asp Ile Gln Lys Leu Glu Lys Val Ala 275 280 285 Val Thr Asp Lys Gly Val Thr Asn Lys Lys Leu Val Gly Lys Ser Ala 290 295 300 Ser Glu Ile Leu Lys Glu Ala Gly Ile Ala Cys Asp Phe Ser Pro Arg 305 310 315 320 Leu Ile Ile Val Glu Thr Glu Lys Thr His Pro Phe Ala Thr Val Glu 325 330 335 Leu Leu Met Pro Ile Val Pro Val Val Arg Val Pro Asn Phe Glu Glu 340 345 350 Ala Leu Glu Val Ala Ile Glu Leu Glu Gln Gly Leu His His Thr Ala 355 360 365 Thr Met His Ser Gln Asn Ile Ser Arg Leu Asn Lys Ala Ala Arg Asp 370 375 380 Met Gln Thr Ser Ile Phe Val Lys Asn Gly Pro Ser Phe Ala Gly Leu 385 390 395 400 Gly Phe Arg Gly Glu Gly Ser Thr Thr Phe Thr Ile Ala Thr Pro Thr 405 410 415 Gly Glu Gly Thr Thr Thr Ala Arg His Phe Ala Arg Arg Arg Arg Cys 420 425 430 Val Leu Thr Asp Gly Phe Ser Ile Arg 435 440 <210> 364 <211> 481 <212> PRT <213> Artificial Sequence <220> <223> Clostridium lavalense <400> 364 Met Glu Ile Glu Thr Arg Asp Ile Glu Arg Ile Val Arg Gln Val Met 1 5 10 15 Ala Val Met Glu Gln Gln Gly Thr Ile Ala Gly Gly Ala Tyr Pro Pro 20 25 30 Ala Pro Gly Thr Pro Ala Pro Arg Gly Asp Asn Gly Val Phe Glu Arg 35 40 45 Val Glu Asp Ala Ile Asp Ala Ala Tyr Ala Ala Gly Arg Glu Trp Ala 50 55 60 Phe His Tyr Lys Val Glu Asp Arg Arg Arg Val Ile Glu Ala Ile Arg 65 70 75 80 Val Met Ala Arg Glu Asn Ala Arg Thr Leu Ala Gln Met Val Arg Asp 85 90 95 Glu Thr Gly Met Gly Arg Met Glu Asp Lys Val Glu Lys His Leu Ala 100 105 110 Val Ala Asp Lys Thr Pro Gly Val Glu Cys Leu Thr Thr Asp Ala Ile 115 120 125 Ser Gly Asp Gly Gly Leu Met Ile Glu Glu Tyr Ala Pro Phe Gly Val 130 135 140 Ile Gly Ala Ile Thr Pro Ser Thr Asn Pro Thr Glu Thr Val Ile His 145 150 155 160 Asn Thr Ile Ser Met Ile Ala Gly Gly Asn Ser Val Val Phe Asn Val 165 170 175 His Pro Gly Ala Lys Lys Cys Cys Ala Phe Cys Leu Gln Leu Leu His 180 185 190 Lys Thr Ile Val Glu Asn Gly Gly Pro Ala Asn Leu Ile Thr Met Gln 195 200 205 Arg Glu Pro Thr Met Asp Ala Val Asn Lys Met Thr Ser Ser Pro Lys 210 215 220 Ile Arg Leu Met Val Gly Thr Gly Gly Met Gly Met Val Asn Ala Leu 225 230 235 240 Leu Arg Ser Gly Lys Lys Thr Ile Gly Ala Gly Ala Gly Asn Pro Pro 245 250 255 Val Ile Val Asp Asp Thr Ala Asp Val Lys Leu Ala Ala Arg Glu Leu 260 265 270 Tyr Trp Gly Ala Ser Phe Asp Asn Asn Leu Phe Cys Phe Ala Glu Lys 275 280 285 Glu Val Phe Val Met Glu Ala Ser Ala Asp Gly Leu Ile Arg Gly Leu 290 295 300 Val Glu Gln Gly Ala Tyr Leu Leu Thr Pro Ala Glu Thr Glu Ala Ile 305 310 315 320 Val Lys Leu Ala Leu Ile Gln Lys Asp Gly Lys Tyr Glu Val Asn Lys 325 330 335 Lys Trp Val Gly Lys Asp Ala Gly Leu Phe Leu Lys Ala Ile Gly Val 340 345 350 Ser Gly His Glu Asn Thr Arg Leu Leu Ile Cys Asp Val Pro Lys Cys 355 360 365 His Pro Tyr Val Met Val Glu Gln Leu Met Pro Val Leu Pro Ile Val 370 375 380 Arg Cys Arg Thr Phe Asp Glu Cys Ile Gln Cys Ser Val Glu Ala Glu 385 390 395 400 Gln Gly Asn Arg His Thr Ser Ser Ile Phe Ser Thr Asn Val Tyr Asn 405 410 415 Met Thr Lys Phe Gly Lys Glu Ile Glu Thr Thr Ile Tyr Val Lys Asn 420 425 430 Gly Ala Thr Leu Arg Gly Leu Gly Ile Gly Gly Glu Gly His Thr Thr 435 440 445 Met Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Cys Ala Arg Ser 450 455 460 Phe Thr Arg Arg Arg Arg Cys Met Leu Ala Glu Gly Gly Leu Arg Ile 465 470 475 480 Ile <210> 365 <211> 474 <212> PRT <213> Artificial Sequence <220> <223> Acetanaerobacterium elongatum <400> 365 Met Glu Phe Ala Val Asn Glu Ile Ser Met Ile Val Glu Gln Val Leu 1 5 10 15 Lys Asn Leu Asp Leu Ser Lys Val Ser Ala Gly Asn Ala Pro Ala Ser 20 25 30 Pro Lys Gly Asp Tyr Gly Val Phe Glu Asn Val Glu Asp Ala Ile Glu 35 40 45 Ala Ala Tyr Gln Ala Gln Lys Ile Tyr Leu Asp Lys Phe Gln Val Lys 50 55 60 Asp Arg Gln Arg Ile Ile Ala Ala Ile Arg Lys Val Cys Arg Glu Asn 65 70 75 80 Ala Glu Thr Leu Ala Arg Met Val Arg Glu Glu Ser Lys Met Gly Arg 85 90 95 Tyr Glu Asp Lys Ile Gln Lys His Leu Ala Val Ile Asp Asn Thr Pro 100 105 110 Gly Pro Glu Cys Leu Thr Thr Asp Ala Ile Ser Gly Asp Ser Gly Leu 115 120 125 Met Leu Glu Glu Tyr Ala Pro Phe Gly Leu Ile Gly Ala Ile Thr Pro 130 135 140 Val Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn Thr Ile Ser Met Ile 145 150 155 160 Ser Gly Gly Asn Ser Val Val Phe Asn Val His Pro Ser Ala Lys Asn 165 170 175 Val Cys Ala Tyr Cys Leu Arg Leu Ile Asn Lys Thr Ile Ile Asp Asn 180 185 190 Gly Gly Pro Ala Asn Leu Ile Thr Met Ala Lys Glu Pro Thr Met Asp 195 200 205 Thr Val Lys Ala Ile Ser Ser Ser Pro Lys Val Arg Leu Met Val Gly 210 215 220 Thr Gly Gly Met Pro Met Val Asn Ala Leu Leu Arg Ser Gly Lys Lys 225 230 235 240 Val Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile Val Asp Asn Thr 245 250 255 Ala Asp Ile Lys Lys Ala Ala Lys Asp Ile Tyr Tyr Gly Ala Ser Phe 260 265 270 Asp Asn Asn Leu Leu Cys Leu Ala Glu Lys Glu Val Phe Val Leu Asp 275 280 285 Glu Val Ala Asn Gln Phe Ile Tyr Asn Met Val Glu Glu Gly Ala Tyr 290 295 300 Leu Leu Asn Gly Val Gln Leu Glu Lys Ile Leu Asn Leu Val Phe Lys 305 310 315 320 Phe Asp Gly Lys Tyr Asp Val Asn Lys Lys Trp Val Gly Gln Asp Ala 325 330 335 Gly Lys Met Leu Asp Ala Ile Gly Val Glu Gly Lys Ser Asp Thr Arg 340 345 350 Leu Leu Ile Cys Glu Val Pro His Asp His Pro Phe Val Met Val Glu 355 360 365 Gln Leu Met Pro Val Leu Pro Ile Val Arg Cys Arg Asn Leu Asp Glu 370 375 380 Ala Ile Glu Tyr Ala Tyr Ile Ala Glu Ser Gly Asn Arg His Thr Ala 385 390 395 400 Ser Met Phe Ser Lys Asn Val Asp Asn Met Thr Arg Phe Ala Arg Lys 405 410 415 Ile Glu Thr Thr Ile Phe Val Lys Asn Gly Pro Thr Leu Asn Gly Val 420 425 430 Gly Ile Gly Gly Glu Gly Tyr Ala Thr Met Thr Ile Ala Gly Pro Thr 435 440 445 Gly Glu Gly Leu Thr Cys Ala Lys Ser Phe Thr Arg Arg Arg Arg Cys 450 455 460 Met Leu Ser Asp Gly Gly Leu Arg Val Ile 465 470 <210> 366 <211> 464 <212> PRT <213> Artificial Sequence <220> <223> Alkaliphilus peptidifermentans DSM <400> 366 Met Val Glu Glu Leu Lys Ile Glu Glu Ile Ile Arg Arg Val Met Lys 1 5 10 15 Glu Ile Ser Ser Lys Asn Glu Thr Gly Glu Glu Gly Ala Tyr Gly Ile 20 25 30 Phe Gln Asp Met Asn Asp Ala Val Asp Ala Ala Tyr Ile Ala Gln Lys 35 40 45 Glu Leu Ile Gly Phe Asn Leu Glu Thr Arg Gly Lys Phe Ile Glu Ala 50 55 60 Met Arg Gln Ala Ala Arg Gln Asn Val Glu Leu Leu Ser Lys Met Ala 65 70 75 80 His Glu Glu Thr Asp Met Gly Arg Tyr Glu Asp Lys Ile Leu Lys Asn 85 90 95 Arg Leu Ala Ile Glu Lys Thr Pro Gly Ile Glu Asp Leu Gly Ser Glu 100 105 110 Val Phe Thr Gly Asp Asp Gly Leu Thr Leu Ile Glu Leu Ser Pro Tyr 115 120 125 Gly Val Ile Gly Ser Ile Ser Pro Val Thr Asn Pro Ser Glu Thr Ile 130 135 140 Ile Cys Asn Ala Ile Gly Met Ile Ala Ala Gly Asn Ala Val Ala Phe 145 150 155 160 Ser Pro His Pro Ser Ala Lys Lys Thr Ser Leu Lys Thr Ile Glu Ile 165 170 175 Leu Asn Lys Gly Ile Ile Glu Ala Gly Gly Pro Lys Asn Leu Ile Val 180 185 190 Ala Val Glu Asn Pro Ser Ile Glu Gln Ala Glu Ala Met Met Lys His 195 200 205 Lys Lys Ile Asn Met Leu Val Ala Thr Gly Gly Pro Gly Val Val Lys 210 215 220 Ser Val Leu Ser Ser Gly Lys Lys Ala Ile Gly Ala Gly Ala Gly Asn 225 230 235 240 Pro Pro Ala Val Val Asp Glu Thr Ala Asp Ile Glu Lys Ala Ala Arg 245 250 255 Asp Ile Ile Ala Gly Cys Ser Phe Asp Asn Asn Leu Pro Cys Val Ala 260 265 270 Glu Lys Glu Val Ile Val Val Asp Ser Val Ala Asp Tyr Leu Ile Phe 275 280 285 Asn Met Lys Lys Asn Gly Ala Tyr Glu Leu Lys Glu Lys Asp Leu Ile 290 295 300 Glu Gln Leu Glu Lys Leu Val Val Asn Glu Lys Gly Tyr Pro Val Lys 305 310 315 320 Glu Phe Val Gly Lys Asn Ala Asp Tyr Ile Leu Ser Lys Met Gly Ile 325 330 335 Lys Cys Asp Asp Ser Ile Arg Ala Ile Ile Val Glu Val Pro Lys Ser 340 345 350 His Pro Phe Val Val Gly Glu Leu Met Met Pro Val Leu Pro Ile Val 355 360 365 Arg Val Asn Asp Val Glu Glu Ala Ile Lys Leu Ala Val Glu Val Glu 370 375 380 His Gly Phe Lys His Thr Ala Ile Met His Ser Lys Asn Ile Asp Arg 385 390 395 400 Leu Ser Lys Phe Ala Lys Glu Ile Gln Thr Thr Ile Phe Val Lys Asn 405 410 415 Gly Pro Ser Phe Ala Gly Ile Gly Val Gly Gly Glu Gly Tyr Ala Thr 420 425 430 Phe Thr Ile Ala Gly Pro Thr Gly Glu Gly Leu Thr Ser Ala Lys Ser 435 440 445 Phe Ala Arg Arg Arg Arg Cys Thr Leu Val Gly Gly Phe Ser Ile Lys 450 455 460 <210> 367 <211> 481 <212> PRT <213> Artificial Sequence <220> <223> Clostridium populeti <400> 367 Met Asp Ile Ser Ser Gln Glu Ile Glu Ala Ile Val Arg Lys Val Ile 1 5 10 15 Ala Gly Ile Asn Pro Ala Thr Asn Val Thr Pro Asp Ile Pro Ala Ile 20 25 30 Lys Ser Pro Lys Tyr Thr Gly Asp Asn Gly Val Phe Glu Arg Val Glu 35 40 45 Glu Ala Val Glu Ala Ala Trp Lys Ala Gln Arg Asp Trp Val Thr Asn 50 55 60 Tyr Lys Val Glu Asp Arg His Arg Ile Val Glu Ala Ile Arg Arg Cys 65 70 75 80 Gly Arg Asp His Val Glu Glu Trp Ser His Leu Ile Val Glu Glu Thr 85 90 95 Gln Met Gly Arg Tyr Glu Asp Lys Val Glu Lys His Leu Ala Val Ile 100 105 110 Asn Lys Thr Pro Gly Pro Glu Cys Leu Thr Thr Glu Ala Ile Ser Gly 115 120 125 Asp Ala Gly Leu Met Ile Glu Glu Tyr Ala Pro Phe Gly Val Ile Gly 130 135 140 Ser Ile Thr Pro Thr Thr Asn Pro Thr Glu Thr Met Ile His Asn Thr 145 150 155 160 Ile Ser Met Ile Ser Gly Gly Asn Ser Ile Val Phe Asn Val His Pro 165 170 175 Arg Ala Lys Arg Val Cys Ala Glu Cys Leu Gln Ala Leu His Lys Ala 180 185 190 Ile Val Asp Ala Gly Gly Pro Ala Asn Leu Ile Thr Met Leu Arg Glu 195 200 205 Pro Thr Met Asp Thr Val Asp Met Leu Thr Ser Asn Pro Lys Val Arg 210 215 220 Leu Met Thr Gly Thr Gly Gly Met Gly Met Val Asn Ala Leu Leu Arg 225 230 235 240 Ser Gly Lys Lys Cys Ile Gly Ala Gly Ala Gly Asn Pro Pro Val Ile 245 250 255 Val Asp Glu Thr Ala Asp Val Glu Leu Ala Ala Arg Lys Ile Tyr Glu 260 265 270 Gly Ala Ser Phe Asp Asn Asn Ile Leu Cys Phe Ala Glu Lys Glu Val 275 280 285 Phe Val Val Ser Pro Asn Tyr Glu Gly Phe Ile His Asn Ile Gln Lys 290 295 300 Gln Gly Ala Tyr Leu Leu Asn Asn Ser Gln Val Glu Ala Leu Val Lys 305 310 315 320 Ile Cys Leu Glu Pro Asn Lys Asn Gln Ser Gly Tyr Glu Val Asn Lys 325 330 335 Lys Trp Val Gly Lys Asn Ala Ala Leu Ile Leu Ala Gln Ile Gly Val 340 345 350 Gln Val Glu Asp Ser Cys Arg Leu Ala Val Cys Glu Val Pro Ala Asp 355 360 365 His Pro Phe Val Leu Val Glu Gln Met Met Pro Val Leu Pro Ile Val 370 375 380 Arg Cys Ser Thr Phe Glu Glu Ala Met Glu Lys Ala Val Ile Ala Glu 385 390 395 400 Gln Gly Asn Arg His Thr Ser Ser Ile Phe Ser Lys Asp Val Asp His 405 410 415 Met Thr Arg Phe Ala Arg Leu Ile Glu Thr Thr Ile Tyr Val Lys Asn 420 425 430 Ser Cys Thr Lys Ala Gly Val Gly Ile Gly Gly Glu Gly His Cys Thr 435 440 445 Met Thr Ile Ala Gly Pro Thr Gly Glu Gly Ile Thr Asn Ala Lys Ser 450 455 460 Phe Cys Arg Arg Arg Arg Cys Met Leu Ala Glu Gly Gly Leu Arg Ile 465 470 475 480 Ile <210> 368 <211> 450 <212> PRT <213> Artificial Sequence <220> <223> Candidatus Bacteroides periocalifornicus <400> 368 Met Thr Ile Ala Glu Met Val Ala Lys Ala Arg Val Ala Gln Ala Glu 1 5 10 15 Phe Glu Lys Asn Phe Asp Gln Ala Lys Thr Asp Ala Val Val Arg Glu 20 25 30 Ile Gly Lys Thr Val Phe Asp Asn Ala Glu Met Leu Ala Lys Met Ala 35 40 45 Val Glu Glu Thr Arg Met Gly Val Tyr Glu Asp Lys Val Ala Lys Asn 50 55 60 Lys Gly Lys Ala Arg Gly Val Trp Tyr Asp Leu Lys Gly Lys Lys Ser 65 70 75 80 Met Gly Val Leu Ser Val Asp Pro Glu Thr Asp Leu Ile Thr Met Leu 85 90 95 Lys Pro Val Gly Val Val Ala Ala Ile Thr Pro Thr Thr Asn Pro Ile 100 105 110 Val Thr Pro Met Ser Lys Ser Met Phe Ala Val Lys Gly Lys Asn Ala 115 120 125 Ile Ile Val Ala Pro His Pro Arg Ser Lys Lys Cys Thr Ala Lys Thr 130 135 140 Ile Glu Leu Ile Asn Lys Ala Ile Ala Lys Phe Gly Val Pro Lys Asp 145 150 155 160 Leu Ile Gln Val Ile Glu Glu Pro Ser Ile Pro Leu Thr Gln Glu Leu 165 170 175 Met Ala Ser Cys Asp Val Val Leu Ala Thr Gly Gly Met Gly Met Val 180 185 190 Lys Ala Ala Tyr Ser Ser Gly Lys Pro Ser Tyr Gly Val Gly Ala Gly 195 200 205 Asn Val Gln Val Ile Ile Asp Arg Gly Val Asp Tyr Asp Lys Ala Ala 210 215 220 Ala Thr Ile Ile Lys Gly Arg Ile Phe Asp Asn Gly Ile Ile Cys Ser 225 230 235 240 Gly Glu Gln Ser Phe Ile Tyr Pro Lys Asp Glu Lys Ala Lys Val Phe 245 250 255 Asp Ala Phe Lys Lys Asn Gly Ala Tyr Ile Val Ala Asp Ala Asp His 260 265 270 Asp Lys Val Val Asn Ala Leu Phe Glu Asp Gly His Ile Ala Gly Asp 275 280 285 Val Val Gly Gln Ser Val Gln Phe Val Ala Lys Lys Ala Gly Leu Asn 290 295 300 Val Pro Ala Asp Ala Arg Val Ile Val Val Glu Ala Lys Gly Val Gly 305 310 315 320 Ala Gln Asp Pro Ile Cys Lys Glu Lys Met Cys Pro Val Leu Ala Ala 325 330 335 Phe Gly Tyr Asp Lys Phe Glu Glu Ala Ile Gln Ile Ala Lys Thr Asn 340 345 350 Leu Leu Asn Glu Gly Asn Gly His Ser Ala Gly Ile His Ser Asn Asn 355 360 365 Glu Glu His Ile Arg Met Val Gly Glu Gly Leu Thr Val Ser Arg Val 370 375 380 Val Val Asn Ala Pro Val Ser Thr Thr Ala Gly Gly Ala Ile Gly Ser 385 390 395 400 Gly Leu Ala Val Thr Asn Thr Leu Gly Cys Gly Thr Trp Gly Asn Asn 405 410 415 Thr Leu Ser Glu Asn Leu Thr Tyr Lys His Leu Leu Asn Thr Thr Arg 420 425 430 Val Ala Arg Ile Ser Pro Lys Val His Gln Pro Thr Asp Glu Glu Leu 435 440 445 Trp Gly 450 <210> 369 <211> 480 <212> PRT <213> Artificial Sequence <220> <223> Anaerocolumna aminovalerica <400> 369 Met Glu Phe Gly Thr Lys Glu Ile Ser Met Ile Val Glu Gln Val Leu 1 5 10 15 Lys Asn Leu Glu Glu Asn Asn Leu Ile Ser Thr Lys Lys Thr Ser Asn 20 25 30 Ser Gly Leu Tyr Ser Asp Lys Gly Asp Tyr Gly Val Phe Glu Arg Val 35 40 45 Glu Asp Ala Ile Asp Ala Ala Tyr Glu Ala Gln Lys Ile Tyr Leu Asp 50 55 60 Asn Phe Lys Ile Lys Asp Arg Gln Arg Leu Ile Ala Ala Ile Arg Lys 65 70 75 80 Val Ser Ile Glu Asn Ala Glu Thr Leu Ala Arg Met Ile Val Glu Glu 85 90 95 Ser Lys Met Gly Arg Val Glu Asp Lys Val Lys Lys His Leu Ala Val 100 105 110 Ile Glu Asn Thr Pro Gly Pro Glu Cys Leu Thr Thr Asp Ala Ile Thr 115 120 125 Gly Asp Gly Gly Leu Met Ile Glu Glu Tyr Ala Pro Phe Gly Leu Ile 130 135 140 Gly Ala Ile Thr Pro Val Thr Asn Pro Thr Glu Thr Ile Ile Asn Asn 145 150 155 160 Thr Ile Ser Met Ile Ser Gly Gly Asn Gly Ile Val Phe Asn Val His 165 170 175 Pro Ser Ala Lys Lys Val Cys Ala Tyr Cys Leu Gln Phe Ile Asn Lys 180 185 190 Thr Ile Ile Glu Asn Gly Gly Pro Ala Asn Leu Ile Thr Met Val Lys 195 200 205 Glu Pro Thr Met Glu Thr Cys Asn Ile Ile Thr Gln Ser Pro Lys Val 210 215 220 Arg Leu Met Val Gly Thr Gly Gly Met Gly Met Val Asn Ser Leu Leu 225 230 235 240 Arg Ser Gly Lys Lys Thr Ile Gly Ala Gly Ala Gly Asn Pro Pro Val 245 250 255 Ile Val Asp Glu Thr Ala Asp Ile Lys Lys Ala Ala Lys Asp Ile Tyr 260 265 270 Tyr Gly Ala Ser Phe Asp Asn Asn Leu Leu Cys Leu Ala Glu Lys Glu 275 280 285 Val Phe Val Leu Glu Glu Val Ala Asn Asp Phe Ile Tyr Asn Met Val 290 295 300 Asp Glu Gly Ala Phe Leu Leu Asn Gly Ala Gln Leu Glu Ala Ile Thr 305 310 315 320 Asn Leu Val Leu Lys Tyr Glu Asn Gly Lys Tyr Asp Ile Asn Lys Lys 325 330 335 Trp Val Gly Gln Asp Ala Gly Lys Met Leu Glu Ala Ile Gly Ile Thr 340 345 350 Gly Lys Ser Asp Thr Arg Leu Leu Ile Cys Asp Val Pro Tyr Asp Asn 355 360 365 Pro Phe Val Leu Leu Glu Gln Leu Met Pro Val Leu Pro Ile Val Arg 370 375 380 Cys Lys Asn Leu Asn Gln Ala Ile Asp Tyr Ala Met Ile Ala Glu Ser 385 390 395 400 Gly Asn Arg His Thr Ala Ser Met Phe Ser Lys Asn Val Asp Asn Met 405 410 415 Thr Arg Phe Ala Arg Lys Ile Glu Thr Thr Ile Phe Val Lys Asn Gly 420 425 430 Cys Thr Leu Glu Gly Val Gly Ile Gly Gly Glu Gly Tyr Thr Thr Met 435 440 445 Thr Ile Ala Gly Pro Thr Gly Glu Gly Ile Thr Cys Ala Lys Ser Phe 450 455 460 Thr Arg Arg Arg Arg Cys Met Leu Ala Asp Gly Gly Leu Arg Ile Ile 465 470 475 480 <210> 370 <211> 405 <212> PRT <213> Artificial Sequence <220> <223> Candida tropicalis <400> 370 Met Ala Met Phe Thr Thr Thr Ala Lys Val Ile Gln Pro Lys Ile Arg 1 5 10 15 Gly Phe Ile Cys Thr Thr Thr His Pro Ile Gly Cys Glu Lys Arg Val 20 25 30 Gln Glu Glu Ile Ala Tyr Ala Arg Ala His Pro Pro Thr Ser Pro Gly 35 40 45 Pro Lys Arg Val Leu Val Ile Gly Cys Ser Thr Gly Tyr Gly Leu Ser 50 55 60 Thr Arg Ile Thr Ala Ala Phe Gly Tyr Gln Ala Ala Thr Leu Gly Val 65 70 75 80 Phe Leu Ala Gly Pro Pro Thr Lys Gly Arg Pro Ala Ala Ala Gly Trp 85 90 95 Tyr Asn Thr Val Ala Phe Glu Lys Ala Ala Leu Glu Ala Gly Leu Tyr 100 105 110 Ala Arg Ser Leu Asn Gly Asp Ala Phe Asp Ser Thr Thr Lys Ala Arg 115 120 125 Thr Val Glu Ala Ile Lys Arg Asp Leu Gly Thr Val Asp Leu Val Val 130 135 140 Tyr Ser Ile Ala Ala Pro Lys Arg Thr Asp Pro Ala Thr Gly Val Leu 145 150 155 160 His Lys Ala Cys Leu Lys Pro Ile Gly Ala Thr Tyr Thr Asn Arg Thr 165 170 175 Val Asn Thr Asp Lys Ala Glu Val Thr Asp Val Ser Ile Glu Pro Ala 180 185 190 Ser Pro Glu Glu Ile Ala Asp Thr Val Lys Val Met Gly Gly Glu Asp 195 200 205 Trp Glu Leu Trp Ile Gln Ala Leu Ser Glu Ala Gly Val Leu Ala Glu 210 215 220 Gly Ala Lys Thr Val Ala Tyr Ser Tyr Ile Gly Pro Glu Met Thr Trp 225 230 235 240 Pro Val Tyr Trp Ser Gly Thr Ile Gly Glu Ala Lys Lys Asp Val Glu 245 250 255 Lys Ala Ala Lys Arg Ile Thr Gln Gln Tyr Gly Cys Pro Ala Tyr Pro 260 265 270 Val Val Ala Lys Ala Leu Val Thr Gln Ala Ser Ser Ala Ile Pro Val 275 280 285 Val Pro Leu Tyr Ile Cys Leu Leu Tyr Arg Val Met Lys Glu Lys Gly 290 295 300 Thr His Glu Gly Cys Ile Glu Gln Met Val Arg Leu Leu Thr Thr Lys 305 310 315 320 Leu Tyr Pro Glu Asn Gly Ala Pro Ile Val Asp Glu Ala Gly Arg Val 325 330 335 Arg Val Asp Asp Trp Glu Met Ala Glu Asp Val Gln Gln Ala Val Lys 340 345 350 Asp Leu Trp Ser Gln Val Ser Thr Ala Asn Leu Lys Asp Ile Ser Asp 355 360 365 Phe Ala Gly Tyr Gln Thr Glu Phe Leu Arg Leu Phe Gly Phe Gly Ile 370 375 380 Asp Gly Val Asp Tyr Asp Gln Pro Val Asp Val Glu Ala Asp Leu Pro 385 390 395 400 Ser Ala Ala Gln Gln 405

Claims (68)

  1. 서열번호 152, 153 또는 254의 아미노산의 하나 이상의 변이를 포함하는 조작된 카르복시산 리덕타제 (CAR) 효소.
  2. 제1항에 있어서, 상기 조작된 CAR 효소는
    (a) 6-아미노카프로익산 기질로부터 6-아미노카프로에이트 세미알데하이드를 합성할 수 있거나;
    (b) 야생형 CAR과 비교해 더 높은 비율로 6-아미노카프로익산 기질로부터 6-아미노카프로에이트 세미알데하이드를 합성할 수 있거나;
    (c) 야생형 CAR과 비교해 6-아미노카프로익산 기질에 대해 더 높은 친화성을 가지거나; 또는
    (d) (a), (b) 및 (c)의 임의 조합을 가진, 조작된 CAR 효소.
  3. 제1항 또는 제2항에 있어서, 상기 조작된 CAR이 서열번호 152, 153 또는 254의 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929 또는 이들의 조합으로 이루어진 군으로부터 선택되는 하나 이상의 잔기 위치에 하나 이상의 아미노산 변이를 포함하는, 조작된 CAR 효소.
  4. 제1항 내지 제3항 중 어느 한 항에 있어서, 상기 조작된 CAR이 서열번호 152, 153 또는 254의 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929 또는 이들의 임의 조합으로 이루어진 군으로부터 선택되는 하나 이상의 잔기 위치에 보존적인 아미노산 치환으로서 하나 이상의 아미노산 변이를 포함하는, 조작된 CAR 효소.
  5. 제1항 내지 제3항 중 어느 한 항에 있어서, 상기 조작된 CAR이 서열번호 152, 153 또는 254의 P141, L245, I247, W270, S274, K275, N276, F278, G279, N279insert, A282, A283, S299, I300, N335, S336, M389, G391, G414, G421, M422, F425, G636, D809, I810, L811, A812 및 F929 또는 이들의 임의 조합으로 이루어진 군으로부터 선택되는 하나 이상의 잔기 위치에 비-보존적인 아미노산 치환으로서 하나 이상의 아미노산 변이를 포함하는, 조작된 CAR 효소.
  6. 제1항 내지 제5항 중 어느 한 항에 있어서, 조작된 단백질의 하나 이상의 아미노산 변이가 서열번호 152, 153 또는 254에 대한 표 9 및 이의 임의 조합들로부터 선택되는 변이인, 조작된 CAR 효소.
  7. 제1항 내지 제6항 중 어느 한 항에 있어서, 상기 아미노산 변이가 서열번호 152, 153 또는 254의 아미노산 서열에서 2개 이상, 3개 이상, 4개 이상, 5개 이상, 6개 이상, 7개 이상 또는 8개 이상을 포함하는, 조작된 CAR 효소.
  8. 제1항 내지 제7항 중 어느 한 항에 있어서, 상기 아미노산 위치가 서열번호 152, 153 또는 254의 아미노산 위치 2개 이상, 3개 이상, 4개 이상, 5개 이상, 6개 이상, 7개 이상 또는 8개 이상을 포함하는, 조작된 CAR 효소.
  9. 제1항 내지 제8항 중 어느 한 항에 있어서, 상기 조작된 CAR이 서열번호 152, 153 또는 254의 CAR 활성보다 적어도 20% 높은 활성을 포함하는, 조작된 CAR 효소.
  10. 제1항 내지 제9항 중 어느 한 항에 있어서, 상기 조작된 CAR이 N335E; N335D; S274D; S274E; K275D; K275E; S299D; S299E; M389D; M389E; G414D; G414E; G421D; G421E; M422D; M422E; F425D; F425E; N335D 및 A282P; N335D 및 A282V; N335D 및 A283C; N335D, A283C 및 F929L; N335D, A283C 및 G636D; N335D 및 A283G; N335D 및 F278A; N335D 및 F278C; N335D 및 F278S; N335D 및 F278V; N335D 및 G279V; N335D 및 I247M; N335D 및 I247Q; N335D 및 I247T; N335D 및 I247V; N335D 및 I300C; N335D 및 I300G; N335D 및 I300M; N335D 및 I300M; N335D 및 I300Y; N335D 및 K275A; N335D 및 K275D; N335D 및 K275D; N335D 및 K275E; N335D 및 K275M; N335D 및 K275N; N335D 및 K275S; N335D 및 K275T; N335D 및 K275V; N335D 및 K275W; N335D 및 L245C; N335D 및 L245G; N335D 및 L245S; N335D 및 L245T; N335D 및 L245V; N335D 및 M389I; N335D 및 M389W; N335D 및 M422D; N335D 및 N276S; N335D 및 N279INSERT; N335D 및 P141G; N335D 및 S299D; N335D 및 S299E; N335D 및 S391G; N335D 및 W270M; K275D, N276S, F278S, A283C 및 N335D; L245V, K275D, N276S, F278S, A283C 및 N335D; I247M, K275D, N276S, F278A, A283C 및 N335D; L245V, K275T, N276S, F278S, A283C 및 N335D; I247M, K275T, N276S, F278S, A283C 및 N335D; K275D, N276S, F278S, A283C, I300G 및 N335D; L245T, K275D, N276S, F278A, A283C 및 N335D; K275N, F278S, A283C, S299D 및 N335D; I247M, K275N, N276S, F278S, A283C 및 N335D; K275N, F278S, A283C, I300G 및 N335D; K275N, N276S, F278S, A283C, I300G 및 N335D; I247M, K275T, F278S, A283C 및 N335D; L245V, K275D, N276S, F278A, A283C 및 N335D; K275N, F278S, A283C, I300G 및 N335D; K275N, F278A, A283C, S299D 및 N335D; K275N, N276S, F278A, A283C 및 N335D; L245V, K275N, N276S, F278S, A283C, I300G 및 N335D; L245T, K275N, N276S, F278S, A283C, I300G 및 N335D; K275N, F278A, S299D 및 N335D; I247M, K275N, F278A, A283C, I300Y 및 N335D; I247M, K275N, F278A, A283C 및 N335D; K275D, N276S, F278A 및 N335D; K275T, F278A, A283C, S299D 및 N335D; F278A, A282P 및 N335D; F278A, A283C 및 N335D; K275N, S299D 및 N335D; L245T, S299D 및 N335D; K275D, S299D 및 N335D; K275N, F278S 및 N335D; S299D, M389W 및 N335D; G279V, S299D 및 N335D; F278A, S283C 및 N335D; K275D, N276S 및 N335D; G279V, S299E 및 N335D; I247M, S299D 및 N335D; P141G, A282P 및 N335D; L245T, A282P 및 N335D; F278S, A283C 및 N335D; K275D, S284I, S299D 및 N335D; I247M, I282P 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D;. K275D, S274A, N276S, F278S, A283C, I300G 및 N335D; K275D, S274P, N276S, F278S, A283C, I300G 및 N335D; K275D, N276S, F278S, A282F, A283C, I300G 및 N335D; K275D, N276S, F278S, A282P, A283C, I300G 및 N335D; K275D, N276S, F278S, A283C, S299I, I300G 및 N335D; K275D, N276S, F278S, A283C, I300G, N335D 및 M389C; K275D, N276S, F278S, A283C, I300G, N335D 및 M389Y; 및 K275D, N276S, F278S, A283C, I300G, N335D 및 M389S로 이루어진 군으로부터 선택되는 하나 이상의 아미노산 변이를 포함하는, 조작된 CAR 효소.
  11. 제1항 내지 제10항 중 어느 한 항에 있어서, 상기 조작된 CAR이 서열번호 153의 아미노산의 하나 이상의 변이를 포함하고, 조작된 CAR이 K275D, N276S, F278S, A283C, I300G 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D; I247V, K275D, N276S, F278S, A283C, I300G 및 N335D;. K275D, S274A, N276S, F278S, A283C, I300G 및 N335D; K275D, S274P, N276S, F278S, A283C, I300G 및 N335D; K275D, N276S, F278S, A282F, A283C, I300G 및 N335D; K275D, N276S, F278S, A282P, A283C, I300G 및 N335D; K275D, N276S, F278S, A283C, S299I, I300G 및 N335D; K275D, N276S, F278S, A283C, I300G, N335D 및 M389C; K275D, N276S, F278S, A283C, I300G, N335D 및 M389Y; 및 K275D, N276S, F278S, A283C, I300G, N335D 및 M389S로 이루어진 군으로부터 선택되는 하나 이상의 아미노산 변이를 포함하는, 조작된 CAR 효소.
  12. 제1항 내지 제11항 중 어느 한 항에 따른 조작된 CAR을 코딩하는 핵산.
  13. 제12항에 있어서, 상기 조작된 CAR을 코딩하는 핵산 서열이 프로모터에 작동가능하게 연결된, 핵산.
  14. 제13항의 핵산을 포함하는 벡터.
  15. (a) 제1항 내지 제11항 중 어느 하나로부터 선택되는 조작된 CAR;
    (b) 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264 중 임의 서열의 연속적인 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는 CAR; 또는
    (c) 서열번호 265 및 267-296 중 임의 서열의 연속적인 아미노산 적어도 25, 50, 75, 100, 150, 200, 250, 300개 또는 그 이상에 대해 적어도 50%의 서열 동일성을 가진 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소
    를 코딩하는 외인성 핵산을 포함하는, 비-천연성 미생물 유기체.
  16. 제15항에 있어서,
    (a) 서열번호 1, 13 또는 31의 아미노산의 하나 이상의 변이를 포함하는 조작된 트랜스아미나제 (TA) 효소;
    (b) 서열번호 1의 잔기 V114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265, L386, G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416, A421, G17, M21, A50, A76, Y77, Q78, I79, G84, F107, T108, K119, G139, M142, A152, P153, E205, G209, G211, D238, M285, A290, G291, G292, L293, Y297, M353, S387, S388 및 G392 또는 이들의 조합으로부터 선택되는 하나 이상의 위치에서 하나 이상의 아미노산 변이를 포함하는 조작된 트랜스아미나제 (TA) 효소;
    (c) 서열번호 1에 대한 표 7에 기술된 변이 및 이들의 조합으로부터 선택되는 조작된 단백질의 하나 이상의 아미노산 변이를 포함하는 조작된 트랜스아미나제 (TA) 효소; 또는
    (d) 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116 중 임의 서열에서 연속적인 아미노산 적어도 25개 이상에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는 트랜스아미나제
    를 코딩하는 외인성 핵산을 더 포함하는, 비-천연성 미생물 유기체.
  17. 제16항에 있어서, 서열번호 1의 하나 이상의 잔기 위치 또는 이들의 조합에서의 하나 이상의 아미노산 변이가 보존적인 아미노산 변이 또는 비-보존적인 아미노산 변이로부터 선택되는, 조작된 TA.
  18. 제15항 내지 제17항 중 어느 한 항에 있어서, 상기 외인성 핵산이 이종의 것인, 비-천연성 미생물 유기체.
  19. 제15항 내지 제17항 중 어느 한 항에 있어서, 상기 외인성 핵산이 동종의 것인, 비-천연성 미생물 유기체.
  20. 제15항 내지 제19항 중 어느 한 항에 있어서, 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 CAR을 포함하는, 비-천연성 미생물 유기체.
  21. 제15항 내지 제19항 중 어느 한 항에 있어서, 표 9에 기재된 CAR 변이체 1-115로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 CAR을 포함하는, 비-천연성 미생물 유기체.
  22. 제15항 내지 제21항 중 어느 한 항에 있어서, 서열번호 265 및 267-296로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 HMD 트랜스아미나제 (TA2)를 포함하는, 비-천연성 미생물 유기체.
  23. 제16항 내지 제22항 중 어느 한 항에 있어서, 표 7에 기재된 TA 변이체 1-233으로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 조작된 트랜스아미나제 (TA)를 포함하는, 비-천연성 미생물 유기체.
  24. 제15항 내지 제23항 중 어느 한 항에 있어서, 아디필-CoA와 반응하여 아디페이트-세미알데하이드를 합성하는 알데하이드 데하이드로게나제 (ALD) 효소를 코딩하는 하나 이상의 외인성 핵산을 더 포함하는, 비-천연성 미생물 유기체.
  25. 제24항에 있어서, 서열번호 141-143 및 297-370으로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 ALD 효소를 포함하는, 비-천연성 미생물 유기체.
  26. 제24항 또는 제25항에 있어서, 상기 ALD 효소가 기질로서 숙시닐-CoA, 아세틸-CoA 또는 숙시닐-CoA 및 아세틸-CoA 둘다에 비해 아디필-CoA 기질에 대해 더 높은 촉매 효율을 가지거나, 및/또는 기질로서 숙시닐-CoA, 아세틸-CoA 또는 숙시닐-CoA 및 아세틸-CoA 둘다와 비해 아디필-CoA 기질에 대해 더 높은 대사회전수를 가진, 비-천연성 미생물 유기체.
  27. 제25항 또는 제26항에 있어서, 헥사메틸렌다이아민 (HMD)을 생산하기 위해 충분한 양으로 발현되는 HMD 경로 효소를 가진 헥사메틸렌다이아민 (HMD) 경로를 포함하고, 상기 HMD 경로가 (1) 3-옥소아디필-CoA 티올라제, (2) 하이드록시아디필-CoA 데하이드로게나제 (HBD), (3) 크로토나제, (4) 트랜스-에노일CoA 리덕타제 (TER), (5) 6ACA-알데하이드 데하이드로게나제 (6ACA-ALD), (6) 6ACA-트랜스아미나제 (TA), (7) 카르복시산 리덕타제 (CAR) 및 (8) HMD-트랜스아미나제 (TA2)를 포함하는, 비-천연성 미생물 유기체.
  28. 제27항에 있어서, 포스포판테테이닐 트랜스퍼라제 HMD 경로 효소를 코딩하는 외인성 핵산을 더 포함하는, 비-천연성 미생물 유기체.
  29. 제27항 또는 제28항에 있어서, 상기 미생물 유기체가 각각 HMD 경로 효소를 코딩하는 외인성 핵산을 1종, 2종, 3종, 4종, 5종, 6종, 7종, 8종 또는 9종 포함하는, 비-천연성 미생물 유기체.
  30. 제27항 또는 제28항에 있어서, 상기 미생물 유기체가 각각 HMD 경로 효소를 코딩하는 외인성 핵산들을 포함하는, 비-천연성 미생물 유기체.
  31. 제27항 내지 제30항 중 어느 한 항에 있어서, 상기 하나 이상의 외인성 핵산이 이종의 핵산인, 비-천연성 미생물 유기체.
  32. 제27항 내지 제31항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가 실질적으로 혐기성 배양 배지에 존재하는, 비-천연성 미생물 유기체.
  33. 제27항 내지 제32항 중 어느 한 항에 있어서, 상기 미생물 유기체가 박테리아, 효모 또는 진균 종인, 비-천연성 미생물 유기체.
  34. 제27항 내지 제33항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가 제15항 내지 제26항 중 어느 한 항의 외인성 핵산을 포함하지 않는 대조군 미생물 유기체와 비교해 6-아미노카프로에이트 세미알데하이드, HMD 또는 이 둘다를 적어도 10% 이상으로 많이 생산할 수 있는, 비-천연성 미생물 유기체.
  35. 제27항 내지 제34항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가, 제15항 내지 제23항 중 어느 한 항의 외인성 핵산을 포함하지 않는 대조군 미생물 유기체를 제외한, 비-천연성 미생물 유기체와 실질적으로 동일한 대조군 미생물 유기체와 비교해,
    (a) 아디페이트 세미알데하이드에서 6-아미노카프로익산으로의 변환;
    (b) 6-아미노카프로익산에서 6-아미노카프로에이트 세미알데하이드로의 변환, 및/또는
    (c) 6-아미노카프로에이트 세미알데하이드에서 HMD로의 변환을 더 높은 수준으로 달성하는, 비-천연성 미생물 유기체.
  36. 하기를 코딩하는 외인성 핵산을 포함하는 비-천연성 미생물 유기체:
    (a) 제1항 내지 제11항 중 어느 한 항으로부터 선택되는 조작된 CAR, 또는
    (b) 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264 중 임의 서열의 연속적인 아미노산 적어도 25개 이상에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는 CAR.
  37. 제36항에 있어서, 하기를 코딩하는 외인성 핵산을 추가로 포함하는, 비-천연성 미생물 유기체:
    (a) 서열번호 1, 13 또는 31의 아미노산의 하나 이상의 변이를 포함하는 조작된 트랜스아미나제 (TA) 효소;
    (b) 서열번호 1의 잔기 V114, S136, T148, P153, I203, I204, P206, V207, V111, T216, A237, T264, M265, L386, G19, C22, D70, R94, D99, T109, E112, A113, F137, G144, I149, K150, Y154, S178, L186, Q208, L234, T242, A315, K318, R338, G336, L386, V390, A406, S416, A421, G17, M21, A50, A76, Y77, Q78, I79, G84, F107, T108, K119, G139, M142, A152, P153, E205, G209, G211, D238, M285, A290, G291, G292, L293, Y297, M353, S387, S388 및 G392로부터 선택되는 하나 이상의 위치 또는 이들의 조합에서 하나 이상의 아미노산 변이를 포함하는, 조작된 트랜스아미나제 (TA) 효소;
    (c) 서열번호 1에 대한 표 7에 기재된 변이 및 이들의 조합으로부터 선택되는 조작된 단백질의 하나 이상의 아미노산 변이를 포함하는, 조작된 트랜스아미나제 (TA) 효소; 또는
    (d) 서열번호 1, 3, 4, 5, 9, 12, 13, 26, 27, 30, 31, 38, 50, 52, 64, 74, 78, 79, 81, 91, 106, 108 및 116 중 임의 서열의 연속적인 아미노산 적어도 25개 이상에 대해 적어도 50%의 서열 동일성을 가진 아미노산 서열을 포함하는, 트랜스아미나제.
  38. 제37항에 있어서, 서열번호 1의 하나 이상의 잔기 위치 또는 이들의 조합에서의 하나 이상의 아미노산 변이가 보존적인 아미노산 변이 또는 비-보존적인 아미노산 변이로부터 선택되는, 비-천연성 미생물 유기체.
  39. 제36항 내지 제38항 중 어느 한 항에 있어서, 상기 외인성 핵산이 이종의 것인, 비-천연성 미생물 유기체.
  40. 제36항 내지 제38항 중 어느 한 항에 있어서, 상기 외인성 핵산이 동종의 것인, 비-천연성 미생물 유기체.
  41. 제36항 내지 제40항 중 어느 한 항에 있어서, 서열번호 150-165, 168-171, 173-178, 180, 183-185, 187-188, 190-193, 195, 198-200, 202-216, 218-219, 221-230, 232-238, 241-244, 246-249, 251-252 및 255-264로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 CAR을 포함하는, 비-천연성 미생물 유기체.
  42. 제36항 내지 제40항 중 어느 한 항에 있어서, 표 9에 기재된 CAR 변이체 1-115로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 CAR을 포함하는, 비-천연성 미생물 유기체.
  43. 제37항 내지 제42항 중 어느 한 항에 있어서, 표 7에 기재된 TA 변이체 1-233으로 이루어진 군으로부터 선택되는 아미노산 서열을 가진 조작된 트랜스아미나제 (TA)를 포함하는, 비-천연성 미생물 유기체.
  44. 제36항 내지 제43항 중 어느 한 항에 있어서, 1,6-헥산다이올 (HDO)을 생산하기 위해 충분한 양으로 발현되는 HDO 경로 효소를 가진 1,6-헥산다이올 (HDO) 경로를 포함하고, 상기 HDO 경로가 (1) 티올라제, (2) 하이드록시아디필-CoA 데하이드로게나제 (HBD), (3) 크로토나제, (4) 트랜스-에노일CoA 리덕타제 (TER), (5) 6ACA-알데하이드 데하이드로게나제 (6ACA-ALD), (6) 6ACA-트랜스아미나제 (TA), (7) 카르복시산 리덕타제 (CAR), (8) 6-아미노카프로에이트 세미알데하이드 리덕타제, (9) 6-아미노헥사놀 아미노트랜스퍼라제 또는 옥시도리덕타제 및 (10) 6-하이드록시헥사날 리덕타제를 포함하는, 비-천연성 미생물 유기체.
  45. 제44항에 있어서, 포스포판테테이닐 트랜스퍼라제 HDO 경로 효소를 코딩하는 외인성 핵산을 추가로 포함하는, 비-천연성 미생물 유기체.
  46. 제44항 또는 제45항에 있어서, 상기 미생물 유기체가 HDO 경로 효소를 각각 코딩하는 외인성 핵산을 1종, 2종, 3종, 4종, 5종, 6종, 7종, 8종, 9종, 10종 또는 11종 포함하는, 비-천연성 미생물 유기체.
  47. 제44항 내지 제46항 중 어느 한 항에 있어서, 상기 미생물 유기체가 HDO 경로의 효소를 각각 코딩하는 외인성 핵산들을 포함하는, 비-천연성 미생물 유기체.
  48. 제44항 내지 제47항 중 어느 한 항에 있어서, 상기 하나 이상의 외인성 핵산이 이종의 핵산인, 비-천연성 미생물 유기체.
  49. 제44항 내지 제48항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가 실질적으로 혐기성 배양 배지에 존재하는, 비-천연성 미생물 유기체.
  50. 제44항 내지 제49항 중 어느 한 항에 있어서, 상기 미생물 유기체가 박테리아, 효모 또는 진균 종인, 비-천연성 미생물 유기체.
  51. 제44항 내지 제50항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가 제36항 내지 제43항 중 어느 한 항에 따른 외인성 핵산을 포함하지 않는 대조군 미생물 유기체와 비교해 6-아미노카프로에이트 세미알데하이드, HDO 또는 이 둘다를 적어도 10% 많이 생산할 수 있는, 비-천연성 미생물 유기체.
  52. 제44항 내지 제51항 중 어느 한 항에 있어서, 상기 비-천연성 미생물 유기체가 제36항 내지 제43항 중 어느 한 항의 외인성 핵산을 포함하지 않는 대조군 미생물 유기체를 제외한 비-천연성 미생물 유기체와 실질적으로 동일한 대조군 미생물과 비교해,
    (a) 아디페이트 세미알데하이드에서 6-아미노카프로익산으로의 변환, 및/또는
    (b) 6-아미노카프로익산에서 6-아미노카프로에이트 세미알데하이드로의 변환을 더 높은 수준으로 달성하는, 비-천연성 미생물 유기체.
  53. 제27항 내지 제35항 중 어느 한 항에 따른 비-천연성 미생물 유기체를 헥사메틸렌다이아민 (HMD)을 생산하기 위해 충분한 기간 및 조건 하에 배양하는 것을 포함하는, HMD의 생산 방법.
  54. 제53항에 있어서, 상기 방법이 배양물에서 다른 성분들로부터 HMD를 분리하는 것을 추가로 포함하는, 방법.
  55. 제54항에 있어서, 상기 분리가 추출, 연속 액체-액체 추출, 투과 증발, 막 여과, 막 분리, 역 삼투압, 전기투석, 증류, 결정화, 원심분리, 추출 여과, 이온 교환 크로마토그래피, 흡착 크로마토그래피 또는 한외여과를 포함하는, 방법.
  56. 제43항 내지 제52항 중 어느 한 항에 따른 비-천연성 미생물 유기체를 HMD를 생산하기 위해 충분한 기간 및 조건 하에 배양하는 것을 포함하는, 1,6-헥산다이올 (HDO)의 생산 방법.
  57. 제56항에 있어서, 상기 방법이 배양물에서 다른 성분들로부터 HMD를 분리하는 것을 추가로 포함하는, 방법.
  58. 제57항에 있어서, 상기 분리가 추출, 연속 액체-액체 추출, 투과 증발, 막 여과, 막 분리, 역 삼투압, 전기투석, 증류, 결정화, 원심분리, 추출 여과, 이온 교환 크로마토그래피, 흡착 크로마토그래피 또는 한외여과를 포함하는, 방법.
  59. 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 포함하는 배양물 배지로서,
    상기 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO가 대기 이산화탄소 흡수원을 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진, 배양물 배지.
  60. 제59항에 있어서, 상기 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO가
    (a) 제15항 내지 제35항 중 어느 한 항에 따른 비-천연성 미생물 유기체;
    (b) 제36항 내지 제52항 중 어느 한 항에 따른 비-천연성 미생물 유기체;
    (c) 제53항 내지 제55항 중 어느 한 항에 따른 방법; 또는
    (d) 제56항 내지 제58항 중 어느 한 항에 따른 방법
    에 의해 생산되는, 배양물 배지.
  61. 제59항 내지 제61항 중 어느 한 항에 있어서, 상기 배양물 배지가
    (a) 제1항 내지 제11항 중 어느 한 항에 따른 조작된 CAR;
    (b) 제12항 내지 제14항 중 어느 한 항에 따른 핵산;
    (c) 제16항, 제17항, 제37항, 제38항 및 제43항 중 어느 한 항에 따른 조작된 트랜스아미나제 (TA) 효소;
    (d) 제16항, 제17항, 제37항, 제38항 및 제43항 중 어느 한 항에 따른 TA 효소를 코딩하는 핵산;
    (e) 제15항에 따른 조작된 헥사메틸렌다이아민 (HMD) 트랜스아미나제 (TA2) 효소;
    (f) 제15항에 따른 TA2 효소를 코딩하는 핵산;
    (g) 제24항 내지 제27항 중 어느 한 항에 따른 알데하이드 데하이드로게나제 (ALD) 효소;
    (h) 제24항 내지 제27항 중 어느 한 항에 따른 ALD 효소를 코딩하는 핵산;
    (i) 제15항 내지 제35항 중 어느 한 항에 따른 비-천연성 미생물 유기체; 또는
    (j) 제36항 내지 제52항 중 어느 한 항에 따른 비-천연성 미생물 유기체
    를 포함하는, 배양물 배지.
  62. 제59항 내지 제61항 중 어느 한 항에 있어서, 상기 배양물 배지는 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 생산하는 비-천연성 미생물 유기체로부터 분리되는, 배양물 배지.
  63. 대기 이산화탄소 흡수원을 반영하는 탄소-12, 탄소-13 및 탄소-14 동위원소 비율을 가진, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO.
  64. 제63항에 있어서,
    (a) 제15항 내지 제35항 중 어느 한 항에 따른 비-천연성 미생물 유기체;
    (b) 제36항 내지 제52항 중 어느 한 항에 따른 비-천연성 미생물 유기체;
    (c) 제53항 내지 제55항 중 어느 한 항에 따른 방법; 또는
    (d) 제56항 내지 제58항 중 어느 한 항에 따른 방법
    에 의해 생산된, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO.
  65. 제63항 또는 제64항에 있어서, 상기 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO가 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95% 또는 적어도 98%의 Fm 값을 가지는, 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO.
  66. 제63항 내지 제65항 중 어느 한 항에 따른 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO; 및 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO 이외의 다른 화합물을 포함하는, 조성물.
  67. 제63항에 따른 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO를 포함하고, 제15항 내지 제42항 중 어느 한 항에 따른 비-천연성 미생물 유기체를 일부 추가로 포함하는, 조성물.
  68. 제66항 또는 제67항에 따른 생물유래 HMD, 6-아미노카프로에이트 세미알데하이드 및/또는 HDO, 또는 이의 세포 용해물 또는 배양 상층액을 포함하는 조성물.
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