KR20080059604A - Ｌ-아미노산 생산 세균 및 ｌ-아미노산 생산 방법 - Google Patents
Ｌ-아미노산 생산 세균 및 ｌ-아미노산 생산 방법 Download PDFInfo
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- KR20080059604A KR20080059604A KR1020087010096A KR20087010096A KR20080059604A KR 20080059604 A KR20080059604 A KR 20080059604A KR 1020087010096 A KR1020087010096 A KR 1020087010096A KR 20087010096 A KR20087010096 A KR 20087010096A KR 20080059604 A KR20080059604 A KR 20080059604A
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Abstract
L-아미노산은 EvgAS 2-성분 시스템 레귤론에 관여하는 전사 인자를 암호화하는 evgA 유전자, gadE 유전자, 또는 ydeO 유전자로부터 선택되는 하나 이상의 유전자의 발현량이 증가되도록 변형된 L-아미노산 생산 능력을 갖는 엔테로박테리아세애 과의 미생물을 배지에서 배양하여; 배지 또는 세포에서 L-아미노산을 생산하고 축적시키고, 배지 또는 세포로부터 L-아미노산을 수거함으로써 생산된다.
엔테로박테리아세애, evgA 유전자, gadE 유전자, L-아미노산, EvgAS 2-성분 시스템
Description
본 발명은 미생물을 사용하여 L-아미노산을 생산하는 방법 및 보다 구체적으로 L-라이신, L-트레오닌, L-트립토판 등과 같은 L-아미노산을 생산하는 방법에 관한 것이다. L-라이신, L-트레오닌 및 L-트립토판은 동물 사료 첨가제, 건강 식품 성분 및 아미노산 주입물로서 산업적으로 사용되고 있다.
L-아미노산 등과 같은 표적 물질을 미생물을 사용한 발효에 의해 생산하는데 있어서, 야생형 미생물(야생형 균주), 야생형 균주로부터 유래된 영양요구성 균주, 야생형 균주로부터 유래된 다양한 유형의 약물 내성 돌연변이 균주중 하나로서 대사 조절 돌연변이 균주, 영양요구성 균주 및 대사 조절 돌연변이 균주 둘다의 특성을 갖는 균주등을 사용하는 방법들이 있다.
최근에는 재조합 DNA 기술을 사용하여 발효에 의해 표적 물질을 생산해 왔다. 예를 들어, L-아미노산을 생산하는 미생물의 능력은 L-아미노산 생합성 효소를 암호화하는 유전자의 발현을 증진시키거나(미국 특허 제5168056호, 미국 특허 제5776736호) L-아미노산 생합성 시스템으로의 탄소원 유입을 증진시킴에 의해(미국 특허 제5906925호) 개선되었다.
에스케리치아 콜리(Escherichia coli)등과 같은 엔테로박테리아세애(Enterobacteriaceae)의 세균에서 발견된 2-성분 시스템 EvgAS에 대하여, 센서 키나제인 EvgS의 기능은 공지되어 있지 않지만 반응 조절인자 전사 인자인 EvgA는 많은 유전자의 전사를 조절하는 것으로 공지되어 있다(Masuda, N. and Church, G. M., J. Bacteriol. 2002. 184(22):6225-6234. Escherichia coli gene expression responsive to levels of the response regulator EvgA.). 또한 전사 인자 EvgA는 2개의 전사 인자 YdeO 및 GadE를 암호화하는 ydeO 및 gadE 유전자의 전사를 양성으로 조절하고 YdeO는 gadE 유전자의 전사를 양성으로 조절하는 것으로 공지되어 있다(Masuda, N. and Church, G. M., Mol. Microbiol. 2003. 48(3):699-712. Regulatory network of acid resistance genes in Escherichia coli.; Ma, Z., Masuda, N., and Foster, J. W., J. Bacteriol. 2004. 186(21):7378-7389. Characterization of EvgAS-YdeO-GadE branched regulatory circuit governing glutamate-dependent acid resistance in Escherichia coli.). 그러나, evgA, gadE, 또는 ydeO 유전자의 발현이 증가된 미생물을 사용한 아미노산의 생산은 이전에 보고되지 않았다.
발명의 기재
본 발명의 목적은 L-아미노산을 효율적으로 생산할 수 있는 엔테로박테리아 세애 과의 세균 균주를 제공하고 또한 세균 균주를 사용하여 L-아미노산을 효율적으로 생산하기 위한 방법을 제공하는 것이다.
본 발명의 발명자는 상기된 문제점을 해결하기 위해 예의 연구하였고 이로써 L-아미노산 생산 능력은 evgA 유전자, gadE 유전자, 또는 ydeO 유전자중 하나 이상의 발현이 증가되도록 미생물을 변형시킴에 의해 개선될 수 있음을 발견하게 되었다. 이들 유전자는 EvgAS 2-성분 시스템에 관여하는 전사 인자를 암호화한다.
본 발명의 목적은 EvgAS 2-성분 시스템에 관여하는 전사 인자를 암호화하는 evgA 유전자, gadE 유전자, 또는 ydeO 유전자로부터 선택되는 하나 이상의 유전자의 발현이 증가되도록 변형된 L-아미노산 생산 능력을 갖는 엔테로박테리아세애 과의 세균을 배지에서 배양하는 단계; 배지에서 L-아미노산을 생산하고 축적시키는 단계 및 배지로부터 L-아미노산을 수거하는 단계를 포함하는, L-아미노산의 생산 방법을 제공하는 것이다.
본 발명의 추가의 목적은 당해 하나 이상의 유전자의 발현이 유전자 각각의 카피수를 증가시키거나 당해 유전자의 발현 조절 서열을 변형시킴에 의해 증가된, 상기된 바와 같은 방법을 제공하는 것이다.
본 발명의 추가의 목적은 당해 하나 이상의 유전자의 발현의 양이 센서 키나제를 암호화하는 evgS 유전자의 발현이 증가되도록 세균을 변형시켜 증가된, 상기된 바와 같은 방법을 제공하는 것이다.
본 발명의 추가의 목적은 evgA 유전자가 하기의 (a) 또는 (b)에 기재된 DNA인, 상기된 바와 같은 방법을 제공하는 것이다:
(a) 서열번호 23의 뉴클레오타이드 서열을 포함하는 DNA,
(b) 서열번호 23의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있고 전사 인자 활성을 갖는 단백질을 암호화하는 DNA.
본 발명의 추가의 목적은 gadE 유전자가 하기의 (c) 또는 (d)에 기재된 DNA인, 상기된 바와 같은 방법을 제공하는 것이다:
(c) 서열번호 27의 뉴클레오타이드 서열을 포함하는 DNA,
(d) 서열번호 27의 뉴클레오타이드 서열과 상보적인 단백질을 암호화하는 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있고 전사 인자 활성을 갖는 DNA.
본 발명의 추가의 목적은 ydeO 유전자가 하기의 (e) 또는 (f)에 기재된 DNA인, 상기된 바와 같은 방법을 제공하는 것이다:
(e) 서열번호 29의 뉴클레오타이드 서열을 포함하는 DNA,
(f) 서열번호 29의 뉴클레오타이드 서열과 상보적인 단백질을 암호화하는 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있고 전사 인자 활성을 갖는 DNA.
본 발명의 추가의 목적은 evgS 유전자가 하기의 (g) 또는 (h)에 기재된 DNA인, 상기된 바와 같은 방법을 제공하는 것이다:
(g) 서열번호 25의 뉴클레오타이드 서열을 포함하는 DNA,
(h) 서열번호 25의 뉴클레오타이드 서열과 상보적인 단백질을 암호화하는 뉴 클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있고 인 전달 활성을 갖는 DNA.
본 발명의 목적은 evgA 유전자가 하기의 (A) 또는 (B)에 기재된 단백질을 암호화하는, 상기된 바와 같은 방법을 제공하는 것이다:
(A) 서열번호 24의 아미노산 서열로 이루어진 단백질,
(B) 하나 이상의 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 24의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질.
본 발명의 추가의 목적은 gadE 유전자가 하기의 (C) 또는 (D)에 기재된 단백질을 암호화하는, 상기된 바와 같은 방법을 제공하는 것이다;
(C) 서열번호 28의 아미노산 서열로 이루어진 단백질,
(D) 하나 이상의 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 28의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질.
본 발명의 추가의 목적은 ydeO 유전자가 하기의 (E) 또는 (F)에 기재된 단백질을 암호화하는, 상기된 바와 같은 방법을 제공하는 것이다:
(E) 서열번호 30의 아미노산 서열로 이루어진 단백질,
(F) 하나 이상의 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 30의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질.
본 발명의 추가의 목적은 evgS 유전자가 하기의 (G) 또는 (H)에 기재된 단백질을 암호화하는, 상기된 바와 같은 방법을 제공하는 것이다:
(G) 서열번호 26의 아미노산 서열로 이루어진 단백질,
(H) 하나 이상의 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 26의 아미노산 서열을 포함하고 포스포트랜스퍼라제 활성을 갖는 단백질.
본 발명의 추가의 목적은 세균이 엔테로박테리아세애 과에 속하고 에스케리치아, 엔테로박터(Enterobacter), 판토에아(Pantoea), 클렙시엘라(Klebsiella), 및 세라티아(Serratia) 속으로 이루어진 그룹으로부터 선택되는 상기된 바와 같은 방법을 제공하는 것이다.
본 발명의 추가의 목적은 L-아미노산이 L-라이신, L-트레오닌, 및 L-트립토판으로 이루어진 그룹으로부터 선택되는 하나 이상의 아미노산인, 상기된 바와 같은 방법을 제공하는 것이다.
도 1은 온도 민감성 복제 오리진을 갖는, 플라스미드 벡터 pTS1의 작제를 도시한다.
이후부터 본 발명은 상세하게 설명된다.
1. 본 발명의 미생물
본 발명의 미생물은 EvgAS 2-성분 시스템 레귤론(rgulon)에 관여하는 전사 인자를 암호화하는 evgA, gadE, 또는 ydeO 유전자중 하나 이상의 발현이 증가되도록 변형된, L-아미노산 생산 능력을 갖는 엔테로박테리아세애 과의 미생물이다. 여기서, "L-아미노산 생산 능력"은 본 발명의 미생물이 배지에서 배양되는 경우 미생물의 배지 또는 세포로부터 수거될 수 있는 수준으로 L-아미노산을 축적하고 L-아미노산을 생산하는 능력을 의미한다. 본 발명의 미생물은 다수의 L-아미노산을 생산하는 능력을 가질 수 있다. 당해 미생물은 고유적으로 L-아미노산을 생산하는 능력을 갖거나 돌연변이 유발 또는 재조합 DNA 기술에 의해 변형되어 하기된 바와 같이 L-아미노산 생산 능력이 부여된 미생물일 수 있다.
또한, 문장 "유전자의 발현을 증가시키는"은 유전자의 전사 및/또는 해독이 증가됨을 의미한다.
특히, L-아미노산의 유형은 제한되지 않는다. 이의 예는 L-라이신, L-오르니틴, L-아르기닌, L-히스티딘, 및 L-시트룰린과 같은 염기성 아미노산; L-이소류신, L-알라닌, L-발린, L-류신, 및 글라이신과 같은 지방족 L-아미노산; L-트레오닌 및 L-세린과 같은 하이드록시모노아미노카복실산인 L-아미노산; L-프롤린과 같은 사이클릭 L-아미노산; L-페닐알라닌, L-티로신, 및 L-트립토판과 같은 방향족 L-아미노산; L-시스테인, L-시스틴, 및 L-메티오닌과 같은 황-함유 L-아미노산; L-글루탐산, 및 L-아스파르트산과 같은 산성 L-아미노산; 및 L-글루타민, 및 L-아스파라긴rhk 같은 산성 L-아미노산의 아미드 등을 포함한다. 특히, L-라이신, L-트레오닌, 및 L-트립토판이 바람직하다. 본 발명의 미생물은 2개 이상의 아미노산을 생산할 수 있다.
1-1. L-아미노산 생산 능력의 부여
하기는 L-아미노산 생산 능력이 부여되어 본 발명에 사용될 수 있는 미생물의 예와 함께. 미생물에 L-아미노산 생산 능력을 부여하는 방법에 대한 기재를 포함하지만 본 발명은 당해 미생물이 L-아미노산 생산 능력을 갖고 있는 이상 당해 미생물로 제한되지 않는다.
본 발명에 사용되는 미생물은 특히, 이것이 에스케리치아, 엔테로박터, 판토에아, 클렙시엘라, 세라티아, 에르위니아(Erwinia), 살모넬라(Salmonella), 모르가넬라(Morganella) 속 등과 같은 엔테로박테리아세애 과에 속하고 L-아미노산 생산 능력을 갖는 이상 제한되지 않는다. 구체적으로, NCBI(National Center for Biotechnology Information) 데이터베이스에 기재된 이의 분류와 함께 엔테로박테리아세애 과에 속하는 임의의 미생물이 사용될 수 있다(http://www.ncbi.nlm.nih.gov/htbin-post/Taxonomy/wgetorg?mode=Tree&id=1236&lvl=3&keep=1&srchmode=1&unlock). 본 발명의 미생물을 유도하기 위해 사용될 수 있는 엔테로박테리아세애 과 기원의 모균주로서, 특히 에스케리치아, 엔테로박터, 또는 판토에아 속에 속하는 미생물을 사용하는 것이 바람직할 수 있다.
본 발명의 세균을 수득하기 위해 사용되어야만 하는 에스케리치아 속 세균의 특정 모균주는 없지만 문헌[Neidhardt et]에 열거된 것들이 사용될 수 있다(Backmann, B. J. 1996. Derivations and Genotypes of some mutant derivatives of Escherichia coli K-12, p. 2460-2488. Table 1. In F. D. Neidhardt (ed.), Escherichia coli and Salmonella Cellular and Molecular Biology/Second Edition, American Society for Microbiology Press, Washington, D.C.). 하나의 예는 에스케리치아 콜리(Escherichia coli)이다. 에스케리치아 콜리의 특정 예는 K12의 야생형 균주로부터 유래하는 프로토타입인 에스케리치아 콜리 W3110 (ATCC 27325), 에스케리치아 콜리 MG1655 (ATCC 47076) 등이다.
이들은 예를 들어, 아메리칸 타입 컬쳐 콜렉션(American Type Culture Collection)(주소: P.O. Box 1549, Manassas, VA 20108, United States of America)로부터 입수할 수 있다. 이들은 각각의 세균 균주에 부여된 기탁번호를 사용하여 기관의 웹 사이트(참조 http:/www.atcc.org)로부터 입수할 수 있다. 각각의 세균 균주에 상응하는 기탁번호는 아메리칸 타입 컬쳐 콜렉션의 카탈로그에 부여되어 있다.
엔테로박터 속의 세균의 예는 엔테로박터 애글로메란스(Enterobacter agglomerans) 및 엔테로박터 아에로게네스(Enterobacter aerogenes)를 포함한다. 판토에아 속의 세균의 예는 판토에아 아나나티스(Pantoea ananatis)를 포함한다. 최근에는, 16S rRNA 뉴클레오타이드 서열 분석을 기초로, 엔테로박터 애글로메란스는 판토에아 애글로메란스, 판토에아 아나나티스 및 판토에아 스튜아르티(Pantoea stewartii)로서 재분류되었다. 본 발명에 대해, 세균이 엔테로박테리아세애 과로 분류되는 한 엔테로박터 또는 판토에아 속에 속하는 임의의 세균이 사용될 수 있다. 판토에아 아나나티스가 유전자 조작에 의해 개량되는 경우, 판토에아 아나나티스 균주 AJ13355 (FERM BP-6614), AJ13356 (FERM BP-6615), AJ13601 (FERM BP-7207), 또는 이의 변이체가 사용될 수 있다. 분리되는 경우, 당해 균주는 엔테로박터 애글로메란스로서 동정되고 기탁된다. 상기된 바와 같이, 16S rRNA 뉴클레오타이드 서열에 의한 분석은 이들이 판토에아 아나나티스로서 재분류되도록 하였다.
하기는 엔테로박테리아세애 과에 속하는 미생물에 L-아미노산 생산 능력을 부여하는 방법 및 이들 미생물에서 L-아미노산 생산 능력을 증가시키는 방법에 대한 기재이다.
L-아미노산 생산 능력을 부여하기 위해, 코리네형 세균 또는 에스케리치아 속의 세균의 개량에 통상적으로 사용되는 방법(문헌참조: "Amino Acid Fermentation", Gakkai Shuppan Center (Ltd.), 1st Edition, published May 30, 1986, pp. 77-100)이 적용될 수 있다. 당해 방법은 영양요구성 돌연변이, 유사체 내성 균주 또는 대사 조절 돌연변이의 획득 또는 L-아미노산 생합성 효소의 발현이 증진된 재조합 균주의 작제를 포함한다. 여기서, L-아미노산 생산 세균의 개량에 영양요구성 돌연변이, 유사체 내성 또는 대사 조절 돌연변이와 같은 하나 이상의 성질이 부여될 수 있다. 하나 이상의 L-아미노산 생합성 효소의 발현은 단독으로 또는 2개 이상의 조합으로 증진될 수 있다. 추가로, 영양요구성 돌연변이, 유사체 내성 또는 대사 조절 돌연변이와 같은 성질을 부여하는 기술은 생합성 효소를 증진시키는 기술과 조합될 수 있다.
L-아미노산 생산 능력을 갖는 영양요구성 돌연변이 균주, L-아미노산 유사체 내성 균주 또는 대사 조절 돌연변이 균주는 모균주 또는 야생형 균주를 통상적인 돌연변이 처리, 예를 들어, X-선 또는 UV 방사선으로의 노출, 또는 N-메틸-N'-니트로-N-니트로소구아니딘(NTG) 또는 에틸 메탄 설포네이트 (EMS) 등과 같은 돌연변이 유발제로의 처리에 적용함에 이어서 영양요구성 돌연변이, 유사체 내성 또는 대사 조절 돌연변이를 나타내고 또한 L-아미노산을 생산하는 능력을 갖는 것들을 선별함에 의해 수득될 수 있다.
L-라이신 생산 세균 및 이의 작제 방법에 대한 예는 하기와 같다.
예를 들어, L-라이신 생산 능력을 갖는 세균은 L-라이신 유사체 내성 균주 또는 대사 조절 돌연변이 균주를 포함한다. L-라이신 유사체의 예는 옥살라이신, 라이신 하이드록사메이트, S-(2-아미노에틸)-시스테인(AEC), -메틸 라이신, -클로로아프롤락탐 등을 포함하지만 이에 제한되지 않는다. 당해 라이신 유사체에 내성을 갖는 돌연변이체 균주는 에스테리치아 속에 속하는 세균을 통상적인 인공 돌연변이 유발 처리에 적용하여 수득될 수 있다. L-라이신 생산 세균의 예는 에스케리치아 콜리 AJ11442 균주(FERM BP-1543, NRRL B-12185;참조: JP56-18596A 및 미국 특허 제4,346,170호), 에스케리치아 콜리 VL611 균주(EP1016710) 등을 포함한다. 에스케리치아 콜리 WC196 균주(참조: WO96/17930) 가 또한 L-라이신 생산 세균으로서 사용될 수 있다. WC196 균주는 에스케리치아 콜리 K-12로부터 유래된 W3110 균주에 AEC 내성을 부여하여 개량되었다. 당해 균주는 에스케리치아 콜리 AJ13069로서 지정되었고 1994년 12월 6일자로 기탁기관[National Institute of Bioscience and Human Technology of the Agency of Industrial Science and Technology (현재, 국제 특허 유기체 기탁기관(International Patent Organism Depositary), National Institute of Advanced Industrial Science and Technology; Chuo 6, 1-1, Higashi 1-chome, Tsukuba-shi, Ibaraki-ken 305-8566, Japan]에 기탁번호 FERM P-14690로 기탁되었다. 이어서, 이것은 1995년 9월 29일자로 부다페스트 조약하에 국제 기탁 기관으로 이관되었고 기탁번호 FERM BP-5252를 부여받았다.
L-라이신-생산 세균은 또한 L-라이신 생합성 효소 활성을 증가시킴에 의해 작제될 수 있다. 당해 효소 활성의 증가는 세포내에서 효소를 암호화하는 유전자의 카피수를 증가시키거나 발현 조절 서열을 변형시킴에 의해 성취될 수 있다. L-라이신 생합성 효소를 암호화하는 유전자의 예는 디하이드로디피콜리네이트 신타제(dapA), 아스파르토키나제(lysC), 디하이드로디피콜리네이트 리덕타제(dapB), 디아미노피멜레이트 데카복실라제(lysA), 디아미노피멜레이트 데하이드로게나제(ddh) (WO96/40934, 미국 특허 제6,040,160호), 포스포에놀피루베이트 카복실라제(ppc)(60-87788A), 아스파르테이트 아미노트랜스퍼라제(aspC) (JP6-102028)B, 디아미노피멜레이트 에피머라제(dapF) (JP2003-135066A), 아스파르테이트 세미알데하이드 데하이드로게나제(asd) (WO00/61723)를 암호화하는 유전자, 및 디아미노피멜레이트 경로의 효소를 암호화하는 기타 유전자 뿐만 아니라 호모아코니테이트 하이드라타제를 암호화하는 유전자(JP2000-157276A) 및 아미노아디페이트 경로의 효소를 암호화하는 기타 유전자를 포함한다.
추가로, 야생형 디하이드로디피콜리네이트 신타제(DDPS) 및 아스파르토키나제(AK)는 L-라이신에 의한 피드백 억제에 의해 억제되는 것으로 공지되어 있고 따라서, dapA 및 lysC가 사용되는 경우, L-라이신에 의한 피드백 억제에 각각 내성인 디하이드로디피콜리네이트 신타제 및 아스파르토키나제를 암호화하는 돌연변이 유전자를 사용하는 것이 바람직할 수 있다(EP 0733710, US5,932,453).
L-라이신에 의한 피드백 억제에 내성인 돌연변이 디하이드로디피콜리네이트 신타제를 암호화하는 DNA의 예는 118번 히스티딘 잔기가 티로신으로 치환된 아미노산 서열을 갖는 DDPS를 암호화하는 DNA를 포함한다(U.S. 5,661,012 및 6,040,160). 추가로, L-라이신에 의한 피드백 억제에 내성인 돌연변이 AK를 암호화하는 DNA의 예는 352번 트레오닌 잔기가 이소류신으로 치환된 아미노산 서열을 갖는 AK를 암호화하는 DNA를 포함한다(U.S. 5,661,012 및 6,040,160). 이들 돌연변이 DNA는 PCR등을 사용한 부위 지시된 돌연변이 유발에 의해 수득될 수 있다.
L-라이신 생합성 효소를 암호화하는 유전자를 숙주로 도입함에 의해 L-라이신 생산 능력을 부여하기 위한 기술의 예는 다음과 같다. 즉, 재조합 DNA는 L-라이신 생합성 유전자를 암호화하는 단편을 선택된 숙주 미생물에서 작용하는 벡터, 바람직하게는, 다중 카피 벡터와 연결시킴에 의해 작제되고 숙주는 당해 재조합 벡터로 형질전환시킨다. 형질전환으로 인해, 숙주 세포에서 L-라이신 생합성 효소를 암호화하는 유전자의 카피수는 증가하여 발현이 증가하고 결국 효소 활성이 증가한다.
L-라이신 생합성 효소를 암호화하는 유전자는 특히 이들이 숙주 미생물에서 발현될 수 있는 이상, 특정되지 않는다. 당해 예는 에스케리치아 콜리로부터 유래하는 유전자 및 세균의 코리네형 그룹으로부터 유래하는 유전자를 포함한다. 에스케리치아 콜리 및 코리네박테리움 글루타미쿰(Corynebacterium glutamicum)의 전체 게놈 서열이 보고되었기 때문에 당해 유전자의 뉴클레오타이드 서열을 기초로 프라이머를 합성하고 에스케리치아 콜리 K12 등과 같은 미생물의 게놈 DNA를 주형으로서 사용하는 PCR에 의해 당해 유전자를 수득할 수 있다.
당해 유전자를 클로닝하기 위해, 엔테로박테리아세애 과에서 자발적으로 복제하는 플라스미드를 사용할 수 있다. 당해 예는 pBR322, pTWV228(Takara Bio Inc.), pMW119 (Nippon Gene Co., Ltd.), pUC19, pSTV29 (Takara Bio Inc.), RSF1010 (Gene, 75:271-288 (1989)) 등을 포함한다. 이들 외에도, 파아지 벡터가 또한 사용될 수 있다.
표적 유전자를 상기 언급된 벡터에 연결하기 위해, 표적 유전자를 포함하는 DNA 단편의 말단과 일치되도록 벡터를 제한 효소로 분해시킨다. 일반적으로 연결은 T4 DNA 리가제와 같은 리가제로 수행한다. 표적 유전자는 각각 별도의 벡터상에 위치하거나 동일한 벡터상에 위치할 수 있다. 당업자에게 공지된 통상적인 방법은 게놈 DNA를 제조하고, PCR을 수행하고 플라스미드 DNA를 제조하고, 형질전환시키고, 올리고뉴클레오타이드 프라이머 등을 디자인하는 것 뿐만 아니라 DNA를 분해하고 연결시키는데 사용될 수 있다. 이들 방법은 문헌[Sambrook, J., and Russell, D.W. Molecular Cloning A Laboratory Manual/Third Edition. New York: Cold Spring Harbor Laboratory Press (2001), etc.]에 기재되어 있다. 적절한 형질전환 효율을 성취하는 임의의 방법을 사용하여 상기된 바와 같이 제조된 재조합 DNA를 숙주 미생물로 도입할 수 있다. 이의 예는 전기천공(Can. J. Microbiol. 43:197-201 (1997))을 포함한다. 당해 방법을 사용하여 제조되는 플라스미드의 예는 dapA, dapB, 및 LysC 유전자를 포함하는 Lys-생산 플라스미드 pCABD2를 포함한다(WO 01/53459).
L-라이신 생합성 효소를 암호화하는 유전자의 발현 증진은 또한 표적 유전자의 다중 카피를 미생물의 게놈 DNA에 도입하여 성취될 수 있다. 다중 카피의 표적 유전자는 상동성 재조합에서 표적으로서 게놈 DNA 상에 다중 카피로 존재하는 서열을 사용하여 미생물의 게놈 DNA로 도입될 수 있다. 상동성 재조합을 사용한 유전자 치환을 기초로 하는 돌연변이의 당해 부위 특이적 도입은 보고되었다. 온도 민감성 복제 오리진을 포함하는 선형 DNA 또는 플라스미드는 당해 방법에 사용될 수 있다(미국 특허 제6,303,383호 및 제JP05-007491A호). 트랜스포존 요소 말단에 존재하는 반복 DNA 및 역위 반복체는 게놈 DNA 상에 다중 카피로 존재하는 서열로서 사용될 수 있다. L-라이신 생합성 유전자는 게놈 고유의 유전자와 함께 반복적으로 연결될 수 있거나 게놈상의 비필수 영역 또는 결실되었을 때 L-라이신 수율을 개선시키는 유전자 영역으로 도입될 수 있다. 또는, 미국 특허 제5,595,889호에 기재된 바와 같이, 표적 유전자는 또한 트랜스포존상에 위치시켜 전달되도록 함에 의해 다중 카피를 게놈 DNA상으로 도입할 수 있다. 어느 방법을 사용하든, 형질전환체내 표적 유전자의 카피수는 증가하여 L-라이신 생합성의 효소 활성은 증가한다.
상기된 유전자 증폭 뿐만 아니라, L-라이신 생합성 효소 활성의 증가는 프로모터 등과 같은, 표적 유전자의 발현 조절 서열을 보다 강한 것으로 대체하여 성취할 수 있다(참조: JP1-215280A). 예를 들어, lac 프로모터, trp 프로모터, trc 프로모터, tac 프로모터, araBA 프로모터, 람다 파아지 PR 프로모터, PL 프로모터, tet 프로모터, T7 프로모터, ψ10 프로모터 등이 강한 프로모터로서 공지되어 있다. 이들 프로모터로의 대체는 표적 유전자의 발현을 증진시키고 따라서 효소 활성을 증가시킨다. 강한 프로모터의 예 및 프로모터의 강도를 평가하기 위한 방법은 문헌[참조: Goldstein et al. (Biotechnol. Annu. Rev., 1, 105-128, (1995) Prokaryotic promoters in biotechnology.) 등에 기재되어 있다.
표적 효소의 활성 증가는 또한 표적 효소를 암호화하는 유전자 발현 조절에 관여하는 요소, 예를 들어, 오퍼레이터 또는 리프레서를 변형시켜 성취할 수 있다(Hamilton et al, J. Bacteriol. 171:4617-4622 (1989)). WO 00/18935에 기재된 바와 같이, 표적 유전자의 프로모터 영역내 여러 염기를 대체하여 당해 프로모터를 변형시키고 강화시킬 수 있다. 추가로, 리보솜 결합 부위(RBS)와 개시 코돈 사이의 스페이서, 특히 개시 코돈 바로 상부의 서열내의 여러 뉴클레오타이드를 대체하는 것이 mRNA 해독 효율에 대해 강한 효과를 나타내는 것으로 공지되어 있다. 따라서, 이들 영역을 변형시켜 전사 효율을 증가시킬 수 있다. 프로모터 등과 같은 표적 유전자의 발현 조절 영역은 프로모터 프로브 벡터 및 유전자 분석 소프트웨어(예를 들어, GENETYX (GENETYX CORPORATION)) 등에 의해 결정될 수 있다. 표적 유전자의 발현은 당해 프로모터를 대체하거나 변형시켜 증가시킬 수 있다. 발현 조절 서열의 대체는 예를 들어, 온도 민감성 플라스미드를 사용하는 상기된 유전자 대체에서와 동일한 방식으로 수행할 수 있다. 레드 구동(The Red-driven) 통합 방법(WO2005/010175)이 또한 사용될 수 있다.
추가로, L-아미노산 생산 세균에서, L-아미노산의 생합성 경로로부터 분기되는, 표적 L-아미노산 이외의 화합물을 생성하는 반응을 촉매하는 효소의 활성 또는 L-아미노산의 합성 또는 축적에 음성 효과를 갖는 효소의 활성은 감소시키거나 결실시킬 수 있다. L-라이신 생산에서, 당해 효소는 호모세린 데하이드로게나제(thrA), 라이신 데카복실라제(cadA, ldcC), 및 말산 효소(sfcA, b2463)를 포함한다. 당해 감소되거나 결핍된 효소 활성을 갖는 균주는 문헌[WO 95/23864, WO96/17930, WO2005/010175, 등]에 기재되어 있다.
당해 효소의 활성을 감소시키거나 결실시키기 위해, 세포내 당해 효소 활성을 감소시키거나 결실시키는 돌연변이가, 통상의 돌연변이 유발 방법 또는 유전자 재조합 기술을 사용하여 게놈상의 상기 언급된 효소의 유전자로 도입될 수 있다. 상기 돌연변이의 도입 방법은 예를 들어, 게놈상에 효소를 암호화하는 유전자를 유전자 재조합으로 결실시키거나 프로모터 또는 샤인-달가노(Shine-Dalgarno (SD)) 서열 등과 같은 발현 조절 서열을 변형시켜 성취할 수 있다. 이것은 또한 게놈상의 효소를 암호화하는 영역에 아미노산 대체(미스센스 돌연변이) 또는 종료 코돈(넌센스 돌연변이)을 도입하거나, 1 또는 2개의 염기를 부가하거나 결실시키는 판독 전이(frameshift) 돌연변이를 도입하거나 유전자 또는 전체 영역의 일부를 결실시킴에 의해 성취할 수 있다(J. Biol. Chem. 272:8611-8617 (1997)). 또한, 효소 활성은 일부 또는 전체 암호화 영역이 결실된 돌연변이 효소를 암호화하는 유전자를 작제함에 이어서 당해 유전자로 게놈상의 정상의 유전자를 상동성 재조합에 의해 대체시키거나 트랜스포존 또는 IS 요소를 당해 유전자에 도입함에 의해 감소되거나 결실될 수 있다. 하기의 방법을 사용하여 유전자 재조합에 의해 상기 언급된 효소 활성을 감소시키거나 결실시키는 돌연변이를 도입할 수 있다. 표적 유전자를 함유하는 분리된 DNA를 돌연변이시켜 수득한 돌연변이 유전자가 정상적으로 기능하는 효소를 생성하지 못하도록 한다. 이어서, 엔테로박테리아세애 과에 속하는 미생물은 돌연변이된 유전자를 함유하는 DNA로 형질전환시켜 게놈상에 돌연변이된 유전자와 표적 유전자간에 재조합이 유발되도록 한다. 따라서, 게놈상의 표적 유전자는 돌연변이된 유전자로 대체될 수 있다. 이러한 종류의 상동성 재조합을 사용한 유전자 대체를 위해, 소위 "레드 구동 통합"으로 불리우는 방법(Datsenko, K. A, and Wanner, B. L. Proc. Natl. Acad. Sci. U S A. 97:6640-6645 (2000))과 같은, 선형 DNA를 사용하는 방법, 레드 구동 통합 방법과 파아지 익시브(excisive) 시스템을 조합한 방법(Cho, E. H., Gumport, R. I., Gardner, J. F. J. Bacteriol. 184: 5200-5203 (2002)) (참조: WO2005/010175) 등이 있고 온도 민감성 복제 오리진을 함유하는 플라스미드를 사용하는 방법이 있다(미국 특허 제6,303,383호; 미국 특허 제5,616,480호). 상기된 바와 같이 상동성 재조합을 사용한 유전자 대체에 의한 돌연변이의 당해 부위 특이적 도입은 또한 선택된 숙주에서 복제 능력을 갖지 않는 플라스미드를 사용하여 수행할 수 있다.
L-라이신 생합성에 관여하는 효소의 활성을 증가시키는 상기 언급된 방법 및 효소 활성을 저하시키는 방법은 또한 기타 L-아미노산 생산 세균을 개량하는데 사용될 수 있다. 기타 L-아미노산 세균을 개량하기 위한 방법은 하기에 기재되어 있다.
본 발명에 바람직하게 사용되는 L-트립토판 생산 세균은 안트라닐레이트 신타제, 포스포글리세레이트 데하이드로게나제 또는 트립토판 신타제 효소중 하나 이상의 활성이 증진된 세균을 포함한다. 안트라닐레이트 신타제 및 포스포글리세레이트 데하이드로게나제 둘다는 L-트립토판 및 L-세린에 의한 피드백 억제를 받기 때문에, 당해 효소의 활성은 탈감작 돌연변이 효소를 보유함에 의해 증가될 수 있다. 예를 들어, 안트라닐레이트 신타제 유전자(trpE) 및/또는 포스포글리세레이트 데하이드로게나제 유전자(serA)를 돌연변이시켜 피드백 억제를 차단함에 이어서 당해 돌연변이 유전자를 엔테로박테리아세애 과에 속하는 미생물에 도입함에 의해 탈감작 효소를 갖는 세균을 수득할 수 있다(미국 특허 제5,618,716호, 미국 특허 제6,180,373호). 이러한 종류의 세균의 특정 예는 탈감작된 포스포글리세레이트 데하이드로게나제를 암호화하는 돌연변이 serA를 갖는 플라스미드 pGH5를, 탈감작된 안트라닐레이트 신타제를 보유하는 에스케리치아 콜리 SV164로 도입함에 의해 수득된 형질전환체를 포함한다(WO94/08301). 균주 SV164는 탈감작된 안트라닐레이트 신타제를 암호화하는 유전자를, 에스케리치아 콜리 KB862(DSM7196)의trpE 결핍 균주로 도입함에 의해 수득된다(참조: WO94/08031).
트립토판 오페론을 함유하는 재조합 DNA로 형질전환된 세균이 또한 바람직할 수 있다. 특정 예는 탈감작된 안트라닐레이트 신타제를 암호화하는 유전자를 포함하는 트립토판 오페론으로 형질전환된 에스케리치아 콜리를 포함한다 (JP57-71397A, JP62-244382A, U.S. Patent No. 4,371,614). 추가로, 트립토판 신타제(trpBA)를 암호화하는 유전자의 발현을 증진시킴에 의해 L-트립토판을 생산하는 능력을 증진시키거나 부여할 수 있다. 트립토판 신타제는 각각 trpA 및 trpB에 의해 암호화된 서브유니트로 이루어진다. trpA의 뉴클레오타이드 서열은 서열번호 13에 나타내고 trpB의 뉴클레오타이드 서열은 서열번호 15에 나탄낸다.
결핍된 trpR, 트립토판 오페론 리프레서를 갖는 균주 및 돌연변이 trpR를 갖는 균주가 또한 바람직할 수 있다(미국 특허 제4,371,614호, WO2005/056776).
또 다른 바람직한 L-트립토판-생산 세균은 말레이트 신타제, 이소시트레이트 리아제, 이소시트레이트 데하이드로게나제/포스파타제 오페론(ace 오페론)이 구조적으로 발현되거나 당해 오페론의 발현이 증진된 세균이다. 특히, ace 오페론의 프로모터가 리프레서 iclR에 의해 억제되지 않거나 iclR에 의한 억제가 제거된 것이 바람직할 수 있다. 당해 세균은 iclR 유전자를 파괴하거나 ace 오페론의 발현 조절 서열을 변형시킴에 의해 수득될 수 있다. 에스케리치아 콜리의 iclR 유전자는 서열번호 5로서 나타낸다. ace 오페론의 발현이 증진된 세균은 ace 오페론을 함유하는 DNA를 강한 프로모터에 연결하고 재조합 DNA를 플라스미드를 사용하거나 상동성 재조합에 의해 세포로 도입하거나 트랜스포존을 사용하여 ace 오페론의 카피수를 증폭시킴에 의해 수득될 수 있다. ace 오페론에 포함되는 유전자는 aceB, aceA, 및 aceK를 포함한다. aceB , aceA 및 aceK의 뉴클레오타이드 서열은 각각, 서열번호 9, 7 및 11에 나타낸다.
L-트립토판 생산 세균의 예는 L-페닐알라닌 및 L-티로신 영양요구성인 에스케리치아 콜리 AGX17 (pGX44) [NRRL B-12263], 및 트립토판 오페론 함유 플라스미드 pGX50을 포함하는 AGX6 (pGX50) aroP [NRRL B-12264]을 포함한다(문헌참조: 미국 특허 제4,371,614호). 이들 균주는 기관[Agricultural Research Service Culture Collection, National Center for Agricultural Utilization Research (address: Peoria, Illinois 61604, USA)]에서 입수할 수 있다.
L-트립토판, L-페닐알라닌 및 L-타이로신은 모두 방향족 아미노산이고 공통된 생합성 경로를 갖는다. 이들 방향족 아미노산에 대한 생합성 효소를 암호화한느 유전자의 예는 데옥시아라비노-헵툴로소네이트 포스페이트 신타제(aroG), 3-데하이드로퀴네이트 신타제(aroB), 시키메이트 데하이라타제, 시키메이트 키나제(aroL), 5-에놀피루빌시키메이트-3-포스페이트 신타제(aroA), 및 코리스메이트 신타제(aroC)(EP763127)를 포함한다. 따라서, 플라스미드 또는 게놈상에 당해 효소를 암호화하는 유전자를 다중 카피함에 의해, 방향족 아미노산 생산 능력은 개선될 수 있다. 당해 유전자가 티로신 리프레서(tyrR)에 의해 조절될 수 있다는 것은 공지되어 있고 따라서 방향족 아미노산 생합성의 효소는 또한 tyrR 유전자를 결실시킴에 의해 증가될 수 있다(문헌참조: EP763127).
L-페닐알라닌 생산 미생물의 예는 tyrA, tyrR 결핍된 에스케리치아 콜리 AJ12739 (tyrA::Tn10, tyrR) (VKPM B-8197) 및 yddG 및 yedA와 같은 페닐알라닌 분비 단백질을 암호화하는 유전자가 증폭된 균주를 포함한다(WO03/044192; US2003/0148473A1).
본원에 사용된 L-트레오닌 생산 세균은 바람직하게 L-트레오닌 생합성 효소가 증진된 엔테로박테리아세애에 속하는 미생물이다. 당해 유전자의 예는 아스파르토키나제 III (lysC), 아스파르테이트-세미알데하이드 데하이드로게나제(asd), 아스파르토키나제 I (thr 오페론에 포함된 thrA), 호모세린 키나제(thrB), 및 트레오닌 신타제(thrC)를 암호화하는 유전자를 포함한다. 2개 이상의 당해 유전자가 도입될 수 있다. L-트레오닌 생합성 유전자는 트레오닌 분해가 억제된 에스케리치아 속의 세균에 도입될 수 있다. 당해 세균의 예는 트레오닌 데하이드로게나제 활성이 결실된 TDH6 균주(미국 특허 제6,960,455호) 등을 포함한다.
L-트레오닌 생합성 경로의 몇몇 효소의 활성은 L-트레오닌에 의해 억제된다. 따라서, L-트레오닌 생산 세균을 작제하기 위해서는, L-트레오닌에 의한 피드백 억제를 받지 않도록 L-트레오닌 생합성 효소를 변형시키는 것이 바람직할 수 있다. 상기 언급된 thrA, thrB, 및 thrC 유전자는 감쇠인자(attenuator) 구조를 함유하는 트레오닌 오페론을 구성한다. 이의 발현은 당해 감쇠에 의해 억제된다. 또한, 트레오닌 오페론의 발현은 배양동안에 존재하는 이소류신 및 트레오닌에 의해 억제된다. 트레오닌 오페론의 변형은 감쇠 영역 또는 감쇠인자내 리더 서열을 제거함에 의해 성취될 수 있다(문헌참조: Lynn, S. P., Burton, W. S., Donohue, T. J., Gould, R. M., Gumport, R. I., and Gardner, J. F. J. Mol. Biol. 194:59-69 (1987); WO02/26993; WO2005/049808).
고유 프로모터는 트레오닌 오페론의 상부에 존재한다. 프로모터는 비고유 프로모터로 대체될 수 있다(참조: WO 98/04715). 또한, 트레오닌 오페론은 트레오닌 생합성에 관여하는 유전자의 발현이 람파 파아지의 리프레서 및 프로모터에 의해 조절되도록 구성될 수 있다(참조: EP0593792). 또한, L-트레오닌에 의한 피드백 억제를 차단하기 위해, 에스케리치아의 세균은 α-아미노-β하이드록시발레르산(AHV) 내성 균주를 선별함에 의해 변형될 수 있다.
L-트레오닌에 의한 피드백 억제가 차단되도록 변형된 트레오닌 오페론의 카피수가 숙주에서 증가되거나 강한 프로모터에 연결되어 오페론의 발현이 증진되는 것이 바람직하다. 또한, 플라스미드를 사용하여 카피수를 증폭시키는 것 뿐만 아니라 카피수는 트랜스포존, Mu-파아지등을 사용하여 게놈상에 트레오닌 오페론을 도입함에 의해 증가될 수 있다.
아스파르토키나제 III 유전자(lysC)에 대해, L-라이신에 의한 피드백 억제가 차단되도록 변형된 유전자를 사용하는 것이 바람직할 수 있다. 피드백 억제를 차단하도록 변형된 lysC 유전자는 미국 특허 제5,932,453호에 기재된 방법을 사용하여 수득될 수 있다.
L-트레오닌 생합성 효소 외에도, 당분해 시스템, TCA 사이클 및 호흡 연쇄 반응과 관련된 유전자, 당해 유전자의 발현을 조절하는 유전자 및 당의 흡수를 유도하는 유전자를 증진시키는 것이 바람직할 수 있다. L-트레오닌 생산에 효과적인 당해 유전자의 예는 트랜스하이드로게나제(pntAB) (EP733712), 포스포에놀피루베이트 카복실라제(ppc)(WO95/06114)를 암호화하는 유전자, 포스포에놀피루베이트 신타제 유전자(pps) (EP877090), 및 코리네형 세균 또는 바실러스(Bacillus)속의 세균의 피루베이트 카복실라제를 암호화하는 유전자를 포함한다(WO99/18228, EP1092776).
또한, L-트레오닌에 대한 내성을 부여하는 유전자 및/또는 L-호모세린에 대한 내성을 부여하는 유전자 또는 숙주에게 L-트레오닌 내성 및/또는 L-호모세린 내성을 부여하는 유전자의 발현을 증진시키는 것이 바람직할 수 있다. 당해 유전자의 예는 rhtA 유전자(Res. Microbiol. 154:123-135 (2003)), rhtB 유전자(EP0994190), rhtC 유잔지(EP1013765), 및 yfiK 및 yeaS 유전자(EP1016710)를 포함한다. 숙주에게 L-트레오닌 내성을 부여하는 방법과 관련하여 문헌[EP0994190, WO90/04636]을 참조한다.
L-트레오닌 생산 세균의 또 다른 예는 에스케리치아 콜리 VKPM B-3996 균주이다(참조: 미국 특허 제5,175,107호). 당해 VKPM B-3996 균주는 1987년 4월 7일자로 기탁기관[Russian National Collection of Industrial Microorganisms (VKPM), GNII Genetika (주소: Russia, 117545 Moscow, 1 Dorozhny proezd. 1)]에 기탁번호 VKPM B-3996으로 기탁되었다. 또한, VKPM B-3996 균주는 트레오닌 생합성 유전자(트레오닌 오페론: thrABC)를, 스트렙토마이신 내성 마커를 포함하는 다양한 숙주 범위 벡터 플라스미드 pAY32에 삽입함에 의해 수득된 플라스미드pVIC40 (WO90/04636)를 포함한다(문헌참조: Chistorerdov, A. Y., and Tsygankov, Y. D. Plasmid, 16, 161-167 (1986)). pVIC40상의 thrA 유전자, 및 아스파르토키나제 I-호모세린 데하이드로게나제 I의 L-트레오닌에 의한 피드백 억제는 탈감작되었다.
L-트레오닌 생산 세균의 추가의 바람직한 예는 에스케리치아 콜리 VKPM B-5318 균주이다(참조: EP0593792). VKPM B-5318 균주는 1990년 5월 3일자로 기탁기관[Russian National Collection of Industrial Microorganisms (VKPM), GNII Genetika (주소: Russia, 117545 Moscow, 1 Dorozhny proezd. 1)]에 기탁번호 VKPM B-5318로 기탁되었다. 당해 VKPM B-5318 균주는 이소류신에 대해 비영양요구성이고 트레오닌 생합성, 즉, 감쇠인자 및 고유 전사 조절 영역이 결실된 트레오닌 오페론이 온도 민감성 CI 리프레서, PR 프로모터 및 람파 파아지의 Cro 단백질의 N-말단의 하부에 위치하고 트레오닌 생합성에 관여하는 유전자의 발현이 람파 파아지 리프레서 및 프로모터에 의해 조절되도록 구성된 재조합 플라스미드 DNA를 포함한다.
본 발명에 사용되는 L-글루탐산 생산 세균의 예는 L-글루탐산 생합성에 관여하는 효소를 암호화하는 유전자의 발현이 증가되도록 변형된 엔테로박테리아세애 과에 속하는 미생물을 포함한다. L-글루탐산 생산에 관여하는 효소는 글루타메이트 데하이드로게나제(이후부터 또한 "GDH"로서 언급됨), 글루타민 신테타제, 글루타메이트 신타제, 이소시트레이트 데하이드로게나제, 아코니테이트 하이드라타제, 시트레이트 신타제(이후부터, 또한 "CS"로서 언급됨), 포스포에놀피루베이트 카복실라제(이후부터 또한 "PEPC"로서 언급됨), 피루베이트 카복실라제, 피루베이트 데하이드로게나제, 피루베이트 키나제, 포스포에놀피루베이트 신타제, 에놀라제, 포스포글리세롤뮤타제, 포스포글리세레이트 키나제, 글리세럴알데하이드-3-포스페이트 데하이드로게나제, 트리오스 포스페이트 이소머라제, 프럭토스-바이포스페이트 알돌라제, 포스포프럭토키나제, 글루코스포스페이트 이소머라제등을 포함한다. 이들 효소중에서, CS, PEPC, 및 GDH중 하나 이상이 바람직할 수 있고 3개 모두가 보다 바람직할 수 있다.
상기된 방법을 사용하여 시트레이트 신타제 유전자, 포스포에놀피루베이트 카복실라제 유전자 및/또는 글루타메이트 데하이드로게나제 유전자의 발현이 증진되도록 변형된 엔테로박테리아세애 과에 속하는 미생물의 예는 미국 특허 제6,197,559호 및 제6,331,419호, EP0999282에 기재되어 있다.
추가로, 6-포스포글루코네이트 데하이드라타제 또는 2-케토-3-데옥시-6-포스포글루코네이트 알돌라제중 어느 하나 또는 둘다의 활성이 증가되도록 변형된 엔테로박테리아세애 과에 속하는 미생물이 또한 사용된다(EP1352966).
L-글루탐산을 생산하는 능력을 갖는 엔테로박테리아세애 과의 미생물로서, L-글루탐산의 생합성 경로부터 분기되는 L-글루탐산 이외의 화합물을 생산하는 반응을 촉매하는 효소의 활성이 결실되거나 감소된 세균이 또한 사용될 수 있다. 당해 효소의 예는 2-옥소글루타레이트 데하이드로게나제, 이소시트레이트 리아제, 포스페이트 아세틸트랜스퍼라제, 아세테이트 키나제, 아세토하이드록시 산 신타제, 아세토락테이트 신타제, 포르메이트 아세틸트랜스퍼라제, 락테이트 데하이드로게나제, 글루타메이트 데카복실라제, 1-피롤린 데하이드로게나제 등을 포함한다. 물론, 2-옥소글루타레이트 데하이드로게나제를 감소시키거나 결실시키는 것이 특히 바람직할 수 있다.
엔테로박테리아세애 과에 속하는 미생물에서 2-옥소글루타레이트 데하이드로게나제의 활성을 결실시키거나 감소시키는 방법은 미국 특허 제5,573,945호, 미국 특허 제6,197,559호, 및 미국 특허 제6,331,419호에 기재되어 있다. 구체적으로, 2-옥소글루타레이트 데하이드로게나제의 활성이 결실되거나 감소된 엔테로박테리아세애 과에 속하는 미생물의 예는 하기의 미생물을 포함한다:
판토에아 아나나티스 AJ13601 (FERM BP-7207)
클렙시엘라 플란티콜라 AJ13410 strain (FERM BP-6617)
에스케리치아 콜리 AJ12949 (FERM BP-4881)
본 발명에 사용하기 위해 바람직한 L-히스티딘 생산 세균의 예는 에스케리치아 콜리 FERM P-5038 및 FERM P-5048를 포함한다. 이들 균주는 L-히스티딘 생합성에 관여하는 유전자 정보를 포함하는 벡터를 포함한다(JP56-005099A). 기타 예는 아미노산 배출 유전자 Rht로 형질전환된 세균 균주(EP1016710), 및 설파구아니딘, D, L-1,2,4-트리아졸-3-알라닌, 및 스트렙토마이신 등에 내성인 에스케리치아 콜리 80(VKPM B-7270, 러시아 특허 제2119536호)을 포함한다.
L-히스티딘 생합성 경로 효소를 암호화하는 유전자가 발현되는 미생물이 사용될 수 있다. 당해 유전자의 예는 ATP 포스포리보실트랜퍼라제(hisG)를 암호화하는 유전자, 포스포리보실 AMP 사이클로하이드롤라제 유전자(hisI), 포스포리보실-ATP 피로포스포하이드롤라제(hisIE), 포스포리보실포름이미노-5-아미노이미다졸 카복스아미드 리보타이드 이소머라제(hisA), 아미도트랜스퍼라제 유전자 (hisH), 히스티디놀 포스페이트 아미노트랜스퍼라제(hisC), 히스티디놀 포스파타제(hisB), 및 히스티딘올 데하이드로게나제 유전자(hisD) 등을 포함한다.
본 발명의 바람직한 L-시스테인 생산 세균은 시스타티오닌 β-리아제의 활성이 감소된 세균(JP2003-169668A), 및 세린 아세틸트랜스퍼라제를 보유하지만 L-시스테인에 의한 피드백 억제가 감소되거나 제거된 에스케리치아 속의 세균(JP11-155571A)을 포함한다.
본 발명의 바람직한 L-프롤린 생산 세균은 3,4-데하이드록시프롤린 및 아제티딘-2-카복실레이트에 내성인 에스케리치아 콜리 702 (VKPMB-8011) 및 ilvA가 결핍되고 균주 702(JP2002-300874A)로부터 유래하는 702 ilvA 균주(JP2002-300874A)를 포함한다.
L-아르기닌 생산 세균의 예는 α-메틸메티오닌, p-플루오로페닐알라닌, D-아르기닌, 아르기닌 하이드록삼산, S-(2-아미노에틸)-시스테인, α-메틸세린, β-2-티에닐알라닌 또는 설파구아니딘에 내성인 에스케리치아 콜리 돌연변이 균주( JP56-106598A)등을 포함한다. 에스케리치아 콜리 237 균주는 L-아르기닌에 의한 피드백 억제에 내성인 돌연변이를 갖고 고활성의 N-아세틸 글루타메이트 신타제를 보유하는 L-아르기닌 생산 세균이고 또한 L-아르기닌 생산 균주가 바람직할 수 있다(러시 특허원 제2000117677호). 당해 균주 VKPM B-7925은 2000년 4월 10일자로 기탁기관[Russian National Collection of Industrial Microorganisms (VKPM), GNII Genetika]에 기탁되었고 2001년 5월 18일자로 부다페스트 조약하에 국제 기탁물로 이관되었다. 237 균주의 유도체이고 아세트산 축적 능력이 개선된 L-아르기닌 생산 세균인 에스케리치아 콜리 382 균주가 또한 사용될 수 있다(JP2002-017342A). 에스케리치아 콜리 382 균주 VKPM B-7926은 2000년 4월 10일자로 기탁기관[Russian National Collection of Industrial Microorganisms (VKPM)]에 기탁되었다.
또한, L-아르기닌 생산 능력을 갖는 미생물로서, L-아르기닌 생합성에 관여하는 효소를 암호화하는 유전자의 발현이 개선된 미생물이 사용될 수 있다. L-아르기닌 생합성 효소의 예는 N-아세틸 글루타메이트 신타제(argA), N-아세틸-글루타밀-포스페이트 리덕타제(argC), 오르니틴 아세틸트랜스퍼라제(argJ), N-아세틸 글루타메이트 키나제(argB), 아세틸 오르니틴 트랜스아미나제(argD), 아세틸 오르니틴 데아세틸라제(argE), 오르니틴 카바모일 트랜스퍼라제(argF), 아르기닌숙시네이트 신타제(argG), 아르기닌이노숙시네이트 리아제 (argH), 및 카바모일 포스페이트 신타제 (carAB)중 하나 이상이다. 각각의 효소가 지명된 후, 이를 암호화하는 유전자 명칭은 괄호안에 주어진다. L-아르기닌 피드백 억제가 야생형에서 15번 내지 19번 위치에 상응하는 아미노산 서열의 치환에 의해 제거된 N-아세틸 글루타메이트 신타제 유전자(argA)의 돌연변이를 사용하는 것이 바람직할 수 있다(EP1170361).
사용될 수 있는 L-류신-생산 세균은 ilvE 유전자에 의해 암호화된 측쇄 아미노산 트랜스아미나제가 불활성화되고 tyrB 유전자에 의해 암호화된 방향족 아미노산 트랜스아미나제의활성이 증진된 에스케리치아 콜리 속의 세균(EP1375655A), 4-아잘류신 또는 5,5,5-트리플루오로류신에 내성인 에스케리치아 콜리 H-9068 균주 (ATCC21530), 에스케리치아 콜리 H-9070 균주 (FERM BP-4704), 에스케리치아 콜리 H-9072 균주 (FERM BP-4706) (미국 특허 제5,744,331호), L-류신에 의한 이소프로필말레이트 신타제 피드백 억제가 탈감작된 에스케리치아 콜리(EP1067191), β-2 티에닐알라닌 및 β- 하이드록실류신에 내성인 에스케리치아 콜리 AJ11478(미국 특허 제5,763,231호) 등을 포함한다.
L-이소류신 생산 세균은 6-디메틸 아미노퓨린 내성 에스케리치아 콜리 돌연변이 균주(JP5-304969A), L-이소류신 하이드록사메이트-내성 에스케리치아 콜리 돌연변이 균주(JP5-130882A), 티아이소류신 내성 에스케리치아 콜리 돌연변이 균주(JP5-130882A), DL-에티오닌-내성 에스케리치아 콜리 돌연변이 균주(JP5-130882A), 및 아르기닌 하이드록사메이트 내성 돌연변이 균주(JP5-130882A)를 포함한다. 재조합 에스케리치아 세균의 예는 L-이소류신 생합성 효소인 트레오닌 데아미나제 또는 아세토하이드록시산 신타제를 암호화하는 유전자가 플라스미드를 사용한 형질전환에 의해 강화된 것들 등이다(JP2-458A, JP2-42988A, JP8-47397).
L-발린 생산 세균의 예는 에스케리치아 콜리 VL1970 균주(미국 특허 제5,658,766호) 등을 포함한다. L-발린 생산 세균의 예는 추가로 성장을 위해 리포산을 요구하고/하거나 H+-ATPase가 결핍된 돌연변이체(WO96/06926), 및 ilvGMEDA 오페론을 함유하는 DNA 단편으로 형질전환되고 ilvG, ilvM, ilvE, 및 ilvD 유전자 하나 이상을 발현하는 에스케리치아 속의 세균을 포함한다. ilvGMEDA 오페론의 발현은 L-발린 및/또는 L-이소류신 및/또는 L-류신에 의해 조절되고(감쇠되기) 때문에, 감쇠를 위해 요구되는 영역은 L-발린에 의한 발현의 억제를 제거하기 위해 제거되거나 돌연변이되는 것이 바람직할 수 있다(U.S. Patent No. 5,998,178). 또한 ilvGMEDA 오페론은 ilvA 유전자에 의해 암호화된 트레오닌 데아미나제의 활성을 발현하지 않는 것이 바람직할 수 있다. 감쇠가 상기된 바와 같이 제거된, ileS17를 갖는 에스케리치아 콜리 VL1970은, 기탁기관[GNIIgenetika (Russian National Collection of Industrial Microorganisms (VKPM) Depositary, GNIIgenetika) (주소: 1, Dorozhny Proezd., 1, 113545, Moscow, Russia)]에 기탁번호 VKPM B-4411로서 기탁되었다.
고유 생합성 효소를 암호화하는 유전자 이외에, 당 흡수, 당 대사(당 분해 시스템) 및 에너지 대사에 관여하는 유전자는 본 발명에 사용되는 L-아미노산 생산 세균에서 증진될 수 있다.
당 대사에 관여하는 유전자의 예는 당 분해 효소 또는 당을 흡수하는 단백질을 암호화하는 유전자, 예를 들어, 글루코스-6-포스페이트 이소머라제를 암호화하는 유전자(pgi; WO01/02542), 포스포에놀피루베이트 신타제를 암호화하는 유전자(pps; EP877090), 포스포글루코뮤타제를 암호화하는 유전자(pgm; WO03/04598), 프럭토스-바이포스페이트 알돌라제를 암호화하는 유전자(fba; WO03/04664), 피루베이트 키나제를 암호화하는 유전자(pykF; WO03/008609), 트랜스알돌라제를 암호화하는 유전자(talB; WO03/008611), 푸마라제를 암호화하는 유전자(fum; WO01/02545), 포스포에놀피루베이트 신타제를 암호화하는 유전자(pps; EP877090), 비-PTS 슈크로스 흡수 시스템(csc; EP149911), 및 슈크로스 동화 유전자(scrAB operon; WO90/04636)이다.
에너지 대사에 관여하는 유전자의 예는 트랜스하이드로게나제 유전자(pntAB; U.S. Patent No. 5,830,716) 및 시토크롬 bo 형 옥시다제 유전자(cyoABCD; EP1070376)를 포함한다.
본 발명의 미생물은 상기된 바와 같이 L-아미노산을 생산하는 능력을 갖는 미생물을, EvgAS 2-성분 시스템에 관여하는 전사 인자를 암호화하는 유전자인 evgA 유전자, gadE 유전자, 또는 ydeO 유전자로부터 선택되는 하나 이상의 유전자의 발현이 증가되도록 변형시켜 수득할 수 있다. 표적 물질을 생산하는 능력은 evgA 유전자, gadE 유전자,또는 ydeO 유전자의 발현량이 증가되도록 변형시킨 후 부여될 수 있다. evgA 유전자, gadE 유전자, 또는 ydeO 유전자의 발현 증가는 이후에 기술되는 바와 같은 프로모터 변형을 포함하는 발현 조절 영역의 변형을 통한 내인성 evgA 유전자, gadE 유전자, 또는 ydeO 유전자의 발현 증가일 수 있거나 이것은 evgA 유전자, gadE 유전자, 또는 ydeO 유전자를 포함하는 플라스미드의 도입을 통한 evgA 유전자, gadE 유전자, 또는 ydeO 유전자의 카피수 증가일 수 있거나 세균의 염색체상의 당해 유전자의 증폭 등일 수 있다. 추가로, 당해 기술을 조합하여 사용할 수 있다.
본 발명에서 "EvgAS 2-성분 시스템"은 EvgA-EvgA 히스티딘-아스파르테이트 인 전달(phosphorelay) 조절을 통해 전사 인자를 활성화시키는 경로를 의미한다. 보다 구체적으로, 센서 키나제인 EvgS 단백질(서열번호 26)은 당해 단백질의 히스티딘 잔기를 자가 인산화시킴에 이어서 포스페이트 그룹을 반응 조절인자이고 전사 인자인 EvgA 단백질(서열번호 24)에 특이적인 아스파르테이트 잔기로 전달한다. 반응 조절인자 전사 인자 EvgA는 당해 인산화에 의해 활성화되어 전사 인자 YdeO 단백질(서열번호 30)을 암호화하는 ydeO 유전자 (서열번호 29) 및/또는 전사 인자 GadE 단백질(서열번호 28)을 암호화하는 gadE 유전자(서열번호 27)의 전사를 활성화시킬 뿐만 아니라 많은 유전자의 전사를 조절한다(J. Bacteriol. 184:6225-6234, 2002; Mol. Microbiol. 48:699-712, 2003). YdeO 단백질은 또한 gadE 유전자의 전사를 활성화시킨다. 활성화된 EvgA 단백질 및 YdeO 단백질에 의해 활성화된 gadE 유전자의 전사 결과로서, GadE 단백질의 발현은 증가하고 양성 전사 인자로서 이것은 다른 유전자의 전사를 증폭시킨다(Microbiology. 150:61-72, 2004; J Bacteriol. 186:7378-89, 2004). 따라서, 본 발명에서 "EvgAS 2-성분 조절 인자에 관여하는 전사 인자"는 EvgA 단백질, GadE 단백질 또는 YdeO 단백질을 지칭한다.
이와 같이 본 발명에서, "센서 키나제"는 리간드로서 환경 인자를 감지하는 역할을 하는 단백질이고 ATP를 사용하여 자신의 히스티딘 잔기를 인산화시킴에 이어서 당해 포스페이트 그룹을 반응 조절인자에 전달한다. 본 발명에서, "반응 조절인자"는 센서 키나제로부터 특정 아스파르테이트상에 인산화를 수용함을 통해 활성화된 후 세포내에서 정보를 전달하는 역할을 하는 단백질이고 많은 경우에 이것은 전사 인자이다.
모균주, 예를 들어, 야생형 균주 또는 비-변형된 균주와 비교하는 경우 EvgA 단백질, GadE 단백질, 또는 YdeO 단백질를 암호화하는 유전자(이후부터, evgA, gadE, 또는 ydeO 유전자)의 발현의 개선은 mRNA의 양을 야생형 또는 비변형된 균주에서의 mRNA의 양과 비교함에 의해 확인될 수 있다. 노던 하이브리드화 및 역-전사효소 PCR(RT-PCR)을 사용하여 발현양을 확인할 수 있다(Sambrook, J., and Russell, D.W. Molecular Cloning A Laboratory Manual/Third Edition. New York: Cold Spring Harbor Laboratory Press (2001)). 효소 활성의 증가 정도는 활성이 야생형 또는 비변형된 균주와 비교하여 증가되는 한 제한되지 않지만 예를 들어 이것이 야생형 또는 비변형된 균주의 1.5배 이상, 바람직하게는 2배 이상, 보다 바람직하게는 3배 이상인 것이 바람직할 수 있다. 효소 활성의 증가는 표적 단백질 양이 비변형 또는 야생형 균주의 것과 비교하여 증가된 것이면 확인될 수 있다. 이것은 예를 들어, 항체를 사용한 웨스턴 블롯(Sambrook, J., and Russell, D.W. Molecular Cloning A Laboratory Manual/Third Edition. New York: Cold Spring Harbor Laboratory Press (2001))에 의해 검출될 수 있다 (Sambrook, J., and Russell, D.W. Molecular Cloning A Laboratory Manual/Third Edition. New York: Cold Spring Harbor Laboratory Press (2001)).
본 발명에서 "전사 인자"는 발현이 EvgSA 2-성분 조절인자에 의해 조절되는 유전자의 전사 인자를 의미하고 EvgA 단백질, GadE 단백질, 및 YdeO 단백질에 해당한다. EvgA 단백질, GadE 단백질 및 YdeO 단백질은 EvgSA 2-성분 조절인자의 조절하에 있는 다양한 대사 효소를 암호화하는 유전자의 전사를 양성으로 조절한다. 예를 들어, 6-포스포글루코네이트 데하이드로게나제(GND)를 암호화하는 gnd 유전자 또는 아데닐숙시네이트 신타제를 암호화하는 purA 유전자의 전사는 EvgSA 2-성분 조절인자의 전사 인자에 의해 활성화된다. 즉, 야생형 균주 또는 비변형된 균주에 비해 EvgA 단백질, GadE 단백질, 또는 YdeO 단백질의 생산량을 개선시킴에 의해, 발현이 EvgAS 2-성분 조직인자에 의해 조절되는 유전자의 전사량은 증가한다. 전사 인자의 활성은 DNA와의 연결을 측정하는 전기영동 이동성 전이 분석 또는 전사 활성의 시험관내 측정을 사용하여 측정될 수 있다(Sambrook, J., and Russell, D.W. Molecular Cloning A Laboratory Manual/Third Edition. New York: Cold Spring Harbor Laboratory Press (2001)).
본 발명의 evgA 유전자 및 이의 상동체는 에스케리치아 속의 세균으로부터 기원한다. 예를 들어, 에스케리치아 콜리의 evgA 유전자는 서열번호 24의 아미노산 서열을 갖는 단백질을 암호화하는 유전자(서열번호 23)이다(GenBank Accession No. NP_416870 [gi:16130301]).
evgA 유전자와 구조적으로 유사성이 높고 숙주로 도입될 때 L-아미노산 생산능력이 개선되고 전사 인자 활성을 나타내는 evgA 유전자의 상동체는 에스케리치아 속의 다른 미생물로부터 유래한다. evgA 상동체의 예는 GenBank에 등록된 살모넬라(Salmonella), 쉬겔라(Shigella), 및 예르시니아(Yersinia) 속 등의 evgA 유전자이다. 추가로, 상기 예에 주어진 유전자와의 상동성을 기준으로, evgA 유전자는, 예를 들어 코리네박테리움 글루타미쿰(Corynebacterium glutamicum), 브레비박테리움 락토퍼멘툼(Brevibacterium lactofermentum) 등과 같은 코리네형 세균; 슈도모나스 아에루기노사(Pseudomonas aeruginosa) 등과 같은 슈도모나스 속의 세균; 마이코박테리움 튜버큘로시스(Mycobacterium tuberculosis) 등과 같은 마이코박테리움 속의 세균; 및 바실러스 속의 세균으로부터 클로닝될 수 있다. 유전자 명칭이 상이한 하나는 이들이 에스케리치아 속의 세균의 evgA와 고도로 상동성인 한 수용될 수 있다. 예를 들어, evgA 유전자 상동체는 서열번호 17 및 18의 합성 올리고뉴클레오타이드를 사용하여 클로닝될 수 있는 유전자를 포함한다.
evgA 유전자 상동체의 뉴클레오타이드 서열은 상기된 서열 정보를 기준으로 공지된 데이터베이스로부터 상동성이 높은 유전자를 검색함에 의해 수득될 수 있다. 아미노산 서열 및 뉴클레오타이드 서열의 상동성은 예를 들어, 카를린 및 알슐의 BLAST 알고리듬(Pro. Natl. Acad. Sci. USA, 90, 5873 (1993)) 또는 FASTA(Methods Enzymol., 183, 63 (1990))을 사용하여 측정할 수 있다. 당해 BLAST 알고리듬을 기준으로, BLASTN 또는 BLASTX로 불리우는 프로그램이 개발되었다(참조: http://www.ncbi. nih.gov/BLAST/).
본 발명의 gadE 유전자는 에스케리치아 속의 세균의 gadE 유전자 및 이의 상동체를 의미한다. 에스케리치아 콜리의 gadE 유전자의 예는 서열번호 28의 아미노산 서열을 갖는 단백질을 암호화하는 유전자(서열번호 27)를 포함한다 (GenBank Accession No. NP_417969 [gi:16131384]).
gadE 유전자의 상동체는 상기된 evgA 유전자 상동체와 함께 에스케리치아 속의 세균의 gadE 유전자와 구조적으로 높은 유사성을 갖고 숙주로 도입되는 경우 L-아미노산 생산능을 개선시키고 전사 인자 활성을 나타내는, 에스케리치아 속의 세균의 유전자이다. gadE 유전자 유사체는 서열번호 19 및 20의 합성 올리고뉴클레오타이드를 사용하여 클로닝될 수 있는 유전자를 포함한다.
본 발명의 ydeO 유전자는 에스케리치아 속의 세균의 ydeO 유전자 및 이의 상동체를 의미한다. 에스케리치아 콜리의 ydeO 유전자의 예는 서열번호 28의 아미노산 서열을 갖는 단백질을 암호화하는 유전자(서열번호 27)를 포함한다 (GenBank Accession No. NP_417969 [gi:16131384]).
상기된 바와 같은 ydeO 유전자 상동체와 함께 에스케리치아 속의 세균의 ydeO 유전자와 구조적으로 높은 유사성을 갖고 L-아미노산 생산능을 개선시키고 숙주에 도입될 때 전사 인자 활성을 나타내는, 다른 미생물로부터 기원하는 유전자이다. ydeO 유전자 상동체는 서열번호 21 및 22의 합성 올리고뉴클레오타이드를 사용하여 클로닝될 수 있는 유전자를 포함한다.
본 발명에 사용되는 evgA 유전자, gadE 유전자, 또는 ydeO 유전자는 이에 의해 암호화된 단백질의 기능, 즉 전사 인자 활성이 손상되지 않는 한 야생형 유전자로 제한되지 않고 이것은 또한 서열번호 24, 28 또는 30의 아미노산 서열에서 하나 또는 여러 아미노산 치환, 결실, 삽입, 부가등을 포함하는 서열을 갖는 단백질을 암호화하는 돌연변이체 또는 인공적으로 변형된 생성물일 수 있다. 여기서, 용어 '여러'는 단백질의 입체구조에서 아미노산 잔기의 위치 또는 아미노산 유형에 따라 다양하고, 특히 이것은 1 내지 20개, 바람직하게는 1 내지 10개 및 보다 바람직하게는 1 내지 5개를 의미한다. 하나 또는 여러 아미노산의 상기 치환, 결실, 삽입 또는 부가는 전사 안지 활성이 보존된 보존성 돌연변이다. 보존성 돌연변이는 치환 부위가 방향족 아미노산인 경우 Phe, Trp, Tyr 간에 상호 치환되는 돌연변이; 치환 부위가 소수성 아미노산인 경우 Leu, Ile, Val간에 상호 치환되는 돌연변이; 이것이 극성 아미노산인 경우 Gln, Asn간에 상호치환되는 돌연변이; 이것이 염기성 아미노산인 경우 Lys, Arg, His간에 상호 치환되는 돌연변이; 이것이 산성 아미노산인 경우 Asp, Glu간에 상호 치환되는 돌연변이; 및 이것이 하이드록실 그룹을 갖는 아미노산인 경우 Ser, Thr간에 상호 치환되는 돌연변이이다. 전형적인 보존성 돌연변이는 보존성 치환이다. 보존성인 것으로 고려되는 치환의 특정 예는: Ala의 Ser 또는 Thr로의 치환; Arg의 Gln, His, 또는 Lys로의 치환; Asn의 with Glu, Gln, Lys, His, 또는 Asp로의 치환; Asp의 Asn, Glu, 또는 Gln로의 치환; Cys의 Ser 또는 Ala로의 치환; Gln의 Asn, Glu, Lys, His, Asp, 또는 Arg로의 치환; Glu의 Gly, Asn, Gln, Lys, 또는 Asp로의 치환; Gly의 Pro로의 치환; His의 Asn, Lys, Gln, Arg, 또는 Tyr로의 치환; Ile의 Leu, Met, Val, 또는 Phe로의 치환; Leu의 Ile, Met, Val, 또는 Phe로의 치환; Lys의 Asn, Glu, Gln, His, 또는 Arg로의 치환; Met의 Ile, Leu, Val, 또는 Phe로의 치환; Phe의 Trp, Tyr, Met, Ile, 또는 Leu로의 치환; Ser의 Thr 또는 Ala로의 치환; Thr의 Ser 또는 Ala로의 치환; Trp의 Phe 또는 Tyr로의 치환; Tyr의 His, Phe, 또는 Trp로의 치환; 및 Val의 Met, Ile, 또는 Leu로의 치환을 포함한다. 상기된 아미노산의 치환, 결실, 삽입, 부가 또는 역위는 evgA, gadE, 및 ydeO 유전자를 보유하는 종의 차이 또는 미생물의 개체 차이에 따라 다양하고 천연적으로 발생하는 돌연변이(돌연변이체 또는 변이체)를 포함한다. 당해 유전자는 예를 들어, 부위 지시된 돌연변이 유발을 사용하여 서열번호 23, 25 및 29에 나타낸 뉴클레오타이드 서열을 변형시켜, 암호화된 단백질내 부위 특이적 아미노산 잔기가 치환, 결실, 삽입 또는 부가를 포함하도록 함에 의해 수득할 수 있다.
더욱이, evgA, gadE, 또는 ydeO 유전자는, 전사 인자이고 서열번호 26, 30 또는 32의 전체 아미노산 서열과 80% 이상, 바람직하게는 90% 이상, 보다 바람직하게는 95% 이상 또는 심지어 보다 바람직하게, 97% 이상의 상동성을 갖는 단백질을 암호화하는 서열이다. 또한, evgA, gadE, 또는 ydeO 유전자에서, 코돈은 당해 유전자가 각각 도입되는 숙주에 의해 보다 용이하게 사용되는 다른 동등한 코돈으로 치환된다. 또한, evgA, gadE, 또는 ydeO 유전자 생성물이 전사 인자의 기능을 보유하고 있는 한, 이의 N 말단 또는 C 말단은 연장되거나 제거될 수 있다. 예를 들어, 연장되거나 제거된 길이는 50개 이하, 바람직하게는 20개 이하, 보다 바람직하게는 10개 이하 및 심지어 보다 바람직하게는 5개 이하의 아미노산 잔기일 수 있다. 보다 구체적으로, 서열번호 24의 50개 내지 5개 아미노산이 연장되거 제거된, N 말단으로부터 18개 또는 30개 아미노산이 연장되거나 제거된, C 말단으로부터 50개 내지 5개 아미노산이 연장되거나 제거된 단백질을 암호화하는 유전자가 사용될 수 있다.
또한, 유전자의 변이체는 하기의 통상적인 돌연변이 처리에 의해 수득할 수 있다. 돌연변이 처리 방법중 하나는 하이드록실아민 등을 사용하는 evgA, gadE, 또는 ydeO 유전자의 시험관내 돌연변이다. 또 다른 방법은 당해 유전자를 갖는 미생물을 처리하기 위해 N-메틸-N'-니트로-N-니트로소구아니딘(NTG) 또는 에틸 메틸 설포네이트(EMS)와 같은 돌연변이 처리에 통상적으로 사용되는 자외선 또는 돌연변이제를 사용한다. 이들 유전자가 전사 인자 활성을 갖는 단백질을 암호화하는지의 여부는 예를 들어, 적당한 세포에서 당해 유전자를 발현시키고 전사 인자 활성이 존재하는지의 여부를 조사함에 의해 확인될 수 있다.
evgA, gadE, 또는 ydeO 유전자는 또한 엄중조건하에서 각각 서열번호 23, 27 또는 29의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 서열로부터 제조되고 전사 활성을 갖는 단백질을 암호화하는 프로브와 하이브리드화하는 DNA일 수 있다. 여기서, 용어 "엄중 조건"은 소위 특이적 하이브리드가 형성되지만 비특이적 하이브리드는 형성되지 않는 조건을 언급한다. 이것은 수치로 당해 조건을 명백하게 나타내기는 어렵지만, 이들은 DNA의 고도로 상동성인 단편, 예를 들어, 70% 이상의 상동성을 갖는 DNA는 서로 하이브리드화하고 상기 보다 낮은 상동성을 갖는 DNA는 서로 하이브리드화하지 않는 조건으로서 예시될 수 있다. 또한, 엄중 조건은 세척이 통상적인 서던 하이브리드화에 전형적인 세척 조건, 즉 60℃, 1 x SSC, 0.1 % SDS, 바람직하게는 0.1 x SSC, 0.1 % SDS, 및 보다 바람직하게는, 68 C, 0.1 x SSC, 0.1 % SDS에 상응하는 온도 및 염 농도에서 1회 또는 바람직하게는 2 내지 3회 수행되는 조건에 의해 예시된다.
프로브로서, 서열번호 23, 27 또는 29의 뉴클레오타이드 서열 또는 이들 서열의 일부가 또한 사용될 수 있다. 당해 프로브는 당해 뉴클레오타이드 서열중 하나를 함유하는 DNA 단편을 주형으로서 사용하고 서열번호 23, 27 또는 29의 뉴클레오타이드 서열을 기초로 제조된 올리고뉴클레오타이드를 프라이머로서 하용하는 PCR을 사용하여 제조될 수 있다. 예를 들어, 약 300bp 길이의 DNA 단편이 프로브로서 사용되는 경우, 하이브리드화를 위한 세척 조건은 50℃, 2 x SSC, 및 0.1% SDS이다.
evgA, gadE, 또는 ydeO 유전자의 발현을 증진시키기 위한 변형은 예를 들어, 세포내에서 유전자 카피수를 증가시키기 위한 유전자 재조합 기술을 사용하여 제조될 수 있다. 예를 들어, evgA, gadE, 또는 ydeO 유전자를 함유하는 DNA 단편은 숙주 미생물에서 작용하는 벡터, 바람직하게는 다중카피 벡터에 연결하여 재조합 DNA를 제조하고 이것은 이어서 미생물에 도입되어 이를 형질전환시킨다.
에스케리치아 콜리의 evgA, gadE, 또는 ydeO 유전자가 사용되는 경우, 이들 유전자는 에스케리치아 콜리의 게놈 DNA가 주형으로서 사용되고 서열번호 22, 27 또는 서열번호 29의 뉴클레오타이드 서열을 기초로 제조된 프라이머, 예를 들어, evgA 유전자에 대해 서열번호 17 및 18에 나타낸 프라이머, gadE 유전자에 대해 서열번호 19 및 20에 나타낸 프라이머 또는 ydeO 유전자에 대해 서열번호 21 및 22에 나타낸 프라이머를 사용하는 PCR(PCR: 폴리머라제 연쇄 반응; 문헌참조: White, T.J. et al., Trends Genet. 5, 185 (1989))에 의해 수득할 수 있다. 엔테로박테리아세애 과에 속하는 다른 미생물의 evgA, gadE, 및 ydeO 유전자는 또한 전사 인자의 다른 서열 정보를 기초로 하여 제조된 올리고뉴클레오타이드가 프라이머로서 사용되는 PCR 또는 상기 언급된 서열 정보를 기초로 제조된 올리고뉴클레오타이드가 프로브로서 사용되는 하이브리드화 방법을 사용하여, 당해 미생물에서 공지된 evgA, gadE, 및 ydeO 유전자 또는 미생물의 게놈 DNA 또는 게놈 DNA 라이브러리로부터 수득할 수 있다. 부수적으로, 게놈 DNA는 DNA 공여체 미생물로부터 제조될 수 있다. 예를 들어, 사이토 및 미우라의 방법(Saito and Miura's method) 등(문헌참조:H. Saito and K. Miura, Biochem. Biophys. Acta, 72, 619 (1963), Seibutsu Kogaku Jikkensho [Bioengineering Experiments], edited by The Society of Biotechnology, Japan, pp. 97-98, Baifukan, 1992)]이 사용될 수 있다.
다음, 재조합 DNA는 PCR에 의해 증폭된 evgA, gadE, 또는 ydeO 유전자를 숙주 미생물의 세포에서 작용할 수 있는 DNA 벡터 연결함에 의해 제조된다. 숙주 미생물의 세포에서 작용할 수 있는 벡터는 숙주 미생물의 세포에서 자발적으로 복제할 수 있는 벡터이다. 에스케리치아 콜리의 세포에서 자발적으로 복제가능한 벡터의 예는 pUC19, pUC18, pHSG299, pHSG399, pHSG398, pACYC184, (pHSG 및 pACYC는 제조원[Takara Bio Inc.]으로부터 입수할 수 있다), RSF1010, pBR322, pMW219 (pMW는 제조원[Nippon Gene Co., Ltd.]으로부터 입수할 수 있다), pSTV29 (제조원[Takara Bio Inc.]으로부터 입수 가능함) 등을 포함한다.
상기된 바와 같이 제조된 재조합 DNA는 지금까지 보고된 형질전환 방법중 어느 하나에 따라 도입할 수 있다. 예를 들어, 한가지 방법은 에스케리치아 콜리 K-12 (Mandel, M. and Higa, A., J. Mol. Biol., 53, 159 (1970))에 대해 보고된 바와 같이 수용체 세균을 염화칼슘으로 처리함에 의해 DNA의 침투성을 증가시키는 것이다. 또 다른 방법은 바실러스 서브틸리스에 관하여 보고된 바와 같이(Duncan, C. H., Wilson, G. A. and Young, F. E., Gene, 1, 153 (1977)), 성장 단계의 세포로부터 컴피턴트 세포를 제조한 후 DNA를 도입하는 것이다. 또한, 적용될 수 있는 또 다른 방법은 바실러스 서브틸리스에 관하여 공지된 바와 같이 DNA 수용체 미생물이 재조합 DNA를 용이하게 흡수할 수 있는 원형질체 또는 부분원형질체로 변화되고 이어서 숙주로 도입되는 방법이다(Chang, S. and Choen, S. N., Molec. Gen. Genet., 168, 111 (1979); Bibb, M. J., Ward, J. M. and Hopwood, O. A., Nature, 274, 398 (1978); Hinnen, A., Hicks, J. B. and Fink, G. R., Proc. Natl. Acad. Sci. USA, 75 1929 (1978)).
evgA, gadE, 또는 ydeO 유전자의 카피수는 미생물의 게놈 DNA상에 상기된 바와 같이 다중 카피수의 evgA, gadE, 또는 ydeO 유전자를 통합시킴에 의해 증가될 수 있다. 다중 카피의 evgA, gadE, 또는 ydeO 유전자의 미생물의 게놈 DNA상으로의 도입은 다중 카피물이 게놈 DNA상에 존재하는 서열을 표적으로서 사용하는 상동성 재조합에 수행된다. 트랜스포존 요소의 말단상에 존재하는 반복 DNA 및 역위 반복체는 다중 카피물로 염색체 DNA 상에 존재하는 서열로서 사용될 수 있다. 또한, 이들 유전자는 게놈상에 존재하는 evgA, gadE, 또는 ydeO 유전자와 반복적으로 연결될 수 있거나 게놈상의 불필요한 유전자에 다중 카피로 도입될 수 있다. 이들 유전자는 온도 민감성 벡터 또는 통합 벡터를 사용하여 도입될 수 있다.
문헌[JP2-109985A]에 기재된 바와 같이, evgA, gadE, 또는 ydeO 유전자를 트랜스포존으로 도입할 수 있고 이를 전달하여 다중 카피의 유전자가 염색체 DNA로 통합될 수 있도록 할 수 있다. evgA, gadE, 또는 ydeO 유전자의 게놈으로의 통합은 evgA, gadE, 또는 ydeO 유전자의 일부를 갖는 프로브를 사용하는 서던 하이브리드화에 의해 확인될 수 있다.
상기된 유전자의 카피수를 증가시키는 것 외에도, evgA, gadE, 또는 ydeO 유전자의 발현은 또한 예를 들어, 게놈 DNA 또는 플라스미드상의 evgA, gadE, 또는 ydeO 유전자등의 프로모터와 같은 발현 조절서열을 보다 강한 것으로 대체하고 각각의 유전자의 -35, -10 영역을 보존성 서열에 근접하게 위치시키고 evgA, gadE, 또는 ydeO 유전자의 발현을 증진시킬 수 있는 조절인자를 증폭시키고 evgA, gadE, 또는 ydeO 유전자의 발현을 감소시키는 조절인자를 결실시키거나 약화시키는, WO 00/18935에 기재된 방법을 사용하여 증진될 수 있다. 예를 들어, lac 프로모터, trp 프로모터, trc 프로모터, tac 프로모터, araBA 프로모터, 람다 파아지 PR 프로모터, PL 프로모터, tet 프로모터, T7 프로모터, 10 프로모터등이 모두 강한 프로모터로서 공지되어 있다. 또한 evgA, gadE, 또는 ydeO 유전자의 프로모터 영역 또는 SD 영역으로 뉴클레오타이드 치환등을 도입하여 프로모터 강도를 증가시킬 수 있다. 프로모터의 강도를 평가하는 방법의 예 및 강한 프로모터의 예는 문헌[Goldstein et al. (Prokaryotic promoters in biotechnology. Biotechnol. Annu. Rev., 1, 105-128 (1995)) 등에 기재되어 있다. 추가로, 리보솜 결합 부위(RBS) 및 개시 코돈 사이의 스페이서 영역, 특히 개시 코돈 바로 상부의 서열에서 여러 뉴클레오타이드의 치환은 mRNA 해독 효율에 대해 강한 효과를 갖는 것으로 공지되어 있다. evgA, gadE, 또는 ydeO 유전자의 프로모터와 같은 발현 조절 영역 등은 GENETYX 등과 같은 프로모터-프로브 및 유전자 분석 소프트웨어에 의해 동정될 수 있다. evgA, gadE, 또는 ydeO 유전자의 발현은 당해 프로모터의 치환 또는 변형에 의해 증진될 수 있다. 발현 조절 서열의 치환은 예를 들어, 온도 민감성 플라스미드 또는 레드 구동 통합 방법을 사용하여 수행할 수 있다(WO2005/010175).
발현이 evgA, gadE, 또는 ydeO 유전자에 의해 조절되는 유전자의 전사를 증가시키는 돌연변이는 또한 evgA, gadE, 또는 ydeO 유전자로 도입할 수 있다. evgA, gadE, 또는 ydeO 유전자에 의해 암호화된 단백질의 활성을 증가시키는 돌연변이의 예는 evgA, gadE, 또는 ydeO 유전자의 전사량을 증가시키는 프로모터 서열의 돌연변이 및 전사의 특이적 활성을 증가시키는 유전자의 암호화된 영역내의 돌연변이이다.
evgA, gadE, 또는 ydeO 유전자에 의해 암호화된 단백질은 히스티딘 키나제 EvgS에 의해 활성화된다. 따라서, 본 발명의 미생물은 evgA, gadE, 또는 ydeO 유전자의 발현량이, EvgS를 암호화하는 evgS 유전자의 발현량을 증가시킴에 의해 증가된 미생물일 수 있다. 여기서, 본 발명의 evgS 유전자는 에스케리치아 속의 세균의 evgS 유전자 및 이의 상동체를 의미한다. 예를 들어, 에스케리치아 콜리의 evgS 유전자는 서열번호 26의 아미노산 서열을 갖는 단백질을 암호화하는 유전자(서열번호 25)에 의해 예시된다(GenBank Accession No. NP_417969 [gi:16131384]).
evgS 유전자의 상동체는 에스케리치아 속의 세균의 evgS 유전자와 구조에 있어서 높은 유사성을 갖고, L-아미노산의 생산능을 개선시키고 숙주로 도입될 때 전사 인자 활성을 나타내는, 다른 미생물 기원의 유전자를 의미한다. evgS 상동체의 예는 GenBank에 등록된 살모넬라, 쉬겔라 및 예르시니아 속의 evgS 유전자를 포함한다. 추가로, 상기 예에서 주어된 유전자와의 상동성을 기준으로, evgS 유전자는 코리네박테리움 글루타미쿰, 브레비박테리움 락토퍼멘툼 등과 같은 코리네형 세균; 슈도모나스 아에루기노사 등과 같은 슈도모나스 속의 세균; 마이코박테리움 튜버큘로시스 등과 같은 마이코박테리움 속의 세균 및 바실러스 속의 세균으로부터 클로닝될 수 있다. 유전자 명칭이 상이한 것은 이들이 에스케리치아 속의 세균의 evgS와 고도로 상동성인 한 수용될 수 있다. 예를 들어, 에스케리치아 콜리에서, evgS 유전자는 evgA 유전자와 오페론을 형성하고 서열번호 17 및 18의 합성 올리고뉴클레오타이드를 사용한 PCR에 의해 evgA 유전자와 함께 수득될 수 있다. 다른 미생물과 함께, 서열번호 17 및 18의 올리고뉴클레오타이드를 사용하여 당해 유전자가 수득될 수 있는 것으로 예상된다.
본 발명에 사용되는 evgS 유전자는 야생형 유전자로 제한되지 않고 단백질의 기능, 즉 전사 인자 활성의 기능이 손상되지 않는 한 이것은 또한 서열번호 26의 아미노산 서열의 하나 또는 다중 위치에서 하나 또는 여러 아미노산 치환, 결실, 삽입, 부가등을 포함하는 서열을 갖는 단백질, 즉, 보존성 돌연변이를 갖는 단백질을 암호화하는 돌연변이 또는 인공적으로 변형된 변이체일 수 있다. 용어 "여러" 및 "보존성 돌연변이"는 evgA 유전자, gadE 유전자, 및 ydeO 유전자에 관하여 상기된 것들과 동일하다.
evgS의 발현양을 증가시키는 것은 상기된 바와 같은 evgA, gadE, 및 ydeO 유전자의 발현양을 증가시키기 위해 사용되는 동일한 방법을 사용하여 수행할 수 있다. evgA, gadE, 또는 ydeO 유전자의 발현양을 증가시키는 것은 유전자 모두에 대해 상기 언급된 수단 또는 각각의 유전자 마다 상이한 수단을 사용하여 수행할 수 있다.
2. L-글루탐산 생산 방법
본 발명의 L-아미노산의 생산 방법은 본 발명의 미생물을 배지에서 배양하고 당해 배지 또는 미생물의 세포에서 L-아미노산을 생산하고 축적시키며 당해 배지 또는 세포로부터 L-아미노산을 수거하는 단계를 포함한다.
미생물을 사용한 L-아미노산의 발효 및 생산에 통상적으로 사용되는 배지가 본 발명에 사용될 수 있다. 즉, 탄소원, 질소원, 무기 이온 및 기타 유기 성분을 함유하는 통상의 배지가 사용될 수 있다. 탄소원은 글루코스, 슈크로스, 락토스, 갈락토스, 프럭토스, 전분 가수분해물과 같은 당 등, 글리세롤, 소르비톨등과 같은 알콜, 푸마르산, 시트르산, 숙신산등과 같은 유기산을 포함한다. 물론, 글루코스, 프럭토스, 및 슈크로스가 바람직하게 사용될 수 있다. 질소원은 황화암모늄, 염화암모늄, 인산암모늄과 같은 무기 암모늄, 대두 가수분해물 등과 같은 유기 질소, 암모니아 가스, 암모니아수 등을 포함한다. 유기 미량영양물 공급원으로서, 비타민 B1, L-호모세린 또는 효모 추출물 등과 같은 적당량의 요구되는 물질이 배지에 존재하는 것이 바람직할 수 있다. 이들 외에도, 필요에 따라, 소량의 인산암모늄, 황산마그네슘, 철 이온, 망간 이온 등이 첨가될 수 있다. 본 발명에 사용되는 배지는 이것이 탄소원, 질소원, 무기 이온 및 경우에 따라 기타 유기 미량영양물을 함유하는 한 천연 또는 합성 배지일 수 있다.
미생물의 성장 또는 표적 물질의 생산성을 개선시키는 아미노산은 배지에 첨가할 수 있다. 예를 들어, L-트레오닌, L-호모세린 또는 L-이소류신이 L-라이신 발효를 위해 첨가되는 것이 바람직할 수 있다. L-이소류신, L-라이신, L-글루탐산 또는 L-호모세린이 L-트레오닌 발효를 위해 첨가되고 L-페닐알라닌 또는 L-티록신 등은 L-트립토판 발효를 위해 첨가된다. 첨가된 L-아미노산의 농도는 약 0.01 내지 10g/L이다.
배양은 배양동안에 24℃ 내지 37℃의 배양 온도 및 pH 5 내지 9에서 1 내지 7일동안 호기 조건하에 수행하는 것이 추천된다. pH를 조정하기 위해, 무기 또는 유기 산성 또는 알칼리 물질 및 암모니아 가스등이 사용될 수 있다. L-아미노산은 통상적인 이온 교환 수지 방법, 침전 방법 및 기타 공지된 방법의 조합을 조합하여 발효 브로쓰로부터 수거될 수 있다. L-아미노산이 세포내부에 축적되는 경우, 세포는 초음파등에 의해 파괴될 수 있다. 이어서, 세포 파쇄물은 원심분리에 의해 제거하여 상등액을 수득할 수 있고 이로부터 L-아미노산은 이온-교환 수지 방법 등을 사용하여 재수거될 수 있다.
본 발명은 하기의 비제한적인 실시예를 참조로 하기에서 보다 구체적으로 설명된다.
참조 실시예 1: L-트립토판 생산 세균의 작제
1-1. serA 유전자의 도입
포스포글리세레이트 데하이드로게나제 유전자(serA)는 플라스미드 pGH5 (WO9408031)에 존재하고 트랜스포존 Mud의 게놈으로 삽입시켰다. MudII1734를 함유하는 플라스미드 pCE1134(JP2-109985A)는 BamHI로 분해시켜 lac 오페론을 함유하는 DNA 단편을 제거하고 말단을 평활 말단화하고 SmaI 링커를 삽입하였다. 당해 플라스미드는 SmaI로 재분해시키고 자가 폐환시켜 환형 플라스미드를 형성하고, pMu1134로 명명하였다. serA를 함유하는 DNA 단편은 ScaI 및 SalI로 절단함에 의해 플라스미드 pGH5로부터 절단하고, 단편의 말단은 평활 말단화시켰다. 이어서 당해 단편은 상기 언급된 pMu1134의 SmaI 부위로 삽입하였다. 따라서, pGH5-유래 serA 유전자가 삽입된 Mud(MudserA로 명명)를 함유하는 플라스미드 pMudserA를 작제하였다.
수용체 세균으로서 탈감작된 안트라닐레이트 신타제를 갖는 L-트립토판 생산 세균 균주 SV164(WO9408031)를 사용하여 MudserA가 게놈상으로 전달된 세균 균주 L1을 지수로서 가나마이신 내성의 획득을 사용함에 의한 통상적인 방법에 따라 수 득하였다. 서던 하이브리드화 실험 결과로부터, MudserA가 L1 균주에 삽입되는 하나의 위치만이 있는 것으로 추론되었다. 또한, PCR에 의한 MudserA를 함유하는 게놈 DNA 단편의 클로닝 및 이의 뉴클레오타이드 서열의 측정을 사용하여 삽입이 이 콜리 K-12 게놈(GenBank 승인 번호 U00096)상의 240번, 950번 위치에 있음을 결정하였다.
1-2. trp 오페론의 도입
이어서, trp 오페론의 카피수를, trp 오페론을 트랜스포존을 사용하여 게놈으로 삽입함에 의해 증가시켰다. trp 오페론 유전자를 플라스미드 pGX100로부터 절단하였다. pGX100을, 탈감작된 trpE 유전자를 갖는 이. 콜리 MTR#2 균주(미국 특허 제4,371,614호)로부터 유래하는 DNA 단편을 플라스미드 pBR313에 삽입하여 작제하였다. 대략 7.6 kb trp 오페론을 함유하는 DNA 단편을 XhoI 및 SmaI로 절단하여 플라스미드로부터 절단할 수 있다. trp 오페론을 함유하는 DNA 단편을 XhoI 및 SmaI로 절단함에 의해 pGX100으로부터 절단하고 단편의 말단을 평활말단화시켰다. 이어서, 당해 단편을 상기 언급된 pCE1134의 SmaI 부위로 삽입하였다. trp 오페론을 함유하는 동일한 DNA 단편을 또한 서열목록에 나타낸 서열번호 1 및 2의 프라이머를 사용하는 PCR을 사용하여 이. 콜리 MTR#2 균주 게놈 DNA로부터 직접 클로닝할 수 있다. 상기된 바와 같이, MTR#2 균주로부터 유래하는 trp 오페론 유전자가 삽입된 Mud(MudtrpG' lac으로 명명)를 함유하는 플라스미드 pMudtrpG' lac를 작제하였다.
MudtrpG' lac을 게놈으로 삽입시킴에 의해 MudtrpG' lac의 카피수를 증가시키기 전에, 락토스 동화 결핍을 균주에 대한 선별 마커로서 락토스 동화능의 보충을 사용할 목적으로 숙주 균주에 부여하였다. L-트레오닌 생산 세균 VKPM B-3996(미국 특허 제5,175,107호)의 ilvG 유전자를 L1 균주로 P1-형질도입하여 L1 균주에 L-발린 내성을 부여하였다(문헌참조 W02005/103228). P1 형질도입은 통상적인 방법에 따라 수행하였고 형질도입체는 M9 최소 배지(4 g/L 글루코스, 12.8 g/L Na2HPO47H2O, 3 g/L KH2PO4, 0.5 g/L NaCl, 1 g/L NH4Cl, 5 mM MgSO4, 0.1 mM CaCl2, 1 mg/L 티아민, 20 mg/l L-Phe, 20 mg/L L-Tyr, 20 mg/L L-Met, 3 mg/L 피리독신, 20 mg/L L-Val, 20 mg/L 테트라사이클린)상에 도말하였고 Val-내성 콜로니를 수득하고 L1ValR로 명명하였다.
lacZ98::Tn10을, 지표로서 Tn10-유래 테트라사이클린 내성을 사용하는 통상적인 방법에 따라 ME8581 균주(HfrH (valS←uxuAB):lacZ98::Tn10 relA1 thi-1, 기탁기관(National Institute of Genetics)에 기탁됨) 기원의 L1ValR로 P1-형질도입하였다. 수득된 균주는 예상된 바와 같이 락토스 동화 결핍이었다. 이어서, 락토스 동화능이 결핍되고 Tn10이 부재인 균주를 수득하기 위해 테트라사이클린 민감성 균주 14-1-lac-tets를 레플리카 방법을 통해 형질도입된 균주로부터 수득하였다. 락토스 동화능은 여전히 14-1-lac-tets 균주에서 결핍이었다. 서던 하이브리드화에 의한 당해 균주의 Tn10 상태를 확인하였을 때, tet 유전자와 하이브리드화하는 어떠한 밴드도 검출되지 않았지만 Tn10의 IS10 영역과 하이브리드화하는 밴드는 검출되었고 따라서 IS10은 lacZ 유전자상에 잔류하는 것으로 사료된다.
수용체 세균으로서 14-1-lac-tets 균주와 함께 pMudtrpG' lac을 사용하여 MudtrpG' lac이 게놈으로 전달된 세균 균주 번호 202를 지표로서 락토스 동화능의 보충을 사용한 통상적인 방법에 따라 수득하였다. 삽입된 트랜스포존 또는 트랜스포존상의 유전자가 트랜스포존 삽입된 균주로부터 이탈하는 경향이 있는 경우, 영양배지상에 계대배양을 수행하여 가나마이신 내성, 락토스 동화능등을 안정하게 보유하는 세균 균주를 선별할 수 있다. 서던 하이브리드화의 결과로서, MudtrpG' lac이 202번 균주에 삽입되는 하나의 위치만이 존재하는 것으로 추론되었다. 또한, PCR에 의한 MudtrpG' lac을 함유하는 게놈 DNA 단편의 클로닝 및 이의 뉴클레오타이드 서열의 결정을 사용하여, 삽입이 이. 콜리 K-12 게놈(GenBank 승인 번호. U00096)상에 530,249번에 존재함을 측정하였다.
이어서, 슈크로스 동화 특성에 관여하는 scrK, scrY, scrA, scrB, 및 scrR 유전자를 P1 형질도입에 의해 202번으로 도입하고 수득한 세균 균주를 202번 scr(문헌참조 WO90/04636)로 지정하였다.
1-3. iclR를 붕괴시키기 위한 플라스미드의 작제
iclR 단편을 첨부된 지침서에 따라 피로베스트 DNA 폴리머라제(Takara Shuzo)를 사용하는 PCR을 사용하여 증폭시켰다. PCR 반응을 위해, 서열번호 3 및 서열번호 4의 올리고뉴클레오타이드를 프라이머로서 사용하고 RNA/DNA maxi 키트 (QIAGEN)를 사용하여 추출된 W3110 게놈을 주형으로서 사용하였다. PCR 후, 증폭된 DNA 단편을 위자드 PCR Prep(Promega)를 사용하여 정제하였다. 정제된 DNA 단 편을 제한 엔도뉴클레아제 EcoRI 및 HindIII(Takara Shuzo)로 분해하고 이어서 페놀 추출 처리 및 에탄올 침전을 진행하여 정제된 DNA를 수득하였다. 동일한 효소로 분해됨에 이어서 정제된 당해 단편 및 pUC18 (Takara Shuzo)을 DNA 연결 키트 버전 2(Takara Shuzo)를 사용하여 연결하였다. 당해 연결 반응 용액을 사용하여 JM109 컴피턴트 세포(Takara Shuzo)를 형질전환시킴에 이어서 50 g/mL 암피실린(Amp) (Meiji Seika) (LB+Amp 플레이트)을 함유하는 LB 한천 플레이트상으로 도말하고 콜로니를 37℃에서 선별하였다. 콜로니를 37℃에서 50 g/mL의 Amp를 함유하는 LB 배지를 사용하여 시험 튜브에서 배양하고 당해 플라스미드를 자동 플라스미드 추출기PI-50 (Kurabo)를 사용하여 추출하였다.
수득된 플라스미드 pUCiclR을 제한 엔도뉴클레아제 EcoO65I (Takara Shuzo)로 분해하고 평활 말단화시키고, BKL 키트(Takara Shuzo)를 사용하여 연결하였다. 연결 반응 용액을 사용하여, JM109를 형질전환시키고 콜로니를 상기된 바와 같이 선별하고 플라스미드를 추출하였다. 수득된 플라스미드를 EcoRI 및 HindIII로 분해시킴에 이어서 정제하고 동일한 효소로 분해되고 정제된 온도 민감성 플라스미드 pTS1과 연결하였다. pTS1은 pMAN031(문헌참조: J. Bacteriol. 162, 1196-1202 (1985), Figure 1)의 PstI-HindIII 단편을 pBR322(Takara Shuzo)의 PstI-HindIII 단편으로 대체하여 수득하였다. 연결 반응 용액을 사용하여, JM109를 형질전환시키고 콜로니를 30℃에서 LB+Amp 플레이트상에서 선별하였다. 콜로니를 50 g/mL Amp를 함유하는 LB 배지를 사용하여 시험 튜브에서 30℃에서 배양하고 플라스미드를 상기된 바와 같이 추출하였다. EcoRI 및 HindIII를 사용한 분해로 예상된 길이를 갖는 단편으로 생성된 플라스미드를 iclR 붕괴 플라스미드 pTS△iclR로서 지정하였다.
1-4. iclR-붕괴된 균주의 수득
202번 scr을 pTS△iclR로 형질전환시키고 콜로니를 30℃에서 LB+Amp 플레이트상에서 선별하였다. 액체 배양을 30℃에서 밤새 수행한 후, 배양물을 10-3으로 희석시키고 LB+Amp 플레이트상에 도말하고 콜로니를 42℃에서 선별하였다. 구체적으로, 배양물을 LB+Amp 플레이트상에 도말하고 30℃에서 배양하고 플레이트의 8분의 1을 차지하는 세포를 2ml의 LB 배지에 현탁시키고 42℃에서 4 내지 5시간동안 교반하면서 배양하였다. 10-5로 희석된 세포를 LB 플레이트상에 도말하고 콜로니를 수득하였고 이중 100여개의 콜로니를 각각 LB 플레이트 및 LB+Amp 플레이트상에 도말하고 이의 성장은 Amp 민감성 및 내성을 확인함에 의해 확인하였다. Amp-민감성 균주는 프라이머로서 서열번호 3 및 4의 올리고뉴클레오타이드를 사용하는 콜로니 PRC를 사용하여 조사하였다. 결과로서 , 증폭된 단편이 EcoO65I로 절단될 수 없는 균주는 iclR-결핍 균주(202번 △iclR)로서 수득하였다.
실시예 1: evgAS, gadE, 및 ydeO 유전자를 증진시키기 위한 플라스미드의 작제
1-1. evgA 및 evgS 유전자를 증진시키기 위한 플라스미드의 작제
에스케리치아 콜리(에스케리치아 콜리 K-12 균주)의 게놈의 전체 뉴클레오타이드 서열은 이미 보고되었고(Science, 277, 1453-1474 (1997)), 이것은 evgAS가 오페론 구조를 형성하는 것으로 공지되어 있다. 상기한 바와 같이 보고된evgAS 유전자의 뉴클레오타이드 서열(GenBank 승인 번호 AAC75428 및 AAC75429)를 기초로, 5'프라이머로서 HindIII 부위를 갖는 서열번호 17로 나타낸 올리고뉴클레오타이드 및 3' 프라이머로서 EcoRI 부위를 갖는 서열번호 18로 나타낸 올리고뉴클레오타이드를 합성하였다. 이들 프라이머를 사용하여, 주형으로서 에스케리치아 콜리 W3110 균주의 게놈 DNA를 사용하여 PCR을 수행하였고 증폭된 생성물을 제한 엔도뉴클레아제 HindIII 및 EcoRI로 처리하여 evgAS 유전자를 함유하는 단편을 수득하였다. 정제된 PCR 생성물을 HindIII 및 EcoRI로 분해된 벡터 pMW118(Nippon Gene Co., Ltd.)에 연결함에 이어서, evgAS 오페론을 증폭시키기 위한 플라스미드 pMW-evgAS를 작제하였다.
1-2. gadE를 증진시키기 위한 플라스미드의 작제
에스케리치아 콜리(에스케리치아 콜리 K-12 균주)의 게놈의 전체 뉴클레오타이드 서열은 이미 보고되었다(Science, 277, 1453-1474 (1997)). 상기한 바와 같이 보고된 gadE 유전자의 뉴클레오타이드 서열(GenBank 승인 번호 AAC76537)를 기초로, 5'프라이머로서 BamHI 부위를 갖는 서열번호 19로 나타낸 올리고뉴클레오타이드 및 3' 프라이머로서 HindII 부위를 갖는 서열번호 20으로 나타낸 올리고뉴클레오타이드를 합성하였다. 이들 프라이머를 사용하여, 주형으로서 에스케리치아 콜리 W3110 균주의 게놈 DNA를 사용하여 PCR을 수행하였고 증폭된 생성물을 제한 엔도뉴클레아제 HindIII 및 BamHI로 처리하여 gadE 유전자를 함유하는 단편을 수득하였다. 정제된 PCR 생성물을 HindIII 및 BamHI로 분해된 벡터 pMW118(Nippon Gene Co., Ltd.)에 연결함에 이어서, gadE를 증폭시키기 위한 플라스미드 pMW-gadE를 작제하였다.
1-3. ydeO를 증진시키기 위한 플라스미드의 작제
에스케리치아 콜리(에스케리치아 콜리 K-12 균주)의 게놈의 전체 뉴클레오타이드 서열은 이미 보고되었다(Science, 277, 1453-1474 (1997)). 상기한 바와 같이 보고된 ydeO 유전자의 뉴클레오타이드 서열(GenBank 승인 번호 AAC74572)를 기초로, 5'프라이머로서 HindIII 부위를 갖는 서열번호 21로 나타낸 올리고뉴클레오타이드 및 3' 프라이머로서 EcoRI 부위를 갖는 서열번호 22로 나타낸 올리고뉴클레오타이드를 합성하였다. 이들 프라이머를 사용하여, 주형으로서 에스케리치아 콜리 W3110 균주의 게놈 DNA를 사용하여 PCR을 수행하였고 증폭된 생성물을 제한 엔도뉴클레아제 HindIII 및 EcoRI로 처리하여 gadE 유전자를 함유하는 단편을 수득하였다. 정제된 PCR 생성물을 HindIII 및 BamHI로 분해된 벡터 pMW118(Nippon Gene Co., Ltd.)에 연결함에 이어서, ydeO를 증폭시키기 위한 플라스미드 pMW-ydeO를 작제하였다.
실시예 2: 에스케리치아 속의 세균의 L-트립토판 생산 균주에 대한 evgAS, ydeO, 및 gadE 유전자 증폭의 효과
참조 실시예 1에서 작제된 L-트립토판-생산 균주 202번△iclR을 실시예 1에서 작제된 gadE-증폭 플라스미드 pMW-gadE, evgAS-증폭 플라스미드 pMW-evgAS, 및 ydeO-증폭 플라스미드 pMW-ydeO로 형질전환시킴에 이어서 암피실린 내성 균주를 수득하였다. 당해 플라스미드가 도입된 것을 확인한 후, gadE-증폭 플라스미드 pMW-gadEwas가 도입된 균주를 202번 △iclR/gadE 균주로 지정하였고; evgAS-증폭 플라스미드 pMW-evgAS가 도입된 균주를 202번 △iclR/evgAS 균주로 지정하였고; ydeO-증폭 플라스미드 pMW-ydeO가 도입된 균주를 202번 △iclR/ydeO 균주로 지정하였다.
evgAS, ydeO, 또는 gadE를 202번 △iclR 균주 이외의 공지된 L-트립토판 생산 세균을 사용하여 동일한 방식으로 증폭시킬 수 있다.
상기된 바와 같이 작제된 균주를, OD600이 약 0.6이 될 때까지 37℃에서 50 mg/L 암피실린을 함유하는 LB 배지에서 배양하였다. 이어서, 동일한 용적의 40% 글리세롤 용액을 배양 브로쓰에 첨가하고 교반함에 이어서 적당량을 분배하고 -80℃에서 저장하여 글리세롤 스톡을 제조하였다.
이들 균주의 글리세롤 스톡을 용융시킨 후, 각각 100 mL을 50 mg/L 암피실린을 함유하는 L 플레이트상으로 균일하게 도말하고 당해 플레이트를 24시간동안 37℃에서 배양하였다. 플레이트상의 세포 약 8분의 1을 500 mL의 사카구치 플라스크에서 50ml의 암피실린을 함유한 20mL의 발효 배지에 접종하고 왕복 진탕 배양기를 사용하여 48시간동안 37℃에서 배양하였다. 배양 후, 배지에 축적된 L-트립토판의 양은 아미노산 분석기 L-8500(Hitachi)를 사용하여 측정하였다. 배양을 위해 사용 된 배지 조성은 다음과 같다.
L-트립토판-생산 배지:
글루코스 40 g/L
(NH4)2SO4 15 g/L
KH2PO4 1.5 g/L
MgSO4 7H2O 0.3 g/L
FeSO4 7H2O 0.01 g/L
MnSO47H2O 0.01 g/L
효모 추출물 2.0 g/L
티아민HCl 0.005 g/L
피리독신 0.03 g/L
L-Met 0.05 g/L
L-Phe 0.1 g/L
L-Tyr 0.1 g/L
CaCO3 30 g/L
KOH를 사용하여 pH 7.0으로 조정하고, 20분동안 120℃에서 오토클레이빙하였다. 글루코스 및 MgSO47H2O를 혼합하고 기타 성분과는 별도로 멸균하였다. CaCO3를 건열 멸균 후 첨가하였다.
48시간에서 OD600 및 L-트립토판 축적은 표 1에 나타낸다.
evgAS, ydeO, 및 gadE 유전자 증폭된 균주인 202번△iclR/evgAS, 202번△iclR/ydeO, 및 202번△iclR/gadE 각각은 대조군 202번△iclR과 비교하여 L-트립토판 축적의 증가를 나타내었다.
실시예 3: 에스케리치아 속의 세균의 L-트레오닌-생산 균주에 대한 evgAS, ydeO, 및 gadE 증폭의 효과
에스케리치아 콜리 VKPM B-5318 균주(문헌참조: EP0593792)를 에스케리치아 속의 세균의 L-트레오닌-생산 균주로서 사용하였다.
VKPM B-5318 균주는 실시예 1에서 작제된 gadE-증폭 플라스미드 pMW-gadE, evgAS-증폭 플라스미드 pMW-evgAS, 및 ydeO-증폭 플라스미드 pMW-ydeO로 형질전환시킴에 이어서 암피실린 내성 균주를 수득하였다. 이들 플라스미드가 도입된 것을 확인한 후, gadE-증폭 플라스미드 pMW-gadE가 도입된 균주를 B5318/gadE 균주로서 지정하고; evgAS-증폭 플라스미드 pMW-evgAS가 도입된 균주를 B5318/evgAS 균주로서 지정하고; ydeO-증폭 플라스미드 pMW-ydeO가 도입된 균주를 B5318/ydeO 균주로서 지정하였다.
evgAS, ydeO, 또는 gadE는 VKPM B-5318 균주 이외의 공지된 L-트레오닌 생산 세균을 사용하여 동일한 방식으로 증폭시킬 수 있다.
상기된 바와 같이 작제된 균주를, OD600이 약 0.6이 될 때까지 37℃에서 50 mg/L 암피실린을 함유하는 LB 배지에서 배양하였다. 이어서, 동일한 용적의 40% 글리세롤 용액을 배양 브로쓰에 첨가하고 교반함에 이어서 적당량을 분배하고 -80℃에서 저장하여 글리세롤 스톡을 제조하였다.
이들 균주의 글리세롤 스톡을 용융시킨 후, 각각 100 mL을 50 mg/L 암피실린을 함유하는 L 플레이트상으로 균일하게 도말하고 당해 플레이트를 24시간동안 37℃에서 배양하였다. 플레이트상의 세포 약 8분의 1을 500 mL의 사카구치 플라스크에서 50ml의 암피실린을 함유한 하기된 바와 같은 20mL의 발효 배지에 접종하고 왕복 진탕 배양기를 사용하여 48시간동안 37℃에서 배양하였다. 배양 후, 배지에 축적된 L-트레오닌의 양은 아미노산 분석기 L-8500(Hitachi)를 사용하여 측정하였다. 배양을 위해 사용된 배지 조성은 다음과 같다.
L-트레오닌-생산 배지:
글루코스 40g/L
(NH4)2SO4 16g/L
KH2PO4 1.0g/L
MgSO4 7H2O 1.0g/L
FeSO4 7H2O 0.01g/L
MnSO47H2O 0.01g/L
효모 추출물 2.0g/L
CaCO3 (일본 약전) 30g/L
KOH를 사용하여 pH 7.0으로 조정하고, 20분동안 120℃에서 오토클레이빙하였다. 글루코스 및 MgSO47H2O를 혼합하고 별도로 멸균하였다. CaCO3를 건열 멸균 후 첨가하였다.
48시간에서 OD600 및 L-트립토판 축적은 표 2에 나타낸다.
evgAS, ydeO, 및 gadE 유전자 증폭된 균주인 B5318/evgAS, B5318/ydeO, 및 B5318/gadE 각각은 대조군 VKPM B-5318과 비교하여 L-트레오닌 축적의 증가를 나타내었다.
실시예 4: L-라이신-생산 세균의 작제
4-1. 라이신 데카복실라제를 암호화하는 cadA 및 ldcC 유전자가 파괴된 균주의 작제
먼저, 라이신 데카복실라제 비-생산 균주를 작제하였다. 라이신 데카복실라제 이소자임은 cadA 유전자(GenBank 승인번호 NP_418555. 서열번호 31) 및 ldcC 유전자(GenBank 승인번호 NP_414728. 서열번호 33) (문헌참조 WO96/17930)에 의해 암호화되어 있다. AEC (S-(2-아미노에틸)-시스테인)-내성 균주인 WC196 균주(문헌참조: WO96/17930)는 에스케리치아 콜리 L-라이신 생산 균주에 대해 모균주로서 사용하였다.
라이신 데카복실라제를 암호화하는 cadA 및 ldcC 유전자는 다첸코 및 와너(Datsenko and Wanner) (Proc. Natl. Acad. Sci. USA. 97. 6640-6645 (2000))에 의해 처음 개발된 "레드-구동 통합"으로 불리우는 방법 및 파아지 절단 시스템(J. Bacteriol. 184. 5200-5203 (2002))을 사용하여 결실시켰다. "레드 구동 통합" 방법에 따라, 프라이머로서 표적 유전자의 일부가 5' 말단에 디자인되고 항생제 내성 유전자가 3' 말단에 디자인된 올리고뉴클레오타이드를 사용하여 수득된 PCR 생성물을 사용하여 단일 단계로 유전자 붕괴된 균주를 작제할 수 있다. 추가로, 파아지 절단 시스템과 조합하여, 유전자 붕괴된 균주로 통합된 항생제 내성 유전자를 제거할 수 있다(JP2005-058227A).
4-2. cadA 유전자의 붕괴
플라스미드 pMW118-attL-Cm-attR (WO2005/010175)을 PCR 주형으로서 사용하였다. pMW118-attL-Cm-attR은 파아지의 접착 부위인 attL 및 attR 유전자, 및 항생제 내성 유전자인 cat 유전자가 pMW118 (Takara Bio Inc.)에 attL-cat-attR의 순서로 삽입된 플라스미드이다.
PCR은 프라이머로서 서열번호 35 및 36으로 나타낸 합성 올리고뉴클레오타이드를 사용하여 수행하였고 여기서 각각의 프라이머는 3' 말단에서 attL 및 attR 의 각 말단에 상응하는 서열을 갖고 5' 말단에서 표적 cadA 유전자의 일부에 상응하는 서열을 갖는다.
PCR 생성물은 아가로스 겔로 정제함에 이어서 전기천공에 의해, 온도 민감성 복제 능력을 갖는 플라스미드 pKD46를 함유하는 에스케리치아 콜리 WC196으로 도입하였다. 플라스미드 pKD46 (Proc. Natl. Acad. Sci. USA. 97. 6640-6645 (2000))은 아라비노스 유도된 ParaB 프로모터(GenBank/EMBL 승인 번호 J02459, 31088th 33241st)에 의해 조절되는 레드 상동성 재조합 시스템에서 레드 리컴비나제를 암호화하는 유전자(γ, β, exo 유전자)를 포함하는 전체 2154 염기의 λ 파아지 DNA 단편을 포함한다.
전기천공을 위한 컴피턴트 세포를 하기와 같이 제조하였다. 즉, 100 mg/L의 암피실린을 함유하는 LB 배지에서 30℃에서 밤새 배양된 에스케리치아 콜리 WC196 균주는암피실린(20 mg/L) 및 L-아라비노스(1 mM)을 함유하는 5ml의 SOB 배지에서 100배 희석하였다(Molecular Cloning: Lab Manual 2nd edition, Sambrook, J., et al., Cold Spring Harbor Laboratory Press (1989)). 희석된 현탁액을 OD 600이 약 0.6이 될 때까지 30℃에서 통기시킴에 이어서 현탁액을 100배 농축시키고 전기천공에서 즉시 사용가능 하도록 10% 글리세롤로 3회 세척하였다. 전기천공은 70μL 컴피턴트 세포 및 약 100ng PCR 생성물을 사용하여 수행하였다. 1 mL의 SOC 배지(Molecular cloning: Lab Manual 2nd edition, Sambrook, J., et al., Cold Spring Harbor Laboratory Press (1989))를 전기천공후 세포에 첨가하고 2.5시간동안 37℃에서 배양함에 이어서 Cm(클로람페니콜) (25 mg/L)을 함유하는 L-한천의 플레이트 배지상에서 37℃에서 배양함에 이어서 Cm-내성 재조합체를 선별하였다. 이어서, pKD46 플라스미드를 제거하기 위해, 재조합체를 Cm을 함유하는 L-한천 배지상에서 42℃에서 2회 계대배양하고 수득된 콜로니의 암피실린 내성을 시험하고 pKD46이 제거된 암피실린 민감성 균주를 수득하였다.
클로람페니콜 내성 유전자에 의해 동정된 돌연변이체내 cadA 유전자의 결실은 PCR을 사용하여 확인하였다. 수득된 cadA 결핍 균주는 WC196△cadA::att-cat 균주로 지정하였다.
이어서, cadA 유전자로 도입된 att-cat 유전자를 제거하기 위해, 헬퍼 플라스미드, pMW-intxis-ts (WO2005/010175)를 사용하였다. pMW-intxis-ts는 파아지 인테그라제(Int)를 암호화하는 유전자 및 엑시시오나제(Xis)를 암호화하는 유전자를 함유하는 플라스미드이다.
상기된 바와 같이 수득된 WC196△cadA::att-cat 균주의 컴피턴트 세포는 통상의 방법을 사용하여 제조하였고 헬퍼 플라스미드 pMW-intxis-ts로 형질전환시키고, 30℃에서 50 mg/L 암피실린을 함유하는 L-한천의 플레이트 배지상에서 배양함에 따라서 암피실린 내성 균주를 선별하였다.
이어서, pMW-intxis-ts 플라스미드를 제거하기 위해, 암피실린 내성 형질전환체를 42℃에서 L-한천 배지상에서 2회 계대배양하고, 수득된 콜로니의 암피실린 내성 및 클로람페니콜 내성을 시험하고 att-cat 및 pMW-intxis-ts가 제거된 클로람페니콜 및 암피실린 민감성 균주를 수득하였다. 당해 균주를 WC196△cadA로 지정하였다.
4-3. WC196△cadA 균주에서 ldcC 유전자의 붕괴
WC196△cadA 균주에서 ldcC 유전자는 ldcC 붕괴 프라이머로서 서열번호 37 및 38을 사용하여 상기된 바와 같은 기술에 따라 결실시켰다. 따라서, cadA, ldcC-붕괴된 균주인 WC196△cadAldcC을 수득하였다.
실시예 5: 에스케리치아 속의 세균의 L-라이신 생산 균주에 대한 evgAS 증폭 효과
5-1. WC196△cadAldcC 균주로의 라이신 생산 플라스미드의 도입
통상적인 방법에 따라, WC196△cadAldcC 균주는 dapA, dapB, 및 lysC 유전자(WO01/53459)를 함유하는 라이신 생산 플라스미드 pCAB1으로 형질전환시켜 WC196△cadAldcC/pCAB1 균주(WC196LC/pCAB1)를 수득하였다.
WC196LC/pCAB1 균주를 실시예 1에서 작제된 evgAS-증폭 플라스미드 pMW-evgAS로 형질전환시킴에 따라 암피실린 내성 균주를 수득하였다. 당해 플라스미드가 도입되는지를 확인한 후 evgAS-증폭 플라스미드 pMW-evgAS-도입된 균주를 WC196LC/pCAB1/evgAS 균주로 지정하였다.
evgAS는 WC196LC/pCAB1 균주 이외의 공지된 L-라이신 생산 세균을 사용하여 동일한 방식으로 증폭시킬 수 있다.
상기된 바와 같이 작제된 균주는 OD 600이 약 0.6이 될 때까지 37℃에서 25 mL 스트렙토마이신 및 50 mg/L 암피실린을 함유하는 LB 배지에서 배양하였다. 이어서, 동일 용적의 40% 글리세롤 용액을 배양 브로쓰에 첨가하고 교반시킴에 이어서 적당량을 분배하고 -80℃에서 저장하여 글리세롤 스톡을 제조하였다.
5-2. 라이신 생산 배양
이들 균주의 글리세롤 스톡을 용융시킨 후, 각각 100 mL을 50 mg/L 암피실린을 함유하는 L 플레이트상으로 균일하게 도말하고 당해 플레이트를 24시간동안 37℃에서 배양하였다. 플레이트상의 세포 약 8분의 1을 500 mL의 사카구치 플라스크에서 50ml의 암피실린을 함유한 하기된 바와 같은 20mL의 발효 배지에 접종하고 왕복 진탕 배양기를 사용하여 48시간동안 37℃에서 배양하였다. 배양 후, 배지에 축적된 L-라이신의 양은 바이오텍-분석기 AS210(Sakura Seiki)를 사용하여 측정하였다. 배양을 위해 사용된 배지 조성은 다음과 같다.
L-라이신 생산 배지:
글루코스 40g/L
(NH4)2SO4 16g/L
KH2PO4 1.0g/L
MgSO4 7H2O 1.0g/L
FeSO4 7H2O 0.01g/L
MnSO47H2O 0.01g/L
효모 추출물 2.0g/L
CaCO3 (일본 약전) 30g/L
KOH를 사용하여 pH 7.0으로 조정하고, 20분동안 120℃에서 오토클레이빙하였다. 글루코스 및 MgSO47H2O를 혼합하고 별도로 멸균하였다. CaCO3를 건열 멸균 후 첨가하였다.
48시간에서 OD600 및 L-라이신 축적은 표 3에 나타낸다.
evgAS 유전자 증폭된 균주인 WC196LC/pCAB1/evgAS는 대조군 WC196LC/pCAB1과 비교하여 L-라이신의 축적이 상당히 증가함을 나타냈다.
실시예 6: 에스케리치아 속의 세균의 L-라이신 생산 균주에 대한 gadE 축적의 효과
6-1. gadE 유전자가 증진된 L-라이신 생산 균주의 작제
gadE 유전자 단편은 실시예 1에서 작제된 에스케리치아 콜리 W3110 균주의 gadE 유전자를 함유하는 플라스미드 pMW-gadE로부터 절단하고 단편을, HindIII 및 BamHI로 분해된 벡터 pUC18(Takara Shuzo)에 연결하여 gadE-증폭 플라스미드pUC-gadE를 수득하였다.
WC196LC/pCAB1 균주를 상기된 pUC-gadE로 형질전환시킴에 따라서 암피실린 내성 균주를 수득하였다. 당해 플라스미드가 도입되었는지를 확인한 후, gadE-증폭 플라스미드 pUC-gadE가 도입된 균주를 WC196LC/pCAB1/pUC-gadE 균주로 지정하였다.
evgAS, ydeO, 또는 gadE는 WC196LC/pCAB1이외의 공지된 L-라이신 생산 세균을 사용하여 동일한 방식으로 증폭시킬 수 있다. 증폭은 또한 evgAS, ydeO, 또는 gadE 유전자의 조합으로 수행할 수 있다.
상기된 바와 같이 작제된 균주는 OD 600이 약 0.6이 될 때까지 37℃에서 25 mL 스트렙토마이신 및 50 mg/L 암피실린을 함유하는 LB 배지에서 배양하였다. 이어서, 동일 용적의 40% 글리세롤 용액을 배양 브로쓰에 첨가하고 교반시킴에 이어서 적당량을 분배하고 -80℃에서 저장하여 글리세롤 스톡을 제조하였다.
6-2. 라이신 생산 배양
이들 균주의 글리세롤 스톡을 용융시킨 후, 각각 100 mL을 25mg/L 스트렙토마이신 및 50 mg/L 암피실린을 함유하는 L 플레이트상으로 균일하게 도말하고 당해 플레이트를 24시간동안 37℃에서 배양하였다. 플레이트상의 세포 약 8분의 1을 500 mL의 사카구치 플라스크에서 25mg/L 스트렙토마이신 및 50 mg/L 암피실린을 함유한 하기된 바와 같은 20mL의 발효 배지에 접종하고 왕복 진탕 배양기를 사용하여 48시간동안 37℃에서 배양하였다. 배양 후, 배지에 축적된 L-라이신의 양은 바이오텍-분석기 AS210(Sakura Seiki)를 사용하여 측정하였다. 배양을 위해 사용된 배지 조성은 다음과 같다.
L-라이신 생산 배지:
글루코스 또는 프럭토스 40g/L
(NH4)2SO4 16g/L
KH2PO4 1.0g/L
MgSO4 7H2O 1.0g/L
FeSO4 7H2O 0.01g/L
MnSO47H2O 0.01g/L
이소류신 0.1 g/L
효모 추출물 2.0g/L
CaCO3 (일본 약전) 30g/L
KOH를 사용하여 pH 7.0으로 조정하고, 20분동안 120℃에서 오토클레이빙하였다. 글루코스 및 MgSO47H2O를 혼합하고 별도로 멸균하였다. CaCO3를 건열 멸균 후 첨가하였다.
48시간에서 OD600 및 L-라이신 축적은 표 4에 나타낸다.
gadE 유전자-증폭된 균주 WC196LC/pCAB1/pUCgadE는 대조군 WC196LC/pCAB1과 비교하여 글루코스 배양 및 프럭토스 배양 둘다에서 L-라이신의 축적에서 증가를 나타내었고, 특히, 프럭토스 배양에서 L-라이신의 축적이 상당히 증가하였다.
본 발명의 미생물을 사용함에 의해, L-아미노산, 특히, L-라이신, L-트레오닌, 및 L-트립토판을 발효에 의해 효율적으로 생산할 수 있다.
서열목록의 설명
서열번호 1: trp 오페론을 증폭시키기 위한 프라이머
서열번호 2: trp 오페론을 증폭시키기 위한 프라이머
서열번호 3: iclR 유전자를 증폭시키기 위한 프라이머
서열번호 4: iclR 유전자를 증폭시키기 위한 프라이머
서열번호 5: iclR 유전자의 뉴클레오타이드 서열
서열번호 6: iclR 유전자에 의해 암호화화된 아미노산의 서열
서열번호 7: aceA 유전자의 뉴클레오타이드 서열
서열번호 8: aceA 유전자에 의해 암호화된 아미노산의 서열
서열번호 9: aceB 유전자의 뉴클레오타이드 서열
서열번호 10: aceB 유전자에 의해 암호화된 아미노산 서열
서열번호 11: aceK 유전자의 뉴클레오타이드 서열
서열번호 12: aceK 유전자에 의해 암호화된 아미노산 서열
서열번호 13: trpA 유전자의 뉴클레오타이드 서열
서열번호 14: trpA 유전자에 의해 암호화된 아미노산 서열
서열번호 15: trpB 유전자의 뉴클레오타이드 서열
서열번호 16: trpB 유전자에 의해 암호화된 아미노산의 서열
서열번호 17: evgAS 오페론을 증폭시키기 위한 프라이머
서열번호 18: evgAS 오페론을 증폭시키기 위한 프라이머
서열번호 19: gadE 유전자를 증폭시키기 위한 프라이머
서열번호 20: gadE 유전자를 증폭시키기 위한 프라이머
서열번호 21: ydeO 유전자를 증폭시키기 위한 프라이머
서열번호 22: ydeO 유전자를 증폭시키기 위한 프라이머
서열번호 23: evgA 유전자의 뉴클레오타이드 서열
서열번호 24: EvgA의 아미노산 서열
서열번호 25: evgS 유전자의 뉴클레오타이드 서열
서열번호 26: EvgS의 아미노산 서열
서열번호 27: gadE 유전자의 뉴클레오타이드 서열
서열번호 28: GadE 아미노산 서열
서열번호 29: ydeO 유전자의 뉴클레오타이드 서열
서열번호 30: YdeO의 아미노산 서열
서열번호 31: cadA 유전자의 뉴클레오타이드 서열
서열번호 32: cadA 유전자에 의해 암호화된 아미노산의 서열
서열번호 33: ldcC 유전자의 뉴클레오타이드 서열
서열번호 34: ldcC 유전자에 의해 암호화된 아미노산 서열
서열번호 35: cadA 유전자를 붕괴시키기 dln한 PCR 프라이머
서열번호 36: cadA 유전자를 붕괴시키기 위한 PCR 프라이머
서열번호 37: ldc 유전자를 붕괴시키기 위한 PCR 프라이머
서열번호 38: ldc 유전자를 붕괴시키기 위한 PCR 프라이머
<110> Ajinomoto Co., Inc.
<120> An L-Amino Acid Producing Bacterium and a Method for Producing
an L-Amino Acid
<130> C557-C6193
<150> JP2005-279027
<151> 2005-09-27
<150> US60/723936
<151> 2005-10-06
<150> JP2006-213584
<151> 2006-08-04
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<210> 1
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<220>
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cgcatctcga ctgcacggtg 20
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<220>
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gccgaattca agtgtgtgaa gtgtatg 27
<210> 4
<211> 27
<212> DNA
<213> Artificial
<220>
<223> primer
<400> 4
gccaagcttc cgacacgctc aacccag 27
<210> 5
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<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(864)
<400> 5
atg aaa atg att tcc acg ata cag aaa aaa gag act gtc atg gtc gca 48
Met Lys Met Ile Ser Thr Ile Gln Lys Lys Glu Thr Val Met Val Ala
1 5 10 15
ccc att ccc gcg aaa cgc ggc aga aaa ccc gcc gtt gcc acc gca cca 96
Pro Ile Pro Ala Lys Arg Gly Arg Lys Pro Ala Val Ala Thr Ala Pro
20 25 30
gcg act gga cag gtt cag tct tta acg cgt ggc ctg aaa tta ctg gag 144
Ala Thr Gly Gln Val Gln Ser Leu Thr Arg Gly Leu Lys Leu Leu Glu
35 40 45
tgg att gcc gaa tcc aat ggc agt gtg gca ctc acg gaa ctg gcg caa 192
Trp Ile Ala Glu Ser Asn Gly Ser Val Ala Leu Thr Glu Leu Ala Gln
50 55 60
caa gcc ggg tta ccc aat tcc acg acc cac cgc ctg cta acc acg atg 240
Gln Ala Gly Leu Pro Asn Ser Thr Thr His Arg Leu Leu Thr Thr Met
65 70 75 80
caa cag cag ggt ttc gtg cgt cag gtt ggc gaa ctg gga cat tgg gca 288
Gln Gln Gln Gly Phe Val Arg Gln Val Gly Glu Leu Gly His Trp Ala
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atc ggc gca cat gcc ttt atg gtc ggc agc agc ttt ctc cag agc cgt 336
Ile Gly Ala His Ala Phe Met Val Gly Ser Ser Phe Leu Gln Ser Arg
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aat ttg tta gcg att gtt cac cct atc ctg cgc aat cta atg gaa gag 384
Asn Leu Leu Ala Ile Val His Pro Ile Leu Arg Asn Leu Met Glu Glu
115 120 125
tct ggc gaa acg gtc aat atg gcg gtg ctt gat caa agc gat cac gaa 432
Ser Gly Glu Thr Val Asn Met Ala Val Leu Asp Gln Ser Asp His Glu
130 135 140
gcg att att atc gac cag gta cag tgt acg cat ctg atg cga atg tcc 480
Ala Ile Ile Ile Asp Gln Val Gln Cys Thr His Leu Met Arg Met Ser
145 150 155 160
gcg cct atc ggc ggt aaa ttg ccg atg cac gct tcc ggt gcg ggt aaa 528
Ala Pro Ile Gly Gly Lys Leu Pro Met His Ala Ser Gly Ala Gly Lys
165 170 175
gcc ttt tta gcc caa ctg agc gaa gaa cag gtg acg aag ctg ctg cac 576
Ala Phe Leu Ala Gln Leu Ser Glu Glu Gln Val Thr Lys Leu Leu His
180 185 190
cgc aaa ggg tta cat gcc tat acc cac gca acg ctg gtg tct cct gtg 624
Arg Lys Gly Leu His Ala Tyr Thr His Ala Thr Leu Val Ser Pro Val
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cat tta aaa gaa gat ctc gcc caa acg cgc aaa cgg ggt tat tca ttt 672
His Leu Lys Glu Asp Leu Ala Gln Thr Arg Lys Arg Gly Tyr Ser Phe
210 215 220
gac gat gag gaa cat gca ctg ggg cta cgt tgc ctt gca gcg tgt att 720
Asp Asp Glu Glu His Ala Leu Gly Leu Arg Cys Leu Ala Ala Cys Ile
225 230 235 240
ttc gat gag cac cgt gaa ccg ttt gcc gca att tct att tcc gga ccg 768
Phe Asp Glu His Arg Glu Pro Phe Ala Ala Ile Ser Ile Ser Gly Pro
245 250 255
att tca cgt att acc gat gac cgc gtg acc gag ttt ggc gcg atg gtg 816
Ile Ser Arg Ile Thr Asp Asp Arg Val Thr Glu Phe Gly Ala Met Val
260 265 270
att aaa gcg gcg aag gaa gtg acg ctg gcg tac ggt gga atg cgc tga 864
Ile Lys Ala Ala Lys Glu Val Thr Leu Ala Tyr Gly Gly Met Arg
275 280 285
<210> 6
<211> 287
<212> PRT
<213> Escherichia coli
<400> 6
Met Lys Met Ile Ser Thr Ile Gln Lys Lys Glu Thr Val Met Val Ala
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Pro Ile Pro Ala Lys Arg Gly Arg Lys Pro Ala Val Ala Thr Ala Pro
20 25 30
Ala Thr Gly Gln Val Gln Ser Leu Thr Arg Gly Leu Lys Leu Leu Glu
35 40 45
Trp Ile Ala Glu Ser Asn Gly Ser Val Ala Leu Thr Glu Leu Ala Gln
50 55 60
Gln Ala Gly Leu Pro Asn Ser Thr Thr His Arg Leu Leu Thr Thr Met
65 70 75 80
Gln Gln Gln Gly Phe Val Arg Gln Val Gly Glu Leu Gly His Trp Ala
85 90 95
Ile Gly Ala His Ala Phe Met Val Gly Ser Ser Phe Leu Gln Ser Arg
100 105 110
Asn Leu Leu Ala Ile Val His Pro Ile Leu Arg Asn Leu Met Glu Glu
115 120 125
Ser Gly Glu Thr Val Asn Met Ala Val Leu Asp Gln Ser Asp His Glu
130 135 140
Ala Ile Ile Ile Asp Gln Val Gln Cys Thr His Leu Met Arg Met Ser
145 150 155 160
Ala Pro Ile Gly Gly Lys Leu Pro Met His Ala Ser Gly Ala Gly Lys
165 170 175
Ala Phe Leu Ala Gln Leu Ser Glu Glu Gln Val Thr Lys Leu Leu His
180 185 190
Arg Lys Gly Leu His Ala Tyr Thr His Ala Thr Leu Val Ser Pro Val
195 200 205
His Leu Lys Glu Asp Leu Ala Gln Thr Arg Lys Arg Gly Tyr Ser Phe
210 215 220
Asp Asp Glu Glu His Ala Leu Gly Leu Arg Cys Leu Ala Ala Cys Ile
225 230 235 240
Phe Asp Glu His Arg Glu Pro Phe Ala Ala Ile Ser Ile Ser Gly Pro
245 250 255
Ile Ser Arg Ile Thr Asp Asp Arg Val Thr Glu Phe Gly Ala Met Val
260 265 270
Ile Lys Ala Ala Lys Glu Val Thr Leu Ala Tyr Gly Gly Met Arg
275 280 285
<210> 7
<211> 1305
<212> DNA
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<220>
<221> CDS
<222> (1)..(1305)
<400> 7
atg aaa acc cgt aca caa caa att gaa gaa tta cag aaa gag tgg act 48
Met Lys Thr Arg Thr Gln Gln Ile Glu Glu Leu Gln Lys Glu Trp Thr
1 5 10 15
caa ccg cgt tgg gaa ggc att act cgc cca tac agt gcg gaa gat gtg 96
Gln Pro Arg Trp Glu Gly Ile Thr Arg Pro Tyr Ser Ala Glu Asp Val
20 25 30
gtg aaa tta cgc ggt tca gtc aat cct gaa tgc acg ctg gcg caa ctg 144
Val Lys Leu Arg Gly Ser Val Asn Pro Glu Cys Thr Leu Ala Gln Leu
35 40 45
ggc gca gcg aaa atg tgg cgt ctg ctg cac ggt gag tcg aaa aaa ggc 192
Gly Ala Ala Lys Met Trp Arg Leu Leu His Gly Glu Ser Lys Lys Gly
50 55 60
tac atc aac agc ctc ggc gca ctg act ggc ggt cag gcg ctg caa cag 240
Tyr Ile Asn Ser Leu Gly Ala Leu Thr Gly Gly Gln Ala Leu Gln Gln
65 70 75 80
gcg aaa gcg ggt att gaa gca gtc tat ctg tcg gga tgg cag gta gcg 288
Ala Lys Ala Gly Ile Glu Ala Val Tyr Leu Ser Gly Trp Gln Val Ala
85 90 95
gcg gac gct aac ctg gcg gcc agc atg tat ccg gat cag tcg ctc tat 336
Ala Asp Ala Asn Leu Ala Ala Ser Met Tyr Pro Asp Gln Ser Leu Tyr
100 105 110
ccg gca aac tcg gtg cca gct gtg gtg gag cgg atc aac aac acc ttc 384
Pro Ala Asn Ser Val Pro Ala Val Val Glu Arg Ile Asn Asn Thr Phe
115 120 125
cgt cgt gcc gat cag atc caa tgg tcc gcg ggc att gag ccg ggc gat 432
Arg Arg Ala Asp Gln Ile Gln Trp Ser Ala Gly Ile Glu Pro Gly Asp
130 135 140
ccg cgc tat gtc gat tac ttc ctg ccg atc gtt gcc gat gcg gaa gcc 480
Pro Arg Tyr Val Asp Tyr Phe Leu Pro Ile Val Ala Asp Ala Glu Ala
145 150 155 160
ggt ttt ggc ggt gtc ctg aat gcc ttt gaa ctg atg aaa gcg atg att 528
Gly Phe Gly Gly Val Leu Asn Ala Phe Glu Leu Met Lys Ala Met Ile
165 170 175
gaa gcc ggt gca gcg gca gtt cac ttc gaa gat cag ctg gcg tca gtg 576
Glu Ala Gly Ala Ala Ala Val His Phe Glu Asp Gln Leu Ala Ser Val
180 185 190
aag aaa tgc ggt cac atg ggc ggc aaa gtt tta gtg cca act cag gaa 624
Lys Lys Cys Gly His Met Gly Gly Lys Val Leu Val Pro Thr Gln Glu
195 200 205
gct att cag aaa ctg gtc gcg gcg cgt ctg gca gct gac gtg acg ggc 672
Ala Ile Gln Lys Leu Val Ala Ala Arg Leu Ala Ala Asp Val Thr Gly
210 215 220
gtt cca acc ctg ctg gtt gcc cgt acc gat gct gat gcg gcg gat ctg 720
Val Pro Thr Leu Leu Val Ala Arg Thr Asp Ala Asp Ala Ala Asp Leu
225 230 235 240
atc acc tcc gat tgc gac ccg tat gac agc gaa ttt att acc ggc gag 768
Ile Thr Ser Asp Cys Asp Pro Tyr Asp Ser Glu Phe Ile Thr Gly Glu
245 250 255
cgt acc agt gaa ggc ttc ttc cgt act cat gcg ggc att gag caa gcg 816
Arg Thr Ser Glu Gly Phe Phe Arg Thr His Ala Gly Ile Glu Gln Ala
260 265 270
atc agc cgt ggc ctg gcg tat gcg cca tat gct gac ctg gtc tgg tgt 864
Ile Ser Arg Gly Leu Ala Tyr Ala Pro Tyr Ala Asp Leu Val Trp Cys
275 280 285
gaa acc tcc acg ccg gat ctg gaa ctg gcg cgt cgc ttt gca caa gct 912
Glu Thr Ser Thr Pro Asp Leu Glu Leu Ala Arg Arg Phe Ala Gln Ala
290 295 300
atc cac gcg aaa tat ccg ggc aaa ctg ctg gct tat aac tgc tcg ccg 960
Ile His Ala Lys Tyr Pro Gly Lys Leu Leu Ala Tyr Asn Cys Ser Pro
305 310 315 320
tcg ttc aac tgg cag aaa aac ctc gac gac aaa act att gcc agc ttc 1008
Ser Phe Asn Trp Gln Lys Asn Leu Asp Asp Lys Thr Ile Ala Ser Phe
325 330 335
cag cag cag ctg tcg gat atg ggc tac aag ttc cag ttc atc acc ctg 1056
Gln Gln Gln Leu Ser Asp Met Gly Tyr Lys Phe Gln Phe Ile Thr Leu
340 345 350
gca ggt atc cac agc atg tgg ttc aac atg ttt gac ctg gca aac gcc 1104
Ala Gly Ile His Ser Met Trp Phe Asn Met Phe Asp Leu Ala Asn Ala
355 360 365
tat gcc cag ggc gag ggt atg aag cac tac gtt gag aaa gtg cag cag 1152
Tyr Ala Gln Gly Glu Gly Met Lys His Tyr Val Glu Lys Val Gln Gln
370 375 380
ccg gaa ttt gcc gcc gcg aaa gat ggc tat acc ttc gta tct cac cag 1200
Pro Glu Phe Ala Ala Ala Lys Asp Gly Tyr Thr Phe Val Ser His Gln
385 390 395 400
cag gaa gtg ggt aca ggt tac ttc gat aaa gtg acg act att att cag 1248
Gln Glu Val Gly Thr Gly Tyr Phe Asp Lys Val Thr Thr Ile Ile Gln
405 410 415
ggc ggc acg tct tca gtc acc gcg ctg acc ggc tcc act gaa gaa tcg 1296
Gly Gly Thr Ser Ser Val Thr Ala Leu Thr Gly Ser Thr Glu Glu Ser
420 425 430
cag ttc taa 1305
Gln Phe
<210> 8
<211> 434
<212> PRT
<213> Escherichia coli
<400> 8
Met Lys Thr Arg Thr Gln Gln Ile Glu Glu Leu Gln Lys Glu Trp Thr
1 5 10 15
Gln Pro Arg Trp Glu Gly Ile Thr Arg Pro Tyr Ser Ala Glu Asp Val
20 25 30
Val Lys Leu Arg Gly Ser Val Asn Pro Glu Cys Thr Leu Ala Gln Leu
35 40 45
Gly Ala Ala Lys Met Trp Arg Leu Leu His Gly Glu Ser Lys Lys Gly
50 55 60
Tyr Ile Asn Ser Leu Gly Ala Leu Thr Gly Gly Gln Ala Leu Gln Gln
65 70 75 80
Ala Lys Ala Gly Ile Glu Ala Val Tyr Leu Ser Gly Trp Gln Val Ala
85 90 95
Ala Asp Ala Asn Leu Ala Ala Ser Met Tyr Pro Asp Gln Ser Leu Tyr
100 105 110
Pro Ala Asn Ser Val Pro Ala Val Val Glu Arg Ile Asn Asn Thr Phe
115 120 125
Arg Arg Ala Asp Gln Ile Gln Trp Ser Ala Gly Ile Glu Pro Gly Asp
130 135 140
Pro Arg Tyr Val Asp Tyr Phe Leu Pro Ile Val Ala Asp Ala Glu Ala
145 150 155 160
Gly Phe Gly Gly Val Leu Asn Ala Phe Glu Leu Met Lys Ala Met Ile
165 170 175
Glu Ala Gly Ala Ala Ala Val His Phe Glu Asp Gln Leu Ala Ser Val
180 185 190
Lys Lys Cys Gly His Met Gly Gly Lys Val Leu Val Pro Thr Gln Glu
195 200 205
Ala Ile Gln Lys Leu Val Ala Ala Arg Leu Ala Ala Asp Val Thr Gly
210 215 220
Val Pro Thr Leu Leu Val Ala Arg Thr Asp Ala Asp Ala Ala Asp Leu
225 230 235 240
Ile Thr Ser Asp Cys Asp Pro Tyr Asp Ser Glu Phe Ile Thr Gly Glu
245 250 255
Arg Thr Ser Glu Gly Phe Phe Arg Thr His Ala Gly Ile Glu Gln Ala
260 265 270
Ile Ser Arg Gly Leu Ala Tyr Ala Pro Tyr Ala Asp Leu Val Trp Cys
275 280 285
Glu Thr Ser Thr Pro Asp Leu Glu Leu Ala Arg Arg Phe Ala Gln Ala
290 295 300
Ile His Ala Lys Tyr Pro Gly Lys Leu Leu Ala Tyr Asn Cys Ser Pro
305 310 315 320
Ser Phe Asn Trp Gln Lys Asn Leu Asp Asp Lys Thr Ile Ala Ser Phe
325 330 335
Gln Gln Gln Leu Ser Asp Met Gly Tyr Lys Phe Gln Phe Ile Thr Leu
340 345 350
Ala Gly Ile His Ser Met Trp Phe Asn Met Phe Asp Leu Ala Asn Ala
355 360 365
Tyr Ala Gln Gly Glu Gly Met Lys His Tyr Val Glu Lys Val Gln Gln
370 375 380
Pro Glu Phe Ala Ala Ala Lys Asp Gly Tyr Thr Phe Val Ser His Gln
385 390 395 400
Gln Glu Val Gly Thr Gly Tyr Phe Asp Lys Val Thr Thr Ile Ile Gln
405 410 415
Gly Gly Thr Ser Ser Val Thr Ala Leu Thr Gly Ser Thr Glu Glu Ser
420 425 430
Gln Phe
<210> 9
<211> 1602
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(1602)
<400> 9
atg act gaa cag gca aca aca acc gat gaa ctg gct ttc aca agg ccg 48
Met Thr Glu Gln Ala Thr Thr Thr Asp Glu Leu Ala Phe Thr Arg Pro
1 5 10 15
tat ggc gag cag gag aag caa att ctt act gcc gaa gcg gta gaa ttt 96
Tyr Gly Glu Gln Glu Lys Gln Ile Leu Thr Ala Glu Ala Val Glu Phe
20 25 30
ctg act gag ctg gtg acg cat ttt acg cca caa cgc aat aaa ctt ctg 144
Leu Thr Glu Leu Val Thr His Phe Thr Pro Gln Arg Asn Lys Leu Leu
35 40 45
gca gcg cgc att cag cag cag caa gat att gat aac gga acg ttg cct 192
Ala Ala Arg Ile Gln Gln Gln Gln Asp Ile Asp Asn Gly Thr Leu Pro
50 55 60
gat ttt att tcg gaa aca gct tcc att cgc gat gct gat tgg aaa att 240
Asp Phe Ile Ser Glu Thr Ala Ser Ile Arg Asp Ala Asp Trp Lys Ile
65 70 75 80
cgc ggg att cct gcg gac tta gaa gac cgc cgc gta gag ata act ggc 288
Arg Gly Ile Pro Ala Asp Leu Glu Asp Arg Arg Val Glu Ile Thr Gly
85 90 95
ccg gta gag cgc aag atg gtg atc aac gcg ctc aac gcc aat gtg aaa 336
Pro Val Glu Arg Lys Met Val Ile Asn Ala Leu Asn Ala Asn Val Lys
100 105 110
gtc ttt atg gcc gat ttc gaa gat tca ctg gca cca gac tgg aac aaa 384
Val Phe Met Ala Asp Phe Glu Asp Ser Leu Ala Pro Asp Trp Asn Lys
115 120 125
gtg atc gac ggg caa att aac ctg cgt gat gcg gtt aac ggc acc atc 432
Val Ile Asp Gly Gln Ile Asn Leu Arg Asp Ala Val Asn Gly Thr Ile
130 135 140
agt tac acc aat gaa gca ggc aaa att tac cag ctc aag ccc aat cca 480
Ser Tyr Thr Asn Glu Ala Gly Lys Ile Tyr Gln Leu Lys Pro Asn Pro
145 150 155 160
gcg gtt ttg att tgt cgg gta cgc ggt ctg cac ttg ccg gaa aaa cat 528
Ala Val Leu Ile Cys Arg Val Arg Gly Leu His Leu Pro Glu Lys His
165 170 175
gtc acc tgg cgt ggt gag gca atc ccc ggc agc ctg ttt gat ttt gcg 576
Val Thr Trp Arg Gly Glu Ala Ile Pro Gly Ser Leu Phe Asp Phe Ala
180 185 190
ctc tat ttc ttc cac aac tat cag gca ctg ttg gca aag ggc agt ggt 624
Leu Tyr Phe Phe His Asn Tyr Gln Ala Leu Leu Ala Lys Gly Ser Gly
195 200 205
ccc tat ttc tat ctg ccg aaa acc cag tcc tgg cag gaa gcg gcc tgg 672
Pro Tyr Phe Tyr Leu Pro Lys Thr Gln Ser Trp Gln Glu Ala Ala Trp
210 215 220
tgg agc gaa gtc ttc agc tat gca gaa gat cgc ttt aat ctg ccg cgc 720
Trp Ser Glu Val Phe Ser Tyr Ala Glu Asp Arg Phe Asn Leu Pro Arg
225 230 235 240
ggc acc atc aag gcg acg ttg ctg att gaa acg ctg ccc gcc gtg ttc 768
Gly Thr Ile Lys Ala Thr Leu Leu Ile Glu Thr Leu Pro Ala Val Phe
245 250 255
cag atg gat gaa atc ctt cac gcg ctg cgt gac cat att gtt ggt ctg 816
Gln Met Asp Glu Ile Leu His Ala Leu Arg Asp His Ile Val Gly Leu
260 265 270
aac tgc ggt cgt tgg gat tac atc ttc agc tat atc aaa acg ttg aaa 864
Asn Cys Gly Arg Trp Asp Tyr Ile Phe Ser Tyr Ile Lys Thr Leu Lys
275 280 285
aac tat ccc gat cgc gtc ctg cca gac aga cag gca gtg acg atg gat 912
Asn Tyr Pro Asp Arg Val Leu Pro Asp Arg Gln Ala Val Thr Met Asp
290 295 300
aaa cca ttc ctg aat gct tac tca cgc ctg ttg att aaa acc tgc cat 960
Lys Pro Phe Leu Asn Ala Tyr Ser Arg Leu Leu Ile Lys Thr Cys His
305 310 315 320
aaa cgc ggt gct ttt gcg atg ggc ggc atg gcg gcg ttt att ccg agc 1008
Lys Arg Gly Ala Phe Ala Met Gly Gly Met Ala Ala Phe Ile Pro Ser
325 330 335
aaa gat gaa gag cac aat aac cag gtg ctc aac aaa gta aaa gcg gat 1056
Lys Asp Glu Glu His Asn Asn Gln Val Leu Asn Lys Val Lys Ala Asp
340 345 350
aaa tcg ctg gaa gcc aat aac ggt cac gat ggc aca tgg atc gct cac 1104
Lys Ser Leu Glu Ala Asn Asn Gly His Asp Gly Thr Trp Ile Ala His
355 360 365
cca ggc ctt gcg gac acg gca atg gcg gta ttc aac gac att ctc ggc 1152
Pro Gly Leu Ala Asp Thr Ala Met Ala Val Phe Asn Asp Ile Leu Gly
370 375 380
tcc cgt aaa aat cag ctt gaa gtg atg cgc gaa caa gac gcg ccg att 1200
Ser Arg Lys Asn Gln Leu Glu Val Met Arg Glu Gln Asp Ala Pro Ile
385 390 395 400
act gcc gat cag ctg ctg gca cct tgt gat ggt gaa cgc acc gaa gaa 1248
Thr Ala Asp Gln Leu Leu Ala Pro Cys Asp Gly Glu Arg Thr Glu Glu
405 410 415
ggt atg cgc gcc aac att cgc gtg gct gtg cag tac atc gaa gcg tgg 1296
Gly Met Arg Ala Asn Ile Arg Val Ala Val Gln Tyr Ile Glu Ala Trp
420 425 430
atc tct ggc aac ggc tgt gtg ccg att tat ggc ctg atg gaa gat gcg 1344
Ile Ser Gly Asn Gly Cys Val Pro Ile Tyr Gly Leu Met Glu Asp Ala
435 440 445
gcg acg gct gaa att tcc cgt acc tcg atc tgg cag tgg atc cat cat 1392
Ala Thr Ala Glu Ile Ser Arg Thr Ser Ile Trp Gln Trp Ile His His
450 455 460
caa aaa acg ttg agc aat ggc aaa ccg gtg acc aaa gcc ttg ttc cgc 1440
Gln Lys Thr Leu Ser Asn Gly Lys Pro Val Thr Lys Ala Leu Phe Arg
465 470 475 480
cag atg ctg ggc gaa gag atg aaa gtc att gcc agc gaa ctg ggc gaa 1488
Gln Met Leu Gly Glu Glu Met Lys Val Ile Ala Ser Glu Leu Gly Glu
485 490 495
gaa cgt ttc tcc cag ggg cgt ttt gac gat gcc gca cgc ttg atg gaa 1536
Glu Arg Phe Ser Gln Gly Arg Phe Asp Asp Ala Ala Arg Leu Met Glu
500 505 510
cag atc acc act tcc gat gag tta att gat ttc ctg acc ctg cca ggc 1584
Gln Ile Thr Thr Ser Asp Glu Leu Ile Asp Phe Leu Thr Leu Pro Gly
515 520 525
tac cgc ctg tta gcg taa 1602
Tyr Arg Leu Leu Ala
530
<210> 10
<211> 533
<212> PRT
<213> Escherichia coli
<400> 10
Met Thr Glu Gln Ala Thr Thr Thr Asp Glu Leu Ala Phe Thr Arg Pro
1 5 10 15
Tyr Gly Glu Gln Glu Lys Gln Ile Leu Thr Ala Glu Ala Val Glu Phe
20 25 30
Leu Thr Glu Leu Val Thr His Phe Thr Pro Gln Arg Asn Lys Leu Leu
35 40 45
Ala Ala Arg Ile Gln Gln Gln Gln Asp Ile Asp Asn Gly Thr Leu Pro
50 55 60
Asp Phe Ile Ser Glu Thr Ala Ser Ile Arg Asp Ala Asp Trp Lys Ile
65 70 75 80
Arg Gly Ile Pro Ala Asp Leu Glu Asp Arg Arg Val Glu Ile Thr Gly
85 90 95
Pro Val Glu Arg Lys Met Val Ile Asn Ala Leu Asn Ala Asn Val Lys
100 105 110
Val Phe Met Ala Asp Phe Glu Asp Ser Leu Ala Pro Asp Trp Asn Lys
115 120 125
Val Ile Asp Gly Gln Ile Asn Leu Arg Asp Ala Val Asn Gly Thr Ile
130 135 140
Ser Tyr Thr Asn Glu Ala Gly Lys Ile Tyr Gln Leu Lys Pro Asn Pro
145 150 155 160
Ala Val Leu Ile Cys Arg Val Arg Gly Leu His Leu Pro Glu Lys His
165 170 175
Val Thr Trp Arg Gly Glu Ala Ile Pro Gly Ser Leu Phe Asp Phe Ala
180 185 190
Leu Tyr Phe Phe His Asn Tyr Gln Ala Leu Leu Ala Lys Gly Ser Gly
195 200 205
Pro Tyr Phe Tyr Leu Pro Lys Thr Gln Ser Trp Gln Glu Ala Ala Trp
210 215 220
Trp Ser Glu Val Phe Ser Tyr Ala Glu Asp Arg Phe Asn Leu Pro Arg
225 230 235 240
Gly Thr Ile Lys Ala Thr Leu Leu Ile Glu Thr Leu Pro Ala Val Phe
245 250 255
Gln Met Asp Glu Ile Leu His Ala Leu Arg Asp His Ile Val Gly Leu
260 265 270
Asn Cys Gly Arg Trp Asp Tyr Ile Phe Ser Tyr Ile Lys Thr Leu Lys
275 280 285
Asn Tyr Pro Asp Arg Val Leu Pro Asp Arg Gln Ala Val Thr Met Asp
290 295 300
Lys Pro Phe Leu Asn Ala Tyr Ser Arg Leu Leu Ile Lys Thr Cys His
305 310 315 320
Lys Arg Gly Ala Phe Ala Met Gly Gly Met Ala Ala Phe Ile Pro Ser
325 330 335
Lys Asp Glu Glu His Asn Asn Gln Val Leu Asn Lys Val Lys Ala Asp
340 345 350
Lys Ser Leu Glu Ala Asn Asn Gly His Asp Gly Thr Trp Ile Ala His
355 360 365
Pro Gly Leu Ala Asp Thr Ala Met Ala Val Phe Asn Asp Ile Leu Gly
370 375 380
Ser Arg Lys Asn Gln Leu Glu Val Met Arg Glu Gln Asp Ala Pro Ile
385 390 395 400
Thr Ala Asp Gln Leu Leu Ala Pro Cys Asp Gly Glu Arg Thr Glu Glu
405 410 415
Gly Met Arg Ala Asn Ile Arg Val Ala Val Gln Tyr Ile Glu Ala Trp
420 425 430
Ile Ser Gly Asn Gly Cys Val Pro Ile Tyr Gly Leu Met Glu Asp Ala
435 440 445
Ala Thr Ala Glu Ile Ser Arg Thr Ser Ile Trp Gln Trp Ile His His
450 455 460
Gln Lys Thr Leu Ser Asn Gly Lys Pro Val Thr Lys Ala Leu Phe Arg
465 470 475 480
Gln Met Leu Gly Glu Glu Met Lys Val Ile Ala Ser Glu Leu Gly Glu
485 490 495
Glu Arg Phe Ser Gln Gly Arg Phe Asp Asp Ala Ala Arg Leu Met Glu
500 505 510
Gln Ile Thr Thr Ser Asp Glu Leu Ile Asp Phe Leu Thr Leu Pro Gly
515 520 525
Tyr Arg Leu Leu Ala
530
<210> 11
<211> 1737
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(1737)
<400> 11
atg ccg cgt ggc ctg gaa tta ttg att gct caa acc att ttg caa ggc 48
Met Pro Arg Gly Leu Glu Leu Leu Ile Ala Gln Thr Ile Leu Gln Gly
1 5 10 15
ttc gat gct cag tat ggt cga ttc ctc gaa gtg acc tcc ggt gcg cag 96
Phe Asp Ala Gln Tyr Gly Arg Phe Leu Glu Val Thr Ser Gly Ala Gln
20 25 30
cag cgt ttc gaa cag gcc gac tgg cat gct gtc cag cag gcg atg aaa 144
Gln Arg Phe Glu Gln Ala Asp Trp His Ala Val Gln Gln Ala Met Lys
35 40 45
aac cgt atc cat ctt tac gat cat cac gtt ggt ctg gtc gtg gag caa 192
Asn Arg Ile His Leu Tyr Asp His His Val Gly Leu Val Val Glu Gln
50 55 60
ctg cgc tgc att act aac ggc caa agt acg gac gcg gca ttt tta cta 240
Leu Arg Cys Ile Thr Asn Gly Gln Ser Thr Asp Ala Ala Phe Leu Leu
65 70 75 80
cgt gtt aaa gag cat tac acc cgg ctg ttg ccg gat tac ccg cgc ttc 288
Arg Val Lys Glu His Tyr Thr Arg Leu Leu Pro Asp Tyr Pro Arg Phe
85 90 95
gag att gcg gag agc ttt ttt aac tcc gtg tac tgt cgg tta ttt gac 336
Glu Ile Ala Glu Ser Phe Phe Asn Ser Val Tyr Cys Arg Leu Phe Asp
100 105 110
cac cgc tcg ctt act ccc gag cgg ctt ttt atc ttt agc tct cag cca 384
His Arg Ser Leu Thr Pro Glu Arg Leu Phe Ile Phe Ser Ser Gln Pro
115 120 125
gag cgc cgc ttt cgt acc att ccc cgc ccg ctg gcg aaa gac ttt cac 432
Glu Arg Arg Phe Arg Thr Ile Pro Arg Pro Leu Ala Lys Asp Phe His
130 135 140
ccc gat cac ggc tgg gaa tct cta ctg atg cgc gtt atc agc gac cta 480
Pro Asp His Gly Trp Glu Ser Leu Leu Met Arg Val Ile Ser Asp Leu
145 150 155 160
ccg ctg cgc ctg cgc tgg cag aat aaa agc cgt gac atc cat tac att 528
Pro Leu Arg Leu Arg Trp Gln Asn Lys Ser Arg Asp Ile His Tyr Ile
165 170 175
att cgc cat ctg acg gaa acg ctg ggg aca gac aac ctc gcg gaa agt 576
Ile Arg His Leu Thr Glu Thr Leu Gly Thr Asp Asn Leu Ala Glu Ser
180 185 190
cat tta cag gtg gcg aac gaa ctg ttt tac cgc aat aaa gcc gcc tgg 624
His Leu Gln Val Ala Asn Glu Leu Phe Tyr Arg Asn Lys Ala Ala Trp
195 200 205
ctg gta ggc aaa ctg atc aca cct tcc ggc aca ttg cca ttt ttg ctg 672
Leu Val Gly Lys Leu Ile Thr Pro Ser Gly Thr Leu Pro Phe Leu Leu
210 215 220
ccg atc cac cag acg gac gac ggc gag tta ttt att gat acc tgc ctg 720
Pro Ile His Gln Thr Asp Asp Gly Glu Leu Phe Ile Asp Thr Cys Leu
225 230 235 240
acg acg acc gcc gaa gcg agc att gtt ttt ggc ttt gcg cgt tct tat 768
Thr Thr Thr Ala Glu Ala Ser Ile Val Phe Gly Phe Ala Arg Ser Tyr
245 250 255
ttt atg gtt tat gcg ccg ctg ccc gca gcg ctg gtc gag tgg cta cgg 816
Phe Met Val Tyr Ala Pro Leu Pro Ala Ala Leu Val Glu Trp Leu Arg
260 265 270
gaa att ctg cca ggt aaa acc acc gct gaa ttg tat atg gct atc ggc 864
Glu Ile Leu Pro Gly Lys Thr Thr Ala Glu Leu Tyr Met Ala Ile Gly
275 280 285
tgc cag aag cac gcc aaa acc gaa agc tac cgc gaa tat ctc gtt tat 912
Cys Gln Lys His Ala Lys Thr Glu Ser Tyr Arg Glu Tyr Leu Val Tyr
290 295 300
cta cag ggc tgt aat gag cag ttc att gaa gcg ccg ggt att cgt gga 960
Leu Gln Gly Cys Asn Glu Gln Phe Ile Glu Ala Pro Gly Ile Arg Gly
305 310 315 320
atg gtg atg ttg gtg ttt acg ctg ccg ggc ttt gat cgg gta ttc aaa 1008
Met Val Met Leu Val Phe Thr Leu Pro Gly Phe Asp Arg Val Phe Lys
325 330 335
gtc atc aaa gac agg ttc gcg ccg cag aaa gag atg tct gcc gct cac 1056
Val Ile Lys Asp Arg Phe Ala Pro Gln Lys Glu Met Ser Ala Ala His
340 345 350
gtt cgt gcc tgc tat caa ctg gtg aaa gag cac gat cgc gtg ggc cga 1104
Val Arg Ala Cys Tyr Gln Leu Val Lys Glu His Asp Arg Val Gly Arg
355 360 365
atg gcg gac acc cag gag ttt gaa aac ttt gtg ctg gag aag cgg cat 1152
Met Ala Asp Thr Gln Glu Phe Glu Asn Phe Val Leu Glu Lys Arg His
370 375 380
att tcc ccg gca tta atg gaa tta ctg ctt cag gaa gca gcg gaa aaa 1200
Ile Ser Pro Ala Leu Met Glu Leu Leu Leu Gln Glu Ala Ala Glu Lys
385 390 395 400
atc acc gat ctc ggc gaa caa att gtg att cgc cat ctt tat att gag 1248
Ile Thr Asp Leu Gly Glu Gln Ile Val Ile Arg His Leu Tyr Ile Glu
405 410 415
cgg cgg atg gtg ccg ctc aat atc tgg ctg gaa caa gtg gaa ggt cag 1296
Arg Arg Met Val Pro Leu Asn Ile Trp Leu Glu Gln Val Glu Gly Gln
420 425 430
cag ttg cgc gac gcc att gaa gaa tac ggt aac gct att cgc cag ctt 1344
Gln Leu Arg Asp Ala Ile Glu Glu Tyr Gly Asn Ala Ile Arg Gln Leu
435 440 445
gcc gct gct aac att ttc cct ggc gac atg ctg ttt aaa aac ttc ggt 1392
Ala Ala Ala Asn Ile Phe Pro Gly Asp Met Leu Phe Lys Asn Phe Gly
450 455 460
gtc acc cgt cac ggg cgt gtg gtt ttt tat gat tac gat gaa att tgc 1440
Val Thr Arg His Gly Arg Val Val Phe Tyr Asp Tyr Asp Glu Ile Cys
465 470 475 480
tac atg acg gaa gtg aat ttc cgc gac atc ccg ccg ccg cgc tat ccg 1488
Tyr Met Thr Glu Val Asn Phe Arg Asp Ile Pro Pro Pro Arg Tyr Pro
485 490 495
gaa gac gaa ctt gcc agc gaa ccg tgg tac agc gtc tcg ccg ggc gat 1536
Glu Asp Glu Leu Ala Ser Glu Pro Trp Tyr Ser Val Ser Pro Gly Asp
500 505 510
gtt ttc ccg gaa gag ttt cgc cac tgg cta tgc gcc gac ccg cgt att 1584
Val Phe Pro Glu Glu Phe Arg His Trp Leu Cys Ala Asp Pro Arg Ile
515 520 525
ggt ccg ctg ttt gaa gag atg cac gcc gac ctg ttc cgc gct gat tac 1632
Gly Pro Leu Phe Glu Glu Met His Ala Asp Leu Phe Arg Ala Asp Tyr
530 535 540
tgg cgc gca cta caa aac cgc ata cgt gaa ggg cat gtg gaa gat gtt 1680
Trp Arg Ala Leu Gln Asn Arg Ile Arg Glu Gly His Val Glu Asp Val
545 550 555 560
tat gcg tat cgg cgc agg caa aga ttt agc gta cgg tat ggg gag atg 1728
Tyr Ala Tyr Arg Arg Arg Gln Arg Phe Ser Val Arg Tyr Gly Glu Met
565 570 575
ctt ttt tga 1737
Leu Phe
<210> 12
<211> 578
<212> PRT
<213> Escherichia coli
<400> 12
Met Pro Arg Gly Leu Glu Leu Leu Ile Ala Gln Thr Ile Leu Gln Gly
1 5 10 15
Phe Asp Ala Gln Tyr Gly Arg Phe Leu Glu Val Thr Ser Gly Ala Gln
20 25 30
Gln Arg Phe Glu Gln Ala Asp Trp His Ala Val Gln Gln Ala Met Lys
35 40 45
Asn Arg Ile His Leu Tyr Asp His His Val Gly Leu Val Val Glu Gln
50 55 60
Leu Arg Cys Ile Thr Asn Gly Gln Ser Thr Asp Ala Ala Phe Leu Leu
65 70 75 80
Arg Val Lys Glu His Tyr Thr Arg Leu Leu Pro Asp Tyr Pro Arg Phe
85 90 95
Glu Ile Ala Glu Ser Phe Phe Asn Ser Val Tyr Cys Arg Leu Phe Asp
100 105 110
His Arg Ser Leu Thr Pro Glu Arg Leu Phe Ile Phe Ser Ser Gln Pro
115 120 125
Glu Arg Arg Phe Arg Thr Ile Pro Arg Pro Leu Ala Lys Asp Phe His
130 135 140
Pro Asp His Gly Trp Glu Ser Leu Leu Met Arg Val Ile Ser Asp Leu
145 150 155 160
Pro Leu Arg Leu Arg Trp Gln Asn Lys Ser Arg Asp Ile His Tyr Ile
165 170 175
Ile Arg His Leu Thr Glu Thr Leu Gly Thr Asp Asn Leu Ala Glu Ser
180 185 190
His Leu Gln Val Ala Asn Glu Leu Phe Tyr Arg Asn Lys Ala Ala Trp
195 200 205
Leu Val Gly Lys Leu Ile Thr Pro Ser Gly Thr Leu Pro Phe Leu Leu
210 215 220
Pro Ile His Gln Thr Asp Asp Gly Glu Leu Phe Ile Asp Thr Cys Leu
225 230 235 240
Thr Thr Thr Ala Glu Ala Ser Ile Val Phe Gly Phe Ala Arg Ser Tyr
245 250 255
Phe Met Val Tyr Ala Pro Leu Pro Ala Ala Leu Val Glu Trp Leu Arg
260 265 270
Glu Ile Leu Pro Gly Lys Thr Thr Ala Glu Leu Tyr Met Ala Ile Gly
275 280 285
Cys Gln Lys His Ala Lys Thr Glu Ser Tyr Arg Glu Tyr Leu Val Tyr
290 295 300
Leu Gln Gly Cys Asn Glu Gln Phe Ile Glu Ala Pro Gly Ile Arg Gly
305 310 315 320
Met Val Met Leu Val Phe Thr Leu Pro Gly Phe Asp Arg Val Phe Lys
325 330 335
Val Ile Lys Asp Arg Phe Ala Pro Gln Lys Glu Met Ser Ala Ala His
340 345 350
Val Arg Ala Cys Tyr Gln Leu Val Lys Glu His Asp Arg Val Gly Arg
355 360 365
Met Ala Asp Thr Gln Glu Phe Glu Asn Phe Val Leu Glu Lys Arg His
370 375 380
Ile Ser Pro Ala Leu Met Glu Leu Leu Leu Gln Glu Ala Ala Glu Lys
385 390 395 400
Ile Thr Asp Leu Gly Glu Gln Ile Val Ile Arg His Leu Tyr Ile Glu
405 410 415
Arg Arg Met Val Pro Leu Asn Ile Trp Leu Glu Gln Val Glu Gly Gln
420 425 430
Gln Leu Arg Asp Ala Ile Glu Glu Tyr Gly Asn Ala Ile Arg Gln Leu
435 440 445
Ala Ala Ala Asn Ile Phe Pro Gly Asp Met Leu Phe Lys Asn Phe Gly
450 455 460
Val Thr Arg His Gly Arg Val Val Phe Tyr Asp Tyr Asp Glu Ile Cys
465 470 475 480
Tyr Met Thr Glu Val Asn Phe Arg Asp Ile Pro Pro Pro Arg Tyr Pro
485 490 495
Glu Asp Glu Leu Ala Ser Glu Pro Trp Tyr Ser Val Ser Pro Gly Asp
500 505 510
Val Phe Pro Glu Glu Phe Arg His Trp Leu Cys Ala Asp Pro Arg Ile
515 520 525
Gly Pro Leu Phe Glu Glu Met His Ala Asp Leu Phe Arg Ala Asp Tyr
530 535 540
Trp Arg Ala Leu Gln Asn Arg Ile Arg Glu Gly His Val Glu Asp Val
545 550 555 560
Tyr Ala Tyr Arg Arg Arg Gln Arg Phe Ser Val Arg Tyr Gly Glu Met
565 570 575
Leu Phe
<210> 13
<211> 807
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(807)
<400> 13
atg gaa cgc tac gaa tct ctg ttt gcc cag ttg aag gag cgc aaa gaa 48
Met Glu Arg Tyr Glu Ser Leu Phe Ala Gln Leu Lys Glu Arg Lys Glu
1 5 10 15
ggc gca ttc gtt cct ttc gtc acg ctc ggt gat ccg ggc att gag cag 96
Gly Ala Phe Val Pro Phe Val Thr Leu Gly Asp Pro Gly Ile Glu Gln
20 25 30
tca ttg aaa att atc gat acg cta att gaa gcc ggt gct gac gcg ctg 144
Ser Leu Lys Ile Ile Asp Thr Leu Ile Glu Ala Gly Ala Asp Ala Leu
35 40 45
gag tta ggt atc ccc ttc tcc gac cca ctg gcg gat ggc ccg acg att 192
Glu Leu Gly Ile Pro Phe Ser Asp Pro Leu Ala Asp Gly Pro Thr Ile
50 55 60
caa aac gcc act ctg cgc gcc ttt gcg gca ggt gtg act ccg gca caa 240
Gln Asn Ala Thr Leu Arg Ala Phe Ala Ala Gly Val Thr Pro Ala Gln
65 70 75 80
tgt ttt gaa atg ctg gca ctg att cgc cag aaa cac ccg acc att ccc 288
Cys Phe Glu Met Leu Ala Leu Ile Arg Gln Lys His Pro Thr Ile Pro
85 90 95
att ggc ctg ttg atg tat gcc aat ctg gtg ttt aac aaa ggc att gat 336
Ile Gly Leu Leu Met Tyr Ala Asn Leu Val Phe Asn Lys Gly Ile Asp
100 105 110
gag ttt tat gcc cag tgc gaa aaa gtc ggc gtc gat tcg gtg ctg gtt 384
Glu Phe Tyr Ala Gln Cys Glu Lys Val Gly Val Asp Ser Val Leu Val
115 120 125
gcc gat gtg cca gtt gaa gag tcc gcg ccc ttc cgc cag gcc gcg ttg 432
Ala Asp Val Pro Val Glu Glu Ser Ala Pro Phe Arg Gln Ala Ala Leu
130 135 140
cgt cat aat gtc gca cct atc ttc atc tgc ccg cca aat gcc gat gac 480
Arg His Asn Val Ala Pro Ile Phe Ile Cys Pro Pro Asn Ala Asp Asp
145 150 155 160
gac ctg ctg cgc cag ata gcc tct tac ggt cgt ggt tac acc tat ttg 528
Asp Leu Leu Arg Gln Ile Ala Ser Tyr Gly Arg Gly Tyr Thr Tyr Leu
165 170 175
ctg tca cga gca ggc gtg acc ggc gca gaa aac cgc gcc gcg tta ccc 576
Leu Ser Arg Ala Gly Val Thr Gly Ala Glu Asn Arg Ala Ala Leu Pro
180 185 190
ctc aat cat ctg gtt gcg aag ctg aaa gag tac aac gct gca cct cca 624
Leu Asn His Leu Val Ala Lys Leu Lys Glu Tyr Asn Ala Ala Pro Pro
195 200 205
ttg cag gga ttt ggt att tcc gcc ccg gat cag gta aaa gca gcg att 672
Leu Gln Gly Phe Gly Ile Ser Ala Pro Asp Gln Val Lys Ala Ala Ile
210 215 220
gat gca gga gct gcg ggc gcg att tct ggt tcg gcc att gtt aaa atc 720
Asp Ala Gly Ala Ala Gly Ala Ile Ser Gly Ser Ala Ile Val Lys Ile
225 230 235 240
atc gag caa cat att aat gag cca gag aaa atg ctg gcg gca ctg aaa 768
Ile Glu Gln His Ile Asn Glu Pro Glu Lys Met Leu Ala Ala Leu Lys
245 250 255
gtt ttt gta caa ccg atg aaa gcg gcg acg cgc agt taa 807
Val Phe Val Gln Pro Met Lys Ala Ala Thr Arg Ser
260 265
<210> 14
<211> 268
<212> PRT
<213> Escherichia coli
<400> 14
Met Glu Arg Tyr Glu Ser Leu Phe Ala Gln Leu Lys Glu Arg Lys Glu
1 5 10 15
Gly Ala Phe Val Pro Phe Val Thr Leu Gly Asp Pro Gly Ile Glu Gln
20 25 30
Ser Leu Lys Ile Ile Asp Thr Leu Ile Glu Ala Gly Ala Asp Ala Leu
35 40 45
Glu Leu Gly Ile Pro Phe Ser Asp Pro Leu Ala Asp Gly Pro Thr Ile
50 55 60
Gln Asn Ala Thr Leu Arg Ala Phe Ala Ala Gly Val Thr Pro Ala Gln
65 70 75 80
Cys Phe Glu Met Leu Ala Leu Ile Arg Gln Lys His Pro Thr Ile Pro
85 90 95
Ile Gly Leu Leu Met Tyr Ala Asn Leu Val Phe Asn Lys Gly Ile Asp
100 105 110
Glu Phe Tyr Ala Gln Cys Glu Lys Val Gly Val Asp Ser Val Leu Val
115 120 125
Ala Asp Val Pro Val Glu Glu Ser Ala Pro Phe Arg Gln Ala Ala Leu
130 135 140
Arg His Asn Val Ala Pro Ile Phe Ile Cys Pro Pro Asn Ala Asp Asp
145 150 155 160
Asp Leu Leu Arg Gln Ile Ala Ser Tyr Gly Arg Gly Tyr Thr Tyr Leu
165 170 175
Leu Ser Arg Ala Gly Val Thr Gly Ala Glu Asn Arg Ala Ala Leu Pro
180 185 190
Leu Asn His Leu Val Ala Lys Leu Lys Glu Tyr Asn Ala Ala Pro Pro
195 200 205
Leu Gln Gly Phe Gly Ile Ser Ala Pro Asp Gln Val Lys Ala Ala Ile
210 215 220
Asp Ala Gly Ala Ala Gly Ala Ile Ser Gly Ser Ala Ile Val Lys Ile
225 230 235 240
Ile Glu Gln His Ile Asn Glu Pro Glu Lys Met Leu Ala Ala Leu Lys
245 250 255
Val Phe Val Gln Pro Met Lys Ala Ala Thr Arg Ser
260 265
<210> 15
<211> 1194
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(1194)
<400> 15
atg aca aca tta ctt aac ccc tat ttt ggt gag ttt ggc ggc atg tac 48
Met Thr Thr Leu Leu Asn Pro Tyr Phe Gly Glu Phe Gly Gly Met Tyr
1 5 10 15
gtg cca caa atc ctg atg cct gct ctg cgc cag ctg gaa gaa gct ttt 96
Val Pro Gln Ile Leu Met Pro Ala Leu Arg Gln Leu Glu Glu Ala Phe
20 25 30
gtc agt gcg caa aaa gat cct gaa ttt cag gct cag ttc aac gac ctg 144
Val Ser Ala Gln Lys Asp Pro Glu Phe Gln Ala Gln Phe Asn Asp Leu
35 40 45
ctg aaa aac tat gcc ggg cgt cca acc gcg ctg acc aaa tgc cag aac 192
Leu Lys Asn Tyr Ala Gly Arg Pro Thr Ala Leu Thr Lys Cys Gln Asn
50 55 60
att aca gcc ggg acg aac acc acg ctg tat ctc aag cgt gaa gat ttg 240
Ile Thr Ala Gly Thr Asn Thr Thr Leu Tyr Leu Lys Arg Glu Asp Leu
65 70 75 80
ctg cac ggc ggc gcg cat aaa act aac cag gtg ctg ggg cag gcg ttg 288
Leu His Gly Gly Ala His Lys Thr Asn Gln Val Leu Gly Gln Ala Leu
85 90 95
ctg gcg aag cgg atg ggt aaa acc gaa atc atc gcc gaa acc ggt gcc 336
Leu Ala Lys Arg Met Gly Lys Thr Glu Ile Ile Ala Glu Thr Gly Ala
100 105 110
ggt cag cat ggc gtg gcg tcg gcc ctt gcc agc gcc ctg ctc ggc ctg 384
Gly Gln His Gly Val Ala Ser Ala Leu Ala Ser Ala Leu Leu Gly Leu
115 120 125
aaa tgc cgt att tat atg ggt gcc aaa gac gtt gaa cgc cag tcg cct 432
Lys Cys Arg Ile Tyr Met Gly Ala Lys Asp Val Glu Arg Gln Ser Pro
130 135 140
aac gtt ttt cgt atg cgc tta atg ggt gcg gaa gtg atc ccg gtg cat 480
Asn Val Phe Arg Met Arg Leu Met Gly Ala Glu Val Ile Pro Val His
145 150 155 160
agc ggt tcc gcg acg ctg aaa gat gcc tgt aac gag gcg ctg cgc gac 528
Ser Gly Ser Ala Thr Leu Lys Asp Ala Cys Asn Glu Ala Leu Arg Asp
165 170 175
tgg tcc ggt agt tac gaa acc gcg cac tat atg ctg ggc acc gca gct 576
Trp Ser Gly Ser Tyr Glu Thr Ala His Tyr Met Leu Gly Thr Ala Ala
180 185 190
ggc ccg cat cct tat ccg acc att gtg cgt gag ttt cag cgg atg att 624
Gly Pro His Pro Tyr Pro Thr Ile Val Arg Glu Phe Gln Arg Met Ile
195 200 205
ggc gaa gaa acc aaa gcg cag att ctg gaa aga gaa ggt cgc ctg ccg 672
Gly Glu Glu Thr Lys Ala Gln Ile Leu Glu Arg Glu Gly Arg Leu Pro
210 215 220
gat gcc gtt atc gcc tgt gtt ggc ggc ggt tcg aat gcc atc ggc atg 720
Asp Ala Val Ile Ala Cys Val Gly Gly Gly Ser Asn Ala Ile Gly Met
225 230 235 240
ttt gct gat ttc atc aat gaa acc aac gtc ggc ctg att ggt gtg gag 768
Phe Ala Asp Phe Ile Asn Glu Thr Asn Val Gly Leu Ile Gly Val Glu
245 250 255
cca ggt ggt cac ggt atc gaa act ggc gag cac ggc gca ccg cta aaa 816
Pro Gly Gly His Gly Ile Glu Thr Gly Glu His Gly Ala Pro Leu Lys
260 265 270
cat ggt cgc gtg ggt atc tat ttc ggt atg aaa gcg ccg atg atg caa 864
His Gly Arg Val Gly Ile Tyr Phe Gly Met Lys Ala Pro Met Met Gln
275 280 285
acc gaa gac ggg cag att gaa gaa tct tac tcc atc tcc gcc gga ctg 912
Thr Glu Asp Gly Gln Ile Glu Glu Ser Tyr Ser Ile Ser Ala Gly Leu
290 295 300
gat ttc ccg tct gtc ggc cca caa cac gcg tat ctt aac agc act gga 960
Asp Phe Pro Ser Val Gly Pro Gln His Ala Tyr Leu Asn Ser Thr Gly
305 310 315 320
cgc gct gat tac gtg tct att acc gat gat gaa gcc ctt gaa gcc ttc 1008
Arg Ala Asp Tyr Val Ser Ile Thr Asp Asp Glu Ala Leu Glu Ala Phe
325 330 335
aaa acg ctg tgc ctg cac gaa ggg atc atc ccg gcg ctg gaa tcc tcc 1056
Lys Thr Leu Cys Leu His Glu Gly Ile Ile Pro Ala Leu Glu Ser Ser
340 345 350
cac gcc ctg gcc cat gcg ttg aaa atg atg cgc gaa aac ccg gat aaa 1104
His Ala Leu Ala His Ala Leu Lys Met Met Arg Glu Asn Pro Asp Lys
355 360 365
gag cag cta ctg gtg gtt aac ctt tcc ggt cgc ggc gat aaa gac atc 1152
Glu Gln Leu Leu Val Val Asn Leu Ser Gly Arg Gly Asp Lys Asp Ile
370 375 380
ttc acc gtt cac gat att ttg aaa gca cga ggg gaa atc tga 1194
Phe Thr Val His Asp Ile Leu Lys Ala Arg Gly Glu Ile
385 390 395
<210> 16
<211> 397
<212> PRT
<213> Escherichia coli
<400> 16
Met Thr Thr Leu Leu Asn Pro Tyr Phe Gly Glu Phe Gly Gly Met Tyr
1 5 10 15
Val Pro Gln Ile Leu Met Pro Ala Leu Arg Gln Leu Glu Glu Ala Phe
20 25 30
Val Ser Ala Gln Lys Asp Pro Glu Phe Gln Ala Gln Phe Asn Asp Leu
35 40 45
Leu Lys Asn Tyr Ala Gly Arg Pro Thr Ala Leu Thr Lys Cys Gln Asn
50 55 60
Ile Thr Ala Gly Thr Asn Thr Thr Leu Tyr Leu Lys Arg Glu Asp Leu
65 70 75 80
Leu His Gly Gly Ala His Lys Thr Asn Gln Val Leu Gly Gln Ala Leu
85 90 95
Leu Ala Lys Arg Met Gly Lys Thr Glu Ile Ile Ala Glu Thr Gly Ala
100 105 110
Gly Gln His Gly Val Ala Ser Ala Leu Ala Ser Ala Leu Leu Gly Leu
115 120 125
Lys Cys Arg Ile Tyr Met Gly Ala Lys Asp Val Glu Arg Gln Ser Pro
130 135 140
Asn Val Phe Arg Met Arg Leu Met Gly Ala Glu Val Ile Pro Val His
145 150 155 160
Ser Gly Ser Ala Thr Leu Lys Asp Ala Cys Asn Glu Ala Leu Arg Asp
165 170 175
Trp Ser Gly Ser Tyr Glu Thr Ala His Tyr Met Leu Gly Thr Ala Ala
180 185 190
Gly Pro His Pro Tyr Pro Thr Ile Val Arg Glu Phe Gln Arg Met Ile
195 200 205
Gly Glu Glu Thr Lys Ala Gln Ile Leu Glu Arg Glu Gly Arg Leu Pro
210 215 220
Asp Ala Val Ile Ala Cys Val Gly Gly Gly Ser Asn Ala Ile Gly Met
225 230 235 240
Phe Ala Asp Phe Ile Asn Glu Thr Asn Val Gly Leu Ile Gly Val Glu
245 250 255
Pro Gly Gly His Gly Ile Glu Thr Gly Glu His Gly Ala Pro Leu Lys
260 265 270
His Gly Arg Val Gly Ile Tyr Phe Gly Met Lys Ala Pro Met Met Gln
275 280 285
Thr Glu Asp Gly Gln Ile Glu Glu Ser Tyr Ser Ile Ser Ala Gly Leu
290 295 300
Asp Phe Pro Ser Val Gly Pro Gln His Ala Tyr Leu Asn Ser Thr Gly
305 310 315 320
Arg Ala Asp Tyr Val Ser Ile Thr Asp Asp Glu Ala Leu Glu Ala Phe
325 330 335
Lys Thr Leu Cys Leu His Glu Gly Ile Ile Pro Ala Leu Glu Ser Ser
340 345 350
His Ala Leu Ala His Ala Leu Lys Met Met Arg Glu Asn Pro Asp Lys
355 360 365
Glu Gln Leu Leu Val Val Asn Leu Ser Gly Arg Gly Asp Lys Asp Ile
370 375 380
Phe Thr Val His Asp Ile Leu Lys Ala Arg Gly Glu Ile
385 390 395
<210> 17
<211> 44
<212> DNA
<213> Artificial
<220>
<223> 5' -primer-evgAS
<400> 17
gggaattcac gcctgtagga ttagtaagaa gacttatagt gcca 44
<210> 18
<211> 44
<212> DNA
<213> Artificial
<220>
<223> 3' -primer-evgAS
<400> 18
ggaagcttcc acatttgaac attgtgggag ccgctattta gtca 44
<210> 19
<211> 44
<212> DNA
<213> Artificial
<220>
<223> 5' -primer-gadE
<400> 19
ggggatccaa agtgaacaaa gagttccgta agcgttgatg ctat 44
<210> 20
<211> 44
<212> DNA
<213> Artificial
<220>
<223> 3' -primer-gadE
<400> 20
ggaagcttat gccagccatc aatttcagtt gcttatgtcc tgac 44
<210> 21
<211> 47
<212> DNA
<213> Artificial
<220>
<223> 5' -primer-ydeO
<400> 21
ggaagcttaa cgcggggcag ggaatggctg ccccatttaa ttcttac 47
<210> 22
<211> 46
<212> DNA
<213> Artificial
<220>
<223> 3' -primer-ydeO
<400> 22
gggaattcgc tgagtatttc agaaatgggt cgcattgcaa gagatc 46
<210> 23
<211> 615
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(615)
<400> 23
atg aac gca ata att att gat gac cat cct ctt gct atc gca gca att 48
Met Asn Ala Ile Ile Ile Asp Asp His Pro Leu Ala Ile Ala Ala Ile
1 5 10 15
cgt aat tta ttg atc aaa aac gat att gaa atc tta gca gag ttg act 96
Arg Asn Leu Leu Ile Lys Asn Asp Ile Glu Ile Leu Ala Glu Leu Thr
20 25 30
gaa ggc gga agt gcc gtt cag cgg gtg gaa aca ctt aag cct gat atc 144
Glu Gly Gly Ser Ala Val Gln Arg Val Glu Thr Leu Lys Pro Asp Ile
35 40 45
gtc atc att gat gtc gat atc ccc gga gtt aac ggt atc cag gtg tta 192
Val Ile Ile Asp Val Asp Ile Pro Gly Val Asn Gly Ile Gln Val Leu
50 55 60
gaa acg ctg agg aag cgc caa tat agc gga att att att atc gtc tcc 240
Glu Thr Leu Arg Lys Arg Gln Tyr Ser Gly Ile Ile Ile Ile Val Ser
65 70 75 80
gct aaa aat gac cat ttt tac ggg aaa cat tgt gct gat gct ggc gct 288
Ala Lys Asn Asp His Phe Tyr Gly Lys His Cys Ala Asp Ala Gly Ala
85 90 95
aat ggt ttc gtg agt aaa aaa gaa ggc atg aac aat atc att gcg gct 336
Asn Gly Phe Val Ser Lys Lys Glu Gly Met Asn Asn Ile Ile Ala Ala
100 105 110
att gaa gct gca aaa aat ggc tac tgc tat ttc ccc ttc tct ctc aac 384
Ile Glu Ala Ala Lys Asn Gly Tyr Cys Tyr Phe Pro Phe Ser Leu Asn
115 120 125
cgg ttt gtt gga agt tta acg tcc gac cag caa aaa ctc gac tcc tta 432
Arg Phe Val Gly Ser Leu Thr Ser Asp Gln Gln Lys Leu Asp Ser Leu
130 135 140
tcg aaa caa gaa att agt gtc atg cgg tat att ctt gat ggc aag gat 480
Ser Lys Gln Glu Ile Ser Val Met Arg Tyr Ile Leu Asp Gly Lys Asp
145 150 155 160
aat aat gac att gct gaa aaa atg ttc atc agc aac aaa act gtc agc 528
Asn Asn Asp Ile Ala Glu Lys Met Phe Ile Ser Asn Lys Thr Val Ser
165 170 175
act tat aaa agt cgc ctg atg gaa aaa tta gaa tgt aaa tca ctg atg 576
Thr Tyr Lys Ser Arg Leu Met Glu Lys Leu Glu Cys Lys Ser Leu Met
180 185 190
gat ctt tac aca ttc gca caa cgt aac aaa atc ggc taa 615
Asp Leu Tyr Thr Phe Ala Gln Arg Asn Lys Ile Gly
195 200
<210> 24
<211> 204
<212> PRT
<213> Escherichia coli
<400> 24
Met Asn Ala Ile Ile Ile Asp Asp His Pro Leu Ala Ile Ala Ala Ile
1 5 10 15
Arg Asn Leu Leu Ile Lys Asn Asp Ile Glu Ile Leu Ala Glu Leu Thr
20 25 30
Glu Gly Gly Ser Ala Val Gln Arg Val Glu Thr Leu Lys Pro Asp Ile
35 40 45
Val Ile Ile Asp Val Asp Ile Pro Gly Val Asn Gly Ile Gln Val Leu
50 55 60
Glu Thr Leu Arg Lys Arg Gln Tyr Ser Gly Ile Ile Ile Ile Val Ser
65 70 75 80
Ala Lys Asn Asp His Phe Tyr Gly Lys His Cys Ala Asp Ala Gly Ala
85 90 95
Asn Gly Phe Val Ser Lys Lys Glu Gly Met Asn Asn Ile Ile Ala Ala
100 105 110
Ile Glu Ala Ala Lys Asn Gly Tyr Cys Tyr Phe Pro Phe Ser Leu Asn
115 120 125
Arg Phe Val Gly Ser Leu Thr Ser Asp Gln Gln Lys Leu Asp Ser Leu
130 135 140
Ser Lys Gln Glu Ile Ser Val Met Arg Tyr Ile Leu Asp Gly Lys Asp
145 150 155 160
Asn Asn Asp Ile Ala Glu Lys Met Phe Ile Ser Asn Lys Thr Val Ser
165 170 175
Thr Tyr Lys Ser Arg Leu Met Glu Lys Leu Glu Cys Lys Ser Leu Met
180 185 190
Asp Leu Tyr Thr Phe Ala Gln Arg Asn Lys Ile Gly
195 200
<210> 25
<211> 3594
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(3594)
<400> 25
atg aag ttt tta ccc tat att ttt ctt ctc tgt tgt ggt ctt tgg tcg 48
Met Lys Phe Leu Pro Tyr Ile Phe Leu Leu Cys Cys Gly Leu Trp Ser
1 5 10 15
acc ata agt ttc gca gac gaa gat tac atc gaa tat cgt ggc atc agt 96
Thr Ile Ser Phe Ala Asp Glu Asp Tyr Ile Glu Tyr Arg Gly Ile Ser
20 25 30
agt aac aac cgt gtc aca ctt gat cca cta cgt ctg agc aac aag gaa 144
Ser Asn Asn Arg Val Thr Leu Asp Pro Leu Arg Leu Ser Asn Lys Glu
35 40 45
tta cgt tgg tta gcg agc aaa aaa aat ctt gtg att gca gta cat aag 192
Leu Arg Trp Leu Ala Ser Lys Lys Asn Leu Val Ile Ala Val His Lys
50 55 60
tcc caa acg gct acg ttg ttg cat acc gat tcg cag caa cgg gtt cgt 240
Ser Gln Thr Ala Thr Leu Leu His Thr Asp Ser Gln Gln Arg Val Arg
65 70 75 80
ggt att aat gct gat tat tta aat ctt tta aaa aga gcg tta aat atc 288
Gly Ile Asn Ala Asp Tyr Leu Asn Leu Leu Lys Arg Ala Leu Asn Ile
85 90 95
aaa tta aca ctc cgg gaa tac gca gat cat caa aaa gca atg gac gcg 336
Lys Leu Thr Leu Arg Glu Tyr Ala Asp His Gln Lys Ala Met Asp Ala
100 105 110
ctt gca gaa ggt gaa gtc gat ata gtg tta tca cat tta gtt act tcg 384
Leu Ala Glu Gly Glu Val Asp Ile Val Leu Ser His Leu Val Thr Ser
115 120 125
ccg cct ctt aat aat gac att gct gca acc aaa cca ttg ata att acc 432
Pro Pro Leu Asn Asn Asp Ile Ala Ala Thr Lys Pro Leu Ile Ile Thr
130 135 140
ttt ccg gcg ctg gta acc acc ctt cac gac tca atg cga ccg ctt acc 480
Phe Pro Ala Leu Val Thr Thr Leu His Asp Ser Met Arg Pro Leu Thr
145 150 155 160
tca cca aaa cca gta aat att gct cgg gta gca aat tac ccc cca gac 528
Ser Pro Lys Pro Val Asn Ile Ala Arg Val Ala Asn Tyr Pro Pro Asp
165 170 175
gag gta att cat caa tca ttt cca aaa gca aca att atc tct ttt aca 576
Glu Val Ile His Gln Ser Phe Pro Lys Ala Thr Ile Ile Ser Phe Thr
180 185 190
aat tta tat cag gca tta gca tcc gtc tca gct ggg cac aat gat tac 624
Asn Leu Tyr Gln Ala Leu Ala Ser Val Ser Ala Gly His Asn Asp Tyr
195 200 205
ttt att ggt agt aac atc att acc agc agt atg att tcc cgc tat ttc 672
Phe Ile Gly Ser Asn Ile Ile Thr Ser Ser Met Ile Ser Arg Tyr Phe
210 215 220
act cac tcc tta aat gta gtg aaa tat tat aac tcg ccg cgt caa tat 720
Thr His Ser Leu Asn Val Val Lys Tyr Tyr Asn Ser Pro Arg Gln Tyr
225 230 235 240
aat ttt ttc ttg acc aga aaa gaa tct gtc att ctt aat gaa gta ctc 768
Asn Phe Phe Leu Thr Arg Lys Glu Ser Val Ile Leu Asn Glu Val Leu
245 250 255
aat aga ttt gtt gat gct tta aca aat gaa gtt cgc tat gaa gta tca 816
Asn Arg Phe Val Asp Ala Leu Thr Asn Glu Val Arg Tyr Glu Val Ser
260 265 270
caa aat tgg ctt gat aca gga aac ctg gcc ttt ctg aac aaa cca tta 864
Gln Asn Trp Leu Asp Thr Gly Asn Leu Ala Phe Leu Asn Lys Pro Leu
275 280 285
gaa ctc act gaa cat gaa aaa cag tgg att aag cag cat ccc aat tta 912
Glu Leu Thr Glu His Glu Lys Gln Trp Ile Lys Gln His Pro Asn Leu
290 295 300
aag gtg ctg gaa aat cct tac tcg ccc ccc tat tct atg acg gat gaa 960
Lys Val Leu Glu Asn Pro Tyr Ser Pro Pro Tyr Ser Met Thr Asp Glu
305 310 315 320
aat ggc tcg gtt cgg ggc gtt atg ggg gac att ctt aat att att acc 1008
Asn Gly Ser Val Arg Gly Val Met Gly Asp Ile Leu Asn Ile Ile Thr
325 330 335
ttg caa aca ggt tta aat ttt tct ccg atc acc gtt tca cac aat atc 1056
Leu Gln Thr Gly Leu Asn Phe Ser Pro Ile Thr Val Ser His Asn Ile
340 345 350
cat gct gga aca cag ctt agc ccc gga gga tgg gat ata ata cct ggc 1104
His Ala Gly Thr Gln Leu Ser Pro Gly Gly Trp Asp Ile Ile Pro Gly
355 360 365
gct att tat agt gaa gat cga gaa aat aat gtt tta ttt gct gaa gcc 1152
Ala Ile Tyr Ser Glu Asp Arg Glu Asn Asn Val Leu Phe Ala Glu Ala
370 375 380
ttc ata aca acg cct tac gtt ttt gtc atg caa aaa gcg cct gac agt 1200
Phe Ile Thr Thr Pro Tyr Val Phe Val Met Gln Lys Ala Pro Asp Ser
385 390 395 400
gaa caa aca tta aaa aaa gga atg aaa gtt gcc att cca tat tat tat 1248
Glu Gln Thr Leu Lys Lys Gly Met Lys Val Ala Ile Pro Tyr Tyr Tyr
405 410 415
gag ctg cat tcg caa tta aaa gag atg tat ccg gag gtt gaa tgg ata 1296
Glu Leu His Ser Gln Leu Lys Glu Met Tyr Pro Glu Val Glu Trp Ile
420 425 430
cag gtc gat aat gcc agc gct gca ttt cac aag gtt aag gaa ggt gaa 1344
Gln Val Asp Asn Ala Ser Ala Ala Phe His Lys Val Lys Glu Gly Glu
435 440 445
ctt gat gct ctg gtc gcg aca cag cta aat tcg cgt tac atg atc gat 1392
Leu Asp Ala Leu Val Ala Thr Gln Leu Asn Ser Arg Tyr Met Ile Asp
450 455 460
cat tac tat cct aat gaa ctt tat cat ttt ctt att cct ggc gtt ccg 1440
His Tyr Tyr Pro Asn Glu Leu Tyr His Phe Leu Ile Pro Gly Val Pro
465 470 475 480
aat gca tcg ctt tcg ttc gct ttt cct cgc gga gaa ccg gaa ctt aag 1488
Asn Ala Ser Leu Ser Phe Ala Phe Pro Arg Gly Glu Pro Glu Leu Lys
485 490 495
gat att att aat aaa gca ctg aat gca att ccc cca agc gaa gtt ctg 1536
Asp Ile Ile Asn Lys Ala Leu Asn Ala Ile Pro Pro Ser Glu Val Leu
500 505 510
cgc ctg acg gaa aaa tgg att aaa atg ccc aat gtg acc att gac aca 1584
Arg Leu Thr Glu Lys Trp Ile Lys Met Pro Asn Val Thr Ile Asp Thr
515 520 525
tgg gac cta tat agc gag caa ttt tat att gtt acg aca tta tcc gtt 1632
Trp Asp Leu Tyr Ser Glu Gln Phe Tyr Ile Val Thr Thr Leu Ser Val
530 535 540
tta tta gtt ggc agt agc ctt tta tgg gga ttc tac ctg tta cgc tca 1680
Leu Leu Val Gly Ser Ser Leu Leu Trp Gly Phe Tyr Leu Leu Arg Ser
545 550 555 560
gtt cgt cgt cgt aaa gtc att cag ggt gat tta gaa aac caa ata tca 1728
Val Arg Arg Arg Lys Val Ile Gln Gly Asp Leu Glu Asn Gln Ile Ser
565 570 575
ttc cga aaa gca ctc tcg gat tcc tta ccg aat cca act tat gtt gta 1776
Phe Arg Lys Ala Leu Ser Asp Ser Leu Pro Asn Pro Thr Tyr Val Val
580 585 590
aac tgg caa ggt aat gtc att agt cat aat agt gct ttt gaa cat tat 1824
Asn Trp Gln Gly Asn Val Ile Ser His Asn Ser Ala Phe Glu His Tyr
595 600 605
ttc act gcg gat tac tac aaa aat gca atg tta cca tta gaa aac agt 1872
Phe Thr Ala Asp Tyr Tyr Lys Asn Ala Met Leu Pro Leu Glu Asn Ser
610 615 620
gac tca ccc ttt aaa gat gtt ttt tct aat gcg cat gaa gtc aca gca 1920
Asp Ser Pro Phe Lys Asp Val Phe Ser Asn Ala His Glu Val Thr Ala
625 630 635 640
gaa acg aaa gaa aat cga aca ata tac aca cag gta ttt gaa att gat 1968
Glu Thr Lys Glu Asn Arg Thr Ile Tyr Thr Gln Val Phe Glu Ile Asp
645 650 655
aat ggc atc gag aaa aga tgc att aat cac tgg cat aca tta tgc aat 2016
Asn Gly Ile Glu Lys Arg Cys Ile Asn His Trp His Thr Leu Cys Asn
660 665 670
ctt cct gca agt gac aat gca gta tat att tgt ggt tgg caa gat att 2064
Leu Pro Ala Ser Asp Asn Ala Val Tyr Ile Cys Gly Trp Gln Asp Ile
675 680 685
act gaa acg cgt gat cta att aat gca ctc gag gta gaa aaa aat aaa 2112
Thr Glu Thr Arg Asp Leu Ile Asn Ala Leu Glu Val Glu Lys Asn Lys
690 695 700
gcg ata aag gct acc gta gca aaa agt cag ttt ctg gca acg atg agt 2160
Ala Ile Lys Ala Thr Val Ala Lys Ser Gln Phe Leu Ala Thr Met Ser
705 710 715 720
cac gaa ata aga aca cca ata agc tct att atg ggc ttc ctg gaa ctt 2208
His Glu Ile Arg Thr Pro Ile Ser Ser Ile Met Gly Phe Leu Glu Leu
725 730 735
ctg tcg ggt tct ggt ctt agc aag gag caa cgg gtg gag gcg att tca 2256
Leu Ser Gly Ser Gly Leu Ser Lys Glu Gln Arg Val Glu Ala Ile Ser
740 745 750
ctt gcc tac gcc acc gga caa tca ctc ctc ggc tta att ggt gaa atc 2304
Leu Ala Tyr Ala Thr Gly Gln Ser Leu Leu Gly Leu Ile Gly Glu Ile
755 760 765
ctt gat gtc gac aaa att gaa tcg ggt aac tat caa ctt caa cca caa 2352
Leu Asp Val Asp Lys Ile Glu Ser Gly Asn Tyr Gln Leu Gln Pro Gln
770 775 780
tgg gtc gat atc cct act tta gtc cag aac act tgt cac tct ttc ggt 2400
Trp Val Asp Ile Pro Thr Leu Val Gln Asn Thr Cys His Ser Phe Gly
785 790 795 800
gcg att gct gca agc aaa tcg atc gca tta agt tgc agc agt acg ttt 2448
Ala Ile Ala Ala Ser Lys Ser Ile Ala Leu Ser Cys Ser Ser Thr Phe
805 810 815
cct gaa cat tac ctg gtt aag atc gac cct cag gcg ttt aag cag gtc 2496
Pro Glu His Tyr Leu Val Lys Ile Asp Pro Gln Ala Phe Lys Gln Val
820 825 830
tta tca aat tta ctg agt aat gct ctc aaa ttt acc acc gag ggg gca 2544
Leu Ser Asn Leu Leu Ser Asn Ala Leu Lys Phe Thr Thr Glu Gly Ala
835 840 845
gta aaa att acg acc tcc ctg ggt cac att gat gac aac cac gct gtt 2592
Val Lys Ile Thr Thr Ser Leu Gly His Ile Asp Asp Asn His Ala Val
850 855 860
atc aaa atg acg att atg gat tct gga agt gga tta tcg cag gaa gaa 2640
Ile Lys Met Thr Ile Met Asp Ser Gly Ser Gly Leu Ser Gln Glu Glu
865 870 875 880
caa caa caa ctg ttt aaa cgc tac agc caa aca agt gca ggt cgt cag 2688
Gln Gln Gln Leu Phe Lys Arg Tyr Ser Gln Thr Ser Ala Gly Arg Gln
885 890 895
caa aca ggt tct ggt tta ggc tta atg atc tgc aaa gaa tta att aaa 2736
Gln Thr Gly Ser Gly Leu Gly Leu Met Ile Cys Lys Glu Leu Ile Lys
900 905 910
aat atg cag ggc gat ttg tca tta gaa agt cat cca ggc ata gga aca 2784
Asn Met Gln Gly Asp Leu Ser Leu Glu Ser His Pro Gly Ile Gly Thr
915 920 925
aca ttt acg atc aca atc ccg gta gaa att agc cag caa gtg gcg act 2832
Thr Phe Thr Ile Thr Ile Pro Val Glu Ile Ser Gln Gln Val Ala Thr
930 935 940
gtc gag gca aaa gca gaa caa ccc atc aca cta cct gaa aag ttg agc 2880
Val Glu Ala Lys Ala Glu Gln Pro Ile Thr Leu Pro Glu Lys Leu Ser
945 950 955 960
ata tta atc gcg gat gat cat ccg acc aac agg cta tta ctc aaa cgc 2928
Ile Leu Ile Ala Asp Asp His Pro Thr Asn Arg Leu Leu Leu Lys Arg
965 970 975
cag cta aat cta tta gga tat gat gtt gat gaa gcc act gat ggt gtg 2976
Gln Leu Asn Leu Leu Gly Tyr Asp Val Asp Glu Ala Thr Asp Gly Val
980 985 990
caa gcg cta cac aaa gtc agt atg caa cat tat gat ctg ctt att act 3024
Gln Ala Leu His Lys Val Ser Met Gln His Tyr Asp Leu Leu Ile Thr
995 1000 1005
gac gtt aat atg ccg aat atg gat ggt ttt gag ttg act cgc aaa 3069
Asp Val Asn Met Pro Asn Met Asp Gly Phe Glu Leu Thr Arg Lys
1010 1015 1020
ctc cgt gag caa aat tct tcc tta ccc atc tgg ggg ctt aca gcc 3114
Leu Arg Glu Gln Asn Ser Ser Leu Pro Ile Trp Gly Leu Thr Ala
1025 1030 1035
aac gca cag gct aac gaa cgt gaa aaa ggg tta agt tgc ggc atg 3159
Asn Ala Gln Ala Asn Glu Arg Glu Lys Gly Leu Ser Cys Gly Met
1040 1045 1050
aac tta tgt ttg ttc aaa ccg ttg acc ctg gat gta ctg aaa aca 3204
Asn Leu Cys Leu Phe Lys Pro Leu Thr Leu Asp Val Leu Lys Thr
1055 1060 1065
cat tta agt cag tta cac caa gtt gcg cat att gca cct cag tat 3249
His Leu Ser Gln Leu His Gln Val Ala His Ile Ala Pro Gln Tyr
1070 1075 1080
cgc cac ctt gat atc gaa gcc ctg aaa aat aat acg gcg aac gat 3294
Arg His Leu Asp Ile Glu Ala Leu Lys Asn Asn Thr Ala Asn Asp
1085 1090 1095
cta caa ctg atg cag gag att ctc atg act ttc cag cat gaa acg 3339
Leu Gln Leu Met Gln Glu Ile Leu Met Thr Phe Gln His Glu Thr
1100 1105 1110
cat aaa gat cta ccc gct gcg ttt caa gca cta gaa gct ggc gat 3384
His Lys Asp Leu Pro Ala Ala Phe Gln Ala Leu Glu Ala Gly Asp
1115 1120 1125
aac aga act ttc cat cag tgt att cat cgc atc cac ggt gcg gct 3429
Asn Arg Thr Phe His Gln Cys Ile His Arg Ile His Gly Ala Ala
1130 1135 1140
aac atc ctg aat ttg caa aag ttg att aat att agc cat cag tta 3474
Asn Ile Leu Asn Leu Gln Lys Leu Ile Asn Ile Ser His Gln Leu
1145 1150 1155
gaa ata aca cct gtt tca gat gac agt aag cct gaa att ctt cag 3519
Glu Ile Thr Pro Val Ser Asp Asp Ser Lys Pro Glu Ile Leu Gln
1160 1165 1170
ttg ctg aac tct gta aaa gaa cac att gca gag ctg gac cag gag 3564
Leu Leu Asn Ser Val Lys Glu His Ile Ala Glu Leu Asp Gln Glu
1175 1180 1185
att gct gtt ttc tgt cag aaa aat gac taa 3594
Ile Ala Val Phe Cys Gln Lys Asn Asp
1190 1195
<210> 26
<211> 1197
<212> PRT
<213> Escherichia coli
<400> 26
Met Lys Phe Leu Pro Tyr Ile Phe Leu Leu Cys Cys Gly Leu Trp Ser
1 5 10 15
Thr Ile Ser Phe Ala Asp Glu Asp Tyr Ile Glu Tyr Arg Gly Ile Ser
20 25 30
Ser Asn Asn Arg Val Thr Leu Asp Pro Leu Arg Leu Ser Asn Lys Glu
35 40 45
Leu Arg Trp Leu Ala Ser Lys Lys Asn Leu Val Ile Ala Val His Lys
50 55 60
Ser Gln Thr Ala Thr Leu Leu His Thr Asp Ser Gln Gln Arg Val Arg
65 70 75 80
Gly Ile Asn Ala Asp Tyr Leu Asn Leu Leu Lys Arg Ala Leu Asn Ile
85 90 95
Lys Leu Thr Leu Arg Glu Tyr Ala Asp His Gln Lys Ala Met Asp Ala
100 105 110
Leu Ala Glu Gly Glu Val Asp Ile Val Leu Ser His Leu Val Thr Ser
115 120 125
Pro Pro Leu Asn Asn Asp Ile Ala Ala Thr Lys Pro Leu Ile Ile Thr
130 135 140
Phe Pro Ala Leu Val Thr Thr Leu His Asp Ser Met Arg Pro Leu Thr
145 150 155 160
Ser Pro Lys Pro Val Asn Ile Ala Arg Val Ala Asn Tyr Pro Pro Asp
165 170 175
Glu Val Ile His Gln Ser Phe Pro Lys Ala Thr Ile Ile Ser Phe Thr
180 185 190
Asn Leu Tyr Gln Ala Leu Ala Ser Val Ser Ala Gly His Asn Asp Tyr
195 200 205
Phe Ile Gly Ser Asn Ile Ile Thr Ser Ser Met Ile Ser Arg Tyr Phe
210 215 220
Thr His Ser Leu Asn Val Val Lys Tyr Tyr Asn Ser Pro Arg Gln Tyr
225 230 235 240
Asn Phe Phe Leu Thr Arg Lys Glu Ser Val Ile Leu Asn Glu Val Leu
245 250 255
Asn Arg Phe Val Asp Ala Leu Thr Asn Glu Val Arg Tyr Glu Val Ser
260 265 270
Gln Asn Trp Leu Asp Thr Gly Asn Leu Ala Phe Leu Asn Lys Pro Leu
275 280 285
Glu Leu Thr Glu His Glu Lys Gln Trp Ile Lys Gln His Pro Asn Leu
290 295 300
Lys Val Leu Glu Asn Pro Tyr Ser Pro Pro Tyr Ser Met Thr Asp Glu
305 310 315 320
Asn Gly Ser Val Arg Gly Val Met Gly Asp Ile Leu Asn Ile Ile Thr
325 330 335
Leu Gln Thr Gly Leu Asn Phe Ser Pro Ile Thr Val Ser His Asn Ile
340 345 350
His Ala Gly Thr Gln Leu Ser Pro Gly Gly Trp Asp Ile Ile Pro Gly
355 360 365
Ala Ile Tyr Ser Glu Asp Arg Glu Asn Asn Val Leu Phe Ala Glu Ala
370 375 380
Phe Ile Thr Thr Pro Tyr Val Phe Val Met Gln Lys Ala Pro Asp Ser
385 390 395 400
Glu Gln Thr Leu Lys Lys Gly Met Lys Val Ala Ile Pro Tyr Tyr Tyr
405 410 415
Glu Leu His Ser Gln Leu Lys Glu Met Tyr Pro Glu Val Glu Trp Ile
420 425 430
Gln Val Asp Asn Ala Ser Ala Ala Phe His Lys Val Lys Glu Gly Glu
435 440 445
Leu Asp Ala Leu Val Ala Thr Gln Leu Asn Ser Arg Tyr Met Ile Asp
450 455 460
His Tyr Tyr Pro Asn Glu Leu Tyr His Phe Leu Ile Pro Gly Val Pro
465 470 475 480
Asn Ala Ser Leu Ser Phe Ala Phe Pro Arg Gly Glu Pro Glu Leu Lys
485 490 495
Asp Ile Ile Asn Lys Ala Leu Asn Ala Ile Pro Pro Ser Glu Val Leu
500 505 510
Arg Leu Thr Glu Lys Trp Ile Lys Met Pro Asn Val Thr Ile Asp Thr
515 520 525
Trp Asp Leu Tyr Ser Glu Gln Phe Tyr Ile Val Thr Thr Leu Ser Val
530 535 540
Leu Leu Val Gly Ser Ser Leu Leu Trp Gly Phe Tyr Leu Leu Arg Ser
545 550 555 560
Val Arg Arg Arg Lys Val Ile Gln Gly Asp Leu Glu Asn Gln Ile Ser
565 570 575
Phe Arg Lys Ala Leu Ser Asp Ser Leu Pro Asn Pro Thr Tyr Val Val
580 585 590
Asn Trp Gln Gly Asn Val Ile Ser His Asn Ser Ala Phe Glu His Tyr
595 600 605
Phe Thr Ala Asp Tyr Tyr Lys Asn Ala Met Leu Pro Leu Glu Asn Ser
610 615 620
Asp Ser Pro Phe Lys Asp Val Phe Ser Asn Ala His Glu Val Thr Ala
625 630 635 640
Glu Thr Lys Glu Asn Arg Thr Ile Tyr Thr Gln Val Phe Glu Ile Asp
645 650 655
Asn Gly Ile Glu Lys Arg Cys Ile Asn His Trp His Thr Leu Cys Asn
660 665 670
Leu Pro Ala Ser Asp Asn Ala Val Tyr Ile Cys Gly Trp Gln Asp Ile
675 680 685
Thr Glu Thr Arg Asp Leu Ile Asn Ala Leu Glu Val Glu Lys Asn Lys
690 695 700
Ala Ile Lys Ala Thr Val Ala Lys Ser Gln Phe Leu Ala Thr Met Ser
705 710 715 720
His Glu Ile Arg Thr Pro Ile Ser Ser Ile Met Gly Phe Leu Glu Leu
725 730 735
Leu Ser Gly Ser Gly Leu Ser Lys Glu Gln Arg Val Glu Ala Ile Ser
740 745 750
Leu Ala Tyr Ala Thr Gly Gln Ser Leu Leu Gly Leu Ile Gly Glu Ile
755 760 765
Leu Asp Val Asp Lys Ile Glu Ser Gly Asn Tyr Gln Leu Gln Pro Gln
770 775 780
Trp Val Asp Ile Pro Thr Leu Val Gln Asn Thr Cys His Ser Phe Gly
785 790 795 800
Ala Ile Ala Ala Ser Lys Ser Ile Ala Leu Ser Cys Ser Ser Thr Phe
805 810 815
Pro Glu His Tyr Leu Val Lys Ile Asp Pro Gln Ala Phe Lys Gln Val
820 825 830
Leu Ser Asn Leu Leu Ser Asn Ala Leu Lys Phe Thr Thr Glu Gly Ala
835 840 845
Val Lys Ile Thr Thr Ser Leu Gly His Ile Asp Asp Asn His Ala Val
850 855 860
Ile Lys Met Thr Ile Met Asp Ser Gly Ser Gly Leu Ser Gln Glu Glu
865 870 875 880
Gln Gln Gln Leu Phe Lys Arg Tyr Ser Gln Thr Ser Ala Gly Arg Gln
885 890 895
Gln Thr Gly Ser Gly Leu Gly Leu Met Ile Cys Lys Glu Leu Ile Lys
900 905 910
Asn Met Gln Gly Asp Leu Ser Leu Glu Ser His Pro Gly Ile Gly Thr
915 920 925
Thr Phe Thr Ile Thr Ile Pro Val Glu Ile Ser Gln Gln Val Ala Thr
930 935 940
Val Glu Ala Lys Ala Glu Gln Pro Ile Thr Leu Pro Glu Lys Leu Ser
945 950 955 960
Ile Leu Ile Ala Asp Asp His Pro Thr Asn Arg Leu Leu Leu Lys Arg
965 970 975
Gln Leu Asn Leu Leu Gly Tyr Asp Val Asp Glu Ala Thr Asp Gly Val
980 985 990
Gln Ala Leu His Lys Val Ser Met Gln His Tyr Asp Leu Leu Ile Thr
995 1000 1005
Asp Val Asn Met Pro Asn Met Asp Gly Phe Glu Leu Thr Arg Lys
1010 1015 1020
Leu Arg Glu Gln Asn Ser Ser Leu Pro Ile Trp Gly Leu Thr Ala
1025 1030 1035
Asn Ala Gln Ala Asn Glu Arg Glu Lys Gly Leu Ser Cys Gly Met
1040 1045 1050
Asn Leu Cys Leu Phe Lys Pro Leu Thr Leu Asp Val Leu Lys Thr
1055 1060 1065
His Leu Ser Gln Leu His Gln Val Ala His Ile Ala Pro Gln Tyr
1070 1075 1080
Arg His Leu Asp Ile Glu Ala Leu Lys Asn Asn Thr Ala Asn Asp
1085 1090 1095
Leu Gln Leu Met Gln Glu Ile Leu Met Thr Phe Gln His Glu Thr
1100 1105 1110
His Lys Asp Leu Pro Ala Ala Phe Gln Ala Leu Glu Ala Gly Asp
1115 1120 1125
Asn Arg Thr Phe His Gln Cys Ile His Arg Ile His Gly Ala Ala
1130 1135 1140
Asn Ile Leu Asn Leu Gln Lys Leu Ile Asn Ile Ser His Gln Leu
1145 1150 1155
Glu Ile Thr Pro Val Ser Asp Asp Ser Lys Pro Glu Ile Leu Gln
1160 1165 1170
Leu Leu Asn Ser Val Lys Glu His Ile Ala Glu Leu Asp Gln Glu
1175 1180 1185
Ile Ala Val Phe Cys Gln Lys Asn Asp
1190 1195
<210> 27
<211> 528
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(528)
<400> 27
atg att ttt ctc atg acg aaa gat tct ttt ctt tta cag ggc ttt tgg 48
Met Ile Phe Leu Met Thr Lys Asp Ser Phe Leu Leu Gln Gly Phe Trp
1 5 10 15
cag ttg aaa gat aat cac gaa atg ata aaa atc aat tcc ctg tca gag 96
Gln Leu Lys Asp Asn His Glu Met Ile Lys Ile Asn Ser Leu Ser Glu
20 25 30
atc aaa aaa gta ggc aat aaa ccc ttc aag gtt atc att gat acc tat 144
Ile Lys Lys Val Gly Asn Lys Pro Phe Lys Val Ile Ile Asp Thr Tyr
35 40 45
cac aat cat atc ctt gat gaa gaa gcg att aaa ttt ctg gag aaa tta 192
His Asn His Ile Leu Asp Glu Glu Ala Ile Lys Phe Leu Glu Lys Leu
50 55 60
gat gcc gag aga att att gtt ttg gca cct tat cac atc agt aaa cta 240
Asp Ala Glu Arg Ile Ile Val Leu Ala Pro Tyr His Ile Ser Lys Leu
65 70 75 80
aaa gct aaa gcg cct att tat ttt gtt agc cgc aaa gaa agt atc aaa 288
Lys Ala Lys Ala Pro Ile Tyr Phe Val Ser Arg Lys Glu Ser Ile Lys
85 90 95
aat ctt ctt gag att act tat ggt aaa cac ttg ccc cat aag aat tca 336
Asn Leu Leu Glu Ile Thr Tyr Gly Lys His Leu Pro His Lys Asn Ser
100 105 110
caa tta tgt ttt tca cat aat cag ttc aaa att atg caa ctg att ctg 384
Gln Leu Cys Phe Ser His Asn Gln Phe Lys Ile Met Gln Leu Ile Leu
115 120 125
aaa aat aaa aat gaa agc aat atc acg tcg acg ctc aat att tcg caa 432
Lys Asn Lys Asn Glu Ser Asn Ile Thr Ser Thr Leu Asn Ile Ser Gln
130 135 140
caa aca tta aag att cag aaa ttc aac att atg tac aag ctg aaa cta 480
Gln Thr Leu Lys Ile Gln Lys Phe Asn Ile Met Tyr Lys Leu Lys Leu
145 150 155 160
aga cgt atg agc gac atc gtc acc ctg ggt atc aca tct tat ttt tag 528
Arg Arg Met Ser Asp Ile Val Thr Leu Gly Ile Thr Ser Tyr Phe
165 170 175
<210> 28
<211> 175
<212> PRT
<213> Escherichia coli
<400> 28
Met Ile Phe Leu Met Thr Lys Asp Ser Phe Leu Leu Gln Gly Phe Trp
1 5 10 15
Gln Leu Lys Asp Asn His Glu Met Ile Lys Ile Asn Ser Leu Ser Glu
20 25 30
Ile Lys Lys Val Gly Asn Lys Pro Phe Lys Val Ile Ile Asp Thr Tyr
35 40 45
His Asn His Ile Leu Asp Glu Glu Ala Ile Lys Phe Leu Glu Lys Leu
50 55 60
Asp Ala Glu Arg Ile Ile Val Leu Ala Pro Tyr His Ile Ser Lys Leu
65 70 75 80
Lys Ala Lys Ala Pro Ile Tyr Phe Val Ser Arg Lys Glu Ser Ile Lys
85 90 95
Asn Leu Leu Glu Ile Thr Tyr Gly Lys His Leu Pro His Lys Asn Ser
100 105 110
Gln Leu Cys Phe Ser His Asn Gln Phe Lys Ile Met Gln Leu Ile Leu
115 120 125
Lys Asn Lys Asn Glu Ser Asn Ile Thr Ser Thr Leu Asn Ile Ser Gln
130 135 140
Gln Thr Leu Lys Ile Gln Lys Phe Asn Ile Met Tyr Lys Leu Lys Leu
145 150 155 160
Arg Arg Met Ser Asp Ile Val Thr Leu Gly Ile Thr Ser Tyr Phe
165 170 175
<210> 29
<211> 762
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(762)
<400> 29
atg tcg ctc gtt tgt tct gtt ata ttt att cat cat gcc ttc aac gct 48
Met Ser Leu Val Cys Ser Val Ile Phe Ile His His Ala Phe Asn Ala
1 5 10 15
aac att tta gat aaa gat tac gcc ttc tct gac ggc gag atc ctg atg 96
Asn Ile Leu Asp Lys Asp Tyr Ala Phe Ser Asp Gly Glu Ile Leu Met
20 25 30
gta gat aac gct gtt cgt acg cat ttt gaa cct tat gag cgg cat ttt 144
Val Asp Asn Ala Val Arg Thr His Phe Glu Pro Tyr Glu Arg His Phe
35 40 45
aaa gag atc gga ttt act gaa aat acc att aaa aaa tat cta caa tgc 192
Lys Glu Ile Gly Phe Thr Glu Asn Thr Ile Lys Lys Tyr Leu Gln Cys
50 55 60
act aac atc cag aca gtg acg gtg cct gtt cct gcg aag ttt tta cgt 240
Thr Asn Ile Gln Thr Val Thr Val Pro Val Pro Ala Lys Phe Leu Arg
65 70 75 80
gct tca aat gta ccg act gga ttg ctt aat gaa atg att gct tat ctc 288
Ala Ser Asn Val Pro Thr Gly Leu Leu Asn Glu Met Ile Ala Tyr Leu
85 90 95
aac tcg gaa gaa cgc aat cat cat aat ttt tca gaa ctt ttg ctt ttt 336
Asn Ser Glu Glu Arg Asn His His Asn Phe Ser Glu Leu Leu Leu Phe
100 105 110
tct tgc ctg tct att ttt gcc gca tgc aaa ggt ttc att aca cta tta 384
Ser Cys Leu Ser Ile Phe Ala Ala Cys Lys Gly Phe Ile Thr Leu Leu
115 120 125
act aac ggt gtg cta tcc gtt tct ggg aaa gtg aga aat att gtc aac 432
Thr Asn Gly Val Leu Ser Val Ser Gly Lys Val Arg Asn Ile Val Asn
130 135 140
atg aag ccg gcg cac cca tgg aag ctg aaa gat att tgt gac tgc ctg 480
Met Lys Pro Ala His Pro Trp Lys Leu Lys Asp Ile Cys Asp Cys Leu
145 150 155 160
tac atc agt gaa agc ctg ttg aag aaa aaa ctt aag caa gag caa acg 528
Tyr Ile Ser Glu Ser Leu Leu Lys Lys Lys Leu Lys Gln Glu Gln Thr
165 170 175
aca ttc tca cag att ctt tta gat gca aga atg cag cac gca aaa aat 576
Thr Phe Ser Gln Ile Leu Leu Asp Ala Arg Met Gln His Ala Lys Asn
180 185 190
ttg ata cgc gta gaa ggt tca gtc aat aaa att gcc gaa caa tgt ggt 624
Leu Ile Arg Val Glu Gly Ser Val Asn Lys Ile Ala Glu Gln Cys Gly
195 200 205
tat gcc agt aca tct tat ttt att tat gcg ttc cgc aaa cat ttc ggc 672
Tyr Ala Ser Thr Ser Tyr Phe Ile Tyr Ala Phe Arg Lys His Phe Gly
210 215 220
aac agt ccg aag aga gtt tct aag gag tac cgt tgt caa agt cac acg 720
Asn Ser Pro Lys Arg Val Ser Lys Glu Tyr Arg Cys Gln Ser His Thr
225 230 235 240
ggt atg aat acg ggc aac acg atg aat gct tta gct att tga 762
Gly Met Asn Thr Gly Asn Thr Met Asn Ala Leu Ala Ile
245 250
<210> 30
<211> 253
<212> PRT
<213> Escherichia coli
<400> 30
Met Ser Leu Val Cys Ser Val Ile Phe Ile His His Ala Phe Asn Ala
1 5 10 15
Asn Ile Leu Asp Lys Asp Tyr Ala Phe Ser Asp Gly Glu Ile Leu Met
20 25 30
Val Asp Asn Ala Val Arg Thr His Phe Glu Pro Tyr Glu Arg His Phe
35 40 45
Lys Glu Ile Gly Phe Thr Glu Asn Thr Ile Lys Lys Tyr Leu Gln Cys
50 55 60
Thr Asn Ile Gln Thr Val Thr Val Pro Val Pro Ala Lys Phe Leu Arg
65 70 75 80
Ala Ser Asn Val Pro Thr Gly Leu Leu Asn Glu Met Ile Ala Tyr Leu
85 90 95
Asn Ser Glu Glu Arg Asn His His Asn Phe Ser Glu Leu Leu Leu Phe
100 105 110
Ser Cys Leu Ser Ile Phe Ala Ala Cys Lys Gly Phe Ile Thr Leu Leu
115 120 125
Thr Asn Gly Val Leu Ser Val Ser Gly Lys Val Arg Asn Ile Val Asn
130 135 140
Met Lys Pro Ala His Pro Trp Lys Leu Lys Asp Ile Cys Asp Cys Leu
145 150 155 160
Tyr Ile Ser Glu Ser Leu Leu Lys Lys Lys Leu Lys Gln Glu Gln Thr
165 170 175
Thr Phe Ser Gln Ile Leu Leu Asp Ala Arg Met Gln His Ala Lys Asn
180 185 190
Leu Ile Arg Val Glu Gly Ser Val Asn Lys Ile Ala Glu Gln Cys Gly
195 200 205
Tyr Ala Ser Thr Ser Tyr Phe Ile Tyr Ala Phe Arg Lys His Phe Gly
210 215 220
Asn Ser Pro Lys Arg Val Ser Lys Glu Tyr Arg Cys Gln Ser His Thr
225 230 235 240
Gly Met Asn Thr Gly Asn Thr Met Asn Ala Leu Ala Ile
245 250
<210> 31
<211> 2148
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(2145)
<400> 31
atg aac gtt att gca ata ttg aat cac atg ggg gtt tat ttt aaa gaa 48
Met Asn Val Ile Ala Ile Leu Asn His Met Gly Val Tyr Phe Lys Glu
1 5 10 15
gaa ccc atc cgt gaa ctt cat cgc gcg ctt gaa cgt ctg aac ttc cag 96
Glu Pro Ile Arg Glu Leu His Arg Ala Leu Glu Arg Leu Asn Phe Gln
20 25 30
att gtt tac ccg aac gac cgt gac gac tta tta aaa ctg atc gaa aac 144
Ile Val Tyr Pro Asn Asp Arg Asp Asp Leu Leu Lys Leu Ile Glu Asn
35 40 45
aat gcg cgt ctg tgc ggc gtt att ttt gac tgg gat aaa tat aat ctc 192
Asn Ala Arg Leu Cys Gly Val Ile Phe Asp Trp Asp Lys Tyr Asn Leu
50 55 60
gag ctg tgc gaa gaa att agc aaa atg aac gag aac ctg ccg ttg tac 240
Glu Leu Cys Glu Glu Ile Ser Lys Met Asn Glu Asn Leu Pro Leu Tyr
65 70 75 80
gcg ttc gct aat acg tat tcc act ctc gat gta agc ctg aat gac ctg 288
Ala Phe Ala Asn Thr Tyr Ser Thr Leu Asp Val Ser Leu Asn Asp Leu
85 90 95
cgt tta cag att agc ttc ttt gaa tat gcg ctg ggt gct gct gaa gat 336
Arg Leu Gln Ile Ser Phe Phe Glu Tyr Ala Leu Gly Ala Ala Glu Asp
100 105 110
att gct aat aag atc aag cag acc act gac gaa tat atc aac act att 384
Ile Ala Asn Lys Ile Lys Gln Thr Thr Asp Glu Tyr Ile Asn Thr Ile
115 120 125
ctg cct ccg ctg act aaa gca ctg ttt aaa tat gtt cgt gaa ggt aaa 432
Leu Pro Pro Leu Thr Lys Ala Leu Phe Lys Tyr Val Arg Glu Gly Lys
130 135 140
tat act ttc tgt act cct ggt cac atg ggc ggt act gca ttc cag aaa 480
Tyr Thr Phe Cys Thr Pro Gly His Met Gly Gly Thr Ala Phe Gln Lys
145 150 155 160
agc ccg gta ggt agc ctg ttc tat gat ttc ttt ggt ccg aat acc atg 528
Ser Pro Val Gly Ser Leu Phe Tyr Asp Phe Phe Gly Pro Asn Thr Met
165 170 175
aaa tct gat att tcc att tca gta tct gaa ctg ggt tct ctg ctg gat 576
Lys Ser Asp Ile Ser Ile Ser Val Ser Glu Leu Gly Ser Leu Leu Asp
180 185 190
cac agt ggt cca cac aaa gaa gca gaa cag tat atc gct cgc gtc ttt 624
His Ser Gly Pro His Lys Glu Ala Glu Gln Tyr Ile Ala Arg Val Phe
195 200 205
aac gca gac cgc agc tac atg gtg acc aac ggt act tcc act gcg aac 672
Asn Ala Asp Arg Ser Tyr Met Val Thr Asn Gly Thr Ser Thr Ala Asn
210 215 220
aaa att gtt ggt atg tac tct gct cca gca ggc agc acc att ctg att 720
Lys Ile Val Gly Met Tyr Ser Ala Pro Ala Gly Ser Thr Ile Leu Ile
225 230 235 240
gac cgt aac tgc cac aaa tcg ctg acc cac ctg atg atg atg agc gat 768
Asp Arg Asn Cys His Lys Ser Leu Thr His Leu Met Met Met Ser Asp
245 250 255
gtt acg cca atc tat ttc cgc ccg acc cgt aac gct tac ggt att ctt 816
Val Thr Pro Ile Tyr Phe Arg Pro Thr Arg Asn Ala Tyr Gly Ile Leu
260 265 270
ggt ggt atc cca cag agt gaa ttc cag cac gct acc att gct aag cgc 864
Gly Gly Ile Pro Gln Ser Glu Phe Gln His Ala Thr Ile Ala Lys Arg
275 280 285
gtg aaa gaa aca cca aac gca acc tgg ccg gta cat gct gta att acc 912
Val Lys Glu Thr Pro Asn Ala Thr Trp Pro Val His Ala Val Ile Thr
290 295 300
aac tct acc tat gat ggt ctg ctg tac aac acc gac ttc atc aag aaa 960
Asn Ser Thr Tyr Asp Gly Leu Leu Tyr Asn Thr Asp Phe Ile Lys Lys
305 310 315 320
aca ctg gat gtg aaa tcc atc cac ttt gac tcc gcg tgg gtg cct tac 1008
Thr Leu Asp Val Lys Ser Ile His Phe Asp Ser Ala Trp Val Pro Tyr
325 330 335
acc aac ttc tca ccg att tac gaa ggt aaa tgc ggt atg agc ggt ggc 1056
Thr Asn Phe Ser Pro Ile Tyr Glu Gly Lys Cys Gly Met Ser Gly Gly
340 345 350
cgt gta gaa ggg aaa gtg att tac gaa acc cag tcc act cac aaa ctg 1104
Arg Val Glu Gly Lys Val Ile Tyr Glu Thr Gln Ser Thr His Lys Leu
355 360 365
ctg gcg gcg ttc tct cag gct tcc atg atc cac gtt aaa ggt gac gta 1152
Leu Ala Ala Phe Ser Gln Ala Ser Met Ile His Val Lys Gly Asp Val
370 375 380
aac gaa gaa acc ttt aac gaa gcc tac atg atg cac acc acc act tct 1200
Asn Glu Glu Thr Phe Asn Glu Ala Tyr Met Met His Thr Thr Thr Ser
385 390 395 400
ccg cac tac ggt atc gtg gcg tcc act gaa acc gct gcg gcg atg atg 1248
Pro His Tyr Gly Ile Val Ala Ser Thr Glu Thr Ala Ala Ala Met Met
405 410 415
aaa ggc aat gca ggt aag cgt ctg atc aac ggt tct att gaa cgt gcg 1296
Lys Gly Asn Ala Gly Lys Arg Leu Ile Asn Gly Ser Ile Glu Arg Ala
420 425 430
atc aaa ttc cgt aaa gag atc aaa cgt ctg aga acg gaa tct gat ggc 1344
Ile Lys Phe Arg Lys Glu Ile Lys Arg Leu Arg Thr Glu Ser Asp Gly
435 440 445
tgg ttc ttt gat gta tgg cag ccg gat cat atc gat acg act gaa tgc 1392
Trp Phe Phe Asp Val Trp Gln Pro Asp His Ile Asp Thr Thr Glu Cys
450 455 460
tgg ccg ctg cgt tct gac agc acc tgg cac ggc ttc aaa aac atc gat 1440
Trp Pro Leu Arg Ser Asp Ser Thr Trp His Gly Phe Lys Asn Ile Asp
465 470 475 480
aac gag cac atg tat ctt gac ccg atc aaa gtc acc ctg ctg act ccg 1488
Asn Glu His Met Tyr Leu Asp Pro Ile Lys Val Thr Leu Leu Thr Pro
485 490 495
ggg atg gaa aaa gac ggc acc atg agc gac ttt ggt att ccg gcc agc 1536
Gly Met Glu Lys Asp Gly Thr Met Ser Asp Phe Gly Ile Pro Ala Ser
500 505 510
atc gtg gcg aaa tac ctc gac gaa cat ggc atc gtt gtt gag aaa acc 1584
Ile Val Ala Lys Tyr Leu Asp Glu His Gly Ile Val Val Glu Lys Thr
515 520 525
ggt ccg tat aac ctg ctg ttc ctg ttc agc atc ggt atc gat aag acc 1632
Gly Pro Tyr Asn Leu Leu Phe Leu Phe Ser Ile Gly Ile Asp Lys Thr
530 535 540
aaa gca ctg agc ctg ctg cgt gct ctg act gac ttt aaa cgt gcg ttc 1680
Lys Ala Leu Ser Leu Leu Arg Ala Leu Thr Asp Phe Lys Arg Ala Phe
545 550 555 560
gac ctg aac ctg cgt gtg aaa aac atg ctg ccg tct ctg tat cgt gaa 1728
Asp Leu Asn Leu Arg Val Lys Asn Met Leu Pro Ser Leu Tyr Arg Glu
565 570 575
gat cct gaa ttc tat gaa aac atg cgt att cag gaa ctg gct cag aat 1776
Asp Pro Glu Phe Tyr Glu Asn Met Arg Ile Gln Glu Leu Ala Gln Asn
580 585 590
atc cac aaa ctg att gtt cac cac aat ctg ccg gat ctg atg tat cgc 1824
Ile His Lys Leu Ile Val His His Asn Leu Pro Asp Leu Met Tyr Arg
595 600 605
gca ttt gaa gtg ctg ccg acg atg gta atg act ccg tat gct gca ttc 1872
Ala Phe Glu Val Leu Pro Thr Met Val Met Thr Pro Tyr Ala Ala Phe
610 615 620
cag aaa gag ctg cac ggt atg acc gaa gaa gtt tac ctc gac gaa atg 1920
Gln Lys Glu Leu His Gly Met Thr Glu Glu Val Tyr Leu Asp Glu Met
625 630 635 640
gta ggt cgt att aac gcc aat atg atc ctt ccg tac ccg ccg gga gtt 1968
Val Gly Arg Ile Asn Ala Asn Met Ile Leu Pro Tyr Pro Pro Gly Val
645 650 655
cct ctg gta atg ccg ggt gaa atg atc acc gaa gaa agc cgt ccg gtt 2016
Pro Leu Val Met Pro Gly Glu Met Ile Thr Glu Glu Ser Arg Pro Val
660 665 670
ctg gag ttc ctg cag atg ctg tgt gaa atc ggc gct cac tat ccg ggc 2064
Leu Glu Phe Leu Gln Met Leu Cys Glu Ile Gly Ala His Tyr Pro Gly
675 680 685
ttt gaa acc gat att cac ggt gca tac cgt cag gct gat ggc cgc tat 2112
Phe Glu Thr Asp Ile His Gly Ala Tyr Arg Gln Ala Asp Gly Arg Tyr
690 695 700
acc gtt aag gta ttg aaa gaa gaa agc aaa aaa taa 2148
Thr Val Lys Val Leu Lys Glu Glu Ser Lys Lys
705 710 715
<210> 32
<211> 715
<212> PRT
<213> Escherichia coli
<400> 32
Met Asn Val Ile Ala Ile Leu Asn His Met Gly Val Tyr Phe Lys Glu
1 5 10 15
Glu Pro Ile Arg Glu Leu His Arg Ala Leu Glu Arg Leu Asn Phe Gln
20 25 30
Ile Val Tyr Pro Asn Asp Arg Asp Asp Leu Leu Lys Leu Ile Glu Asn
35 40 45
Asn Ala Arg Leu Cys Gly Val Ile Phe Asp Trp Asp Lys Tyr Asn Leu
50 55 60
Glu Leu Cys Glu Glu Ile Ser Lys Met Asn Glu Asn Leu Pro Leu Tyr
65 70 75 80
Ala Phe Ala Asn Thr Tyr Ser Thr Leu Asp Val Ser Leu Asn Asp Leu
85 90 95
Arg Leu Gln Ile Ser Phe Phe Glu Tyr Ala Leu Gly Ala Ala Glu Asp
100 105 110
Ile Ala Asn Lys Ile Lys Gln Thr Thr Asp Glu Tyr Ile Asn Thr Ile
115 120 125
Leu Pro Pro Leu Thr Lys Ala Leu Phe Lys Tyr Val Arg Glu Gly Lys
130 135 140
Tyr Thr Phe Cys Thr Pro Gly His Met Gly Gly Thr Ala Phe Gln Lys
145 150 155 160
Ser Pro Val Gly Ser Leu Phe Tyr Asp Phe Phe Gly Pro Asn Thr Met
165 170 175
Lys Ser Asp Ile Ser Ile Ser Val Ser Glu Leu Gly Ser Leu Leu Asp
180 185 190
His Ser Gly Pro His Lys Glu Ala Glu Gln Tyr Ile Ala Arg Val Phe
195 200 205
Asn Ala Asp Arg Ser Tyr Met Val Thr Asn Gly Thr Ser Thr Ala Asn
210 215 220
Lys Ile Val Gly Met Tyr Ser Ala Pro Ala Gly Ser Thr Ile Leu Ile
225 230 235 240
Asp Arg Asn Cys His Lys Ser Leu Thr His Leu Met Met Met Ser Asp
245 250 255
Val Thr Pro Ile Tyr Phe Arg Pro Thr Arg Asn Ala Tyr Gly Ile Leu
260 265 270
Gly Gly Ile Pro Gln Ser Glu Phe Gln His Ala Thr Ile Ala Lys Arg
275 280 285
Val Lys Glu Thr Pro Asn Ala Thr Trp Pro Val His Ala Val Ile Thr
290 295 300
Asn Ser Thr Tyr Asp Gly Leu Leu Tyr Asn Thr Asp Phe Ile Lys Lys
305 310 315 320
Thr Leu Asp Val Lys Ser Ile His Phe Asp Ser Ala Trp Val Pro Tyr
325 330 335
Thr Asn Phe Ser Pro Ile Tyr Glu Gly Lys Cys Gly Met Ser Gly Gly
340 345 350
Arg Val Glu Gly Lys Val Ile Tyr Glu Thr Gln Ser Thr His Lys Leu
355 360 365
Leu Ala Ala Phe Ser Gln Ala Ser Met Ile His Val Lys Gly Asp Val
370 375 380
Asn Glu Glu Thr Phe Asn Glu Ala Tyr Met Met His Thr Thr Thr Ser
385 390 395 400
Pro His Tyr Gly Ile Val Ala Ser Thr Glu Thr Ala Ala Ala Met Met
405 410 415
Lys Gly Asn Ala Gly Lys Arg Leu Ile Asn Gly Ser Ile Glu Arg Ala
420 425 430
Ile Lys Phe Arg Lys Glu Ile Lys Arg Leu Arg Thr Glu Ser Asp Gly
435 440 445
Trp Phe Phe Asp Val Trp Gln Pro Asp His Ile Asp Thr Thr Glu Cys
450 455 460
Trp Pro Leu Arg Ser Asp Ser Thr Trp His Gly Phe Lys Asn Ile Asp
465 470 475 480
Asn Glu His Met Tyr Leu Asp Pro Ile Lys Val Thr Leu Leu Thr Pro
485 490 495
Gly Met Glu Lys Asp Gly Thr Met Ser Asp Phe Gly Ile Pro Ala Ser
500 505 510
Ile Val Ala Lys Tyr Leu Asp Glu His Gly Ile Val Val Glu Lys Thr
515 520 525
Gly Pro Tyr Asn Leu Leu Phe Leu Phe Ser Ile Gly Ile Asp Lys Thr
530 535 540
Lys Ala Leu Ser Leu Leu Arg Ala Leu Thr Asp Phe Lys Arg Ala Phe
545 550 555 560
Asp Leu Asn Leu Arg Val Lys Asn Met Leu Pro Ser Leu Tyr Arg Glu
565 570 575
Asp Pro Glu Phe Tyr Glu Asn Met Arg Ile Gln Glu Leu Ala Gln Asn
580 585 590
Ile His Lys Leu Ile Val His His Asn Leu Pro Asp Leu Met Tyr Arg
595 600 605
Ala Phe Glu Val Leu Pro Thr Met Val Met Thr Pro Tyr Ala Ala Phe
610 615 620
Gln Lys Glu Leu His Gly Met Thr Glu Glu Val Tyr Leu Asp Glu Met
625 630 635 640
Val Gly Arg Ile Asn Ala Asn Met Ile Leu Pro Tyr Pro Pro Gly Val
645 650 655
Pro Leu Val Met Pro Gly Glu Met Ile Thr Glu Glu Ser Arg Pro Val
660 665 670
Leu Glu Phe Leu Gln Met Leu Cys Glu Ile Gly Ala His Tyr Pro Gly
675 680 685
Phe Glu Thr Asp Ile His Gly Ala Tyr Arg Gln Ala Asp Gly Arg Tyr
690 695 700
Thr Val Lys Val Leu Lys Glu Glu Ser Lys Lys
705 710 715
<210> 33
<211> 2142
<212> DNA
<213> Escherichia coli
<220>
<221> CDS
<222> (1)..(2139)
<400> 33
atg aac atc att gcc att atg gga ccg cat ggc gtc ttt tat aaa gat 48
Met Asn Ile Ile Ala Ile Met Gly Pro His Gly Val Phe Tyr Lys Asp
1 5 10 15
gag ccc atc aaa gaa ctg gag tcg gcg ctg gtg gcg caa ggc ttt cag 96
Glu Pro Ile Lys Glu Leu Glu Ser Ala Leu Val Ala Gln Gly Phe Gln
20 25 30
att atc tgg cca caa aac agc gtt gat ttg ctg aaa ttt atc gag cat 144
Ile Ile Trp Pro Gln Asn Ser Val Asp Leu Leu Lys Phe Ile Glu His
35 40 45
aac cct cga att tgc ggc gtg att ttt gac tgg gat gag tac agt ctc 192
Asn Pro Arg Ile Cys Gly Val Ile Phe Asp Trp Asp Glu Tyr Ser Leu
50 55 60
gat tta tgt agc gat atc aat cag ctt aat gaa tat ctc ccg ctt tat 240
Asp Leu Cys Ser Asp Ile Asn Gln Leu Asn Glu Tyr Leu Pro Leu Tyr
65 70 75 80
gcc ttc atc aac acc cac tcg acg atg gat gtc agc gtg cag gat atg 288
Ala Phe Ile Asn Thr His Ser Thr Met Asp Val Ser Val Gln Asp Met
85 90 95
cgg atg gcg ctc tgg ttt ttt gaa tat gcg ctg ggg cag gcg gaa gat 336
Arg Met Ala Leu Trp Phe Phe Glu Tyr Ala Leu Gly Gln Ala Glu Asp
100 105 110
atc gcc att cgt atg cgt cag tac acc gac gaa tat ctt gat aac att 384
Ile Ala Ile Arg Met Arg Gln Tyr Thr Asp Glu Tyr Leu Asp Asn Ile
115 120 125
aca ccg ccg ttc acg aaa gcc ttg ttt acc tac gtc aaa gag cgg aag 432
Thr Pro Pro Phe Thr Lys Ala Leu Phe Thr Tyr Val Lys Glu Arg Lys
130 135 140
tac acc ttt tgt acg ccg ggg cat atg ggc ggc acc gca tat caa aaa 480
Tyr Thr Phe Cys Thr Pro Gly His Met Gly Gly Thr Ala Tyr Gln Lys
145 150 155 160
agc ccg gtt ggc tgt ctg ttt tat gat ttt ttc ggc ggg aat act ctt 528
Ser Pro Val Gly Cys Leu Phe Tyr Asp Phe Phe Gly Gly Asn Thr Leu
165 170 175
aag gct gat gtc tct att tcg gtc acc gag ctt ggt tcg ttg ctc gac 576
Lys Ala Asp Val Ser Ile Ser Val Thr Glu Leu Gly Ser Leu Leu Asp
180 185 190
cac acc ggg cca cac ctg gaa gcg gaa gag tac atc gcg cgg act ttt 624
His Thr Gly Pro His Leu Glu Ala Glu Glu Tyr Ile Ala Arg Thr Phe
195 200 205
ggc gcg gaa cag agt tat atc gtt acc aac gga aca tcg acg tcg aac 672
Gly Ala Glu Gln Ser Tyr Ile Val Thr Asn Gly Thr Ser Thr Ser Asn
210 215 220
aaa att gtg ggt atg tac gcc gcg cca tcc ggc agt acg ctg ttg atc 720
Lys Ile Val Gly Met Tyr Ala Ala Pro Ser Gly Ser Thr Leu Leu Ile
225 230 235 240
gac cgc aat tgt cat aaa tcg ctg gcg cat ctg ttg atg atg aac gat 768
Asp Arg Asn Cys His Lys Ser Leu Ala His Leu Leu Met Met Asn Asp
245 250 255
gta gtg cca gtc tgg ctg aaa ccg acg cgt aat gcg ttg ggg att ctt 816
Val Val Pro Val Trp Leu Lys Pro Thr Arg Asn Ala Leu Gly Ile Leu
260 265 270
ggt ggg atc ccg cgc cgt gaa ttt act cgc gac agc atc gaa gag aaa 864
Gly Gly Ile Pro Arg Arg Glu Phe Thr Arg Asp Ser Ile Glu Glu Lys
275 280 285
gtc gct gct acc acg caa gca caa tgg ccg gtt cat gcg gtg atc acc 912
Val Ala Ala Thr Thr Gln Ala Gln Trp Pro Val His Ala Val Ile Thr
290 295 300
aac tcc acc tat gat ggc ttg ctc tac aac acc gac tgg atc aaa cag 960
Asn Ser Thr Tyr Asp Gly Leu Leu Tyr Asn Thr Asp Trp Ile Lys Gln
305 310 315 320
acg ctg gat gtc ccg tcg att cac ttc gat tct gcc tgg gtg ccg tac 1008
Thr Leu Asp Val Pro Ser Ile His Phe Asp Ser Ala Trp Val Pro Tyr
325 330 335
acc cat ttt cat ccg atc tac cag ggt aaa agt ggt atg agc ggc gag 1056
Thr His Phe His Pro Ile Tyr Gln Gly Lys Ser Gly Met Ser Gly Glu
340 345 350
cgt gtt gcg gga aaa gtg atc ttc gaa acg caa tcg acc cac aaa atg 1104
Arg Val Ala Gly Lys Val Ile Phe Glu Thr Gln Ser Thr His Lys Met
355 360 365
ctg gcg gcg tta tcg cag gct tcg ctg atc cac att aaa ggc gag tat 1152
Leu Ala Ala Leu Ser Gln Ala Ser Leu Ile His Ile Lys Gly Glu Tyr
370 375 380
gac gaa gag gcc ttt aac gaa gcc ttt atg atg cat acc acc acc tcg 1200
Asp Glu Glu Ala Phe Asn Glu Ala Phe Met Met His Thr Thr Thr Ser
385 390 395 400
ccc agt tat ccc att gtt gct tcg gtt gag acg gcg gcg gcg atg ctg 1248
Pro Ser Tyr Pro Ile Val Ala Ser Val Glu Thr Ala Ala Ala Met Leu
405 410 415
cgt ggt aat ccg ggc aaa cgg ctg att aac cgt tca gta gaa cga gct 1296
Arg Gly Asn Pro Gly Lys Arg Leu Ile Asn Arg Ser Val Glu Arg Ala
420 425 430
ctg cat ttt cgc aaa gag gtc cag cgg ctg cgg gaa gag tct gac ggt 1344
Leu His Phe Arg Lys Glu Val Gln Arg Leu Arg Glu Glu Ser Asp Gly
435 440 445
tgg ttt ttc gat atc tgg caa ccg ccg cag gtg gat gaa gcc gaa tgc 1392
Trp Phe Phe Asp Ile Trp Gln Pro Pro Gln Val Asp Glu Ala Glu Cys
450 455 460
tgg ccc gtt gcg cct ggc gaa cag tgg cac ggc ttt aac gat gcg gat 1440
Trp Pro Val Ala Pro Gly Glu Gln Trp His Gly Phe Asn Asp Ala Asp
465 470 475 480
gcc gat cat atg ttt ctc gat ccg gtt aaa gtc act att ttg aca ccg 1488
Ala Asp His Met Phe Leu Asp Pro Val Lys Val Thr Ile Leu Thr Pro
485 490 495
ggg atg gac gag cag ggc aat atg agc gag gag ggg atc ccg gcg gcg 1536
Gly Met Asp Glu Gln Gly Asn Met Ser Glu Glu Gly Ile Pro Ala Ala
500 505 510
ctg gta gca aaa ttc ctc gac gaa cgt ggg atc gta gta gag aaa acc 1584
Leu Val Ala Lys Phe Leu Asp Glu Arg Gly Ile Val Val Glu Lys Thr
515 520 525
ggc cct tat aac ctg ctg ttt ctc ttt agt att ggc atc gat aaa acc 1632
Gly Pro Tyr Asn Leu Leu Phe Leu Phe Ser Ile Gly Ile Asp Lys Thr
530 535 540
aaa gca atg gga tta ttg cgt ggg ttg acg gaa ttc aaa cgc tct tac 1680
Lys Ala Met Gly Leu Leu Arg Gly Leu Thr Glu Phe Lys Arg Ser Tyr
545 550 555 560
gat ctc aac ctg cgg atc aaa aat atg cta ccc gat ctc tat gca gaa 1728
Asp Leu Asn Leu Arg Ile Lys Asn Met Leu Pro Asp Leu Tyr Ala Glu
565 570 575
gat ccc gat ttc tac cgc aat atg cgt att cag gat ctg gca caa ggg 1776
Asp Pro Asp Phe Tyr Arg Asn Met Arg Ile Gln Asp Leu Ala Gln Gly
580 585 590
atc cat aag ctg att cgt aaa cac gat ctt ccc ggt ttg atg ttg cgg 1824
Ile His Lys Leu Ile Arg Lys His Asp Leu Pro Gly Leu Met Leu Arg
595 600 605
gca ttc gat act ttg ccg gag atg atc atg acg cca cat cag gca tgg 1872
Ala Phe Asp Thr Leu Pro Glu Met Ile Met Thr Pro His Gln Ala Trp
610 615 620
caa cga caa att aaa ggc gaa gta gaa acc att gcg ctg gaa caa ctg 1920
Gln Arg Gln Ile Lys Gly Glu Val Glu Thr Ile Ala Leu Glu Gln Leu
625 630 635 640
gtc ggt aga gta tcg gca aat atg atc ctg cct tat cca ccg ggc gta 1968
Val Gly Arg Val Ser Ala Asn Met Ile Leu Pro Tyr Pro Pro Gly Val
645 650 655
ccg ctg ttg atg cct gga gaa atg ctg acc aaa gag agc cgc aca gta 2016
Pro Leu Leu Met Pro Gly Glu Met Leu Thr Lys Glu Ser Arg Thr Val
660 665 670
ctc gat ttt cta ctg atg ctt tgt tcc gtc ggg caa cat tac ccc ggt 2064
Leu Asp Phe Leu Leu Met Leu Cys Ser Val Gly Gln His Tyr Pro Gly
675 680 685
ttt gaa acg gat att cac ggc gcg aaa cag gac gaa gac ggc gtt tac 2112
Phe Glu Thr Asp Ile His Gly Ala Lys Gln Asp Glu Asp Gly Val Tyr
690 695 700
cgc gta cga gtc cta aaa atg gcg gga taa 2142
Arg Val Arg Val Leu Lys Met Ala Gly
705 710
<210> 34
<211> 713
<212> PRT
<213> Escherichia coli
<400> 34
Met Asn Ile Ile Ala Ile Met Gly Pro His Gly Val Phe Tyr Lys Asp
1 5 10 15
Glu Pro Ile Lys Glu Leu Glu Ser Ala Leu Val Ala Gln Gly Phe Gln
20 25 30
Ile Ile Trp Pro Gln Asn Ser Val Asp Leu Leu Lys Phe Ile Glu His
35 40 45
Asn Pro Arg Ile Cys Gly Val Ile Phe Asp Trp Asp Glu Tyr Ser Leu
50 55 60
Asp Leu Cys Ser Asp Ile Asn Gln Leu Asn Glu Tyr Leu Pro Leu Tyr
65 70 75 80
Ala Phe Ile Asn Thr His Ser Thr Met Asp Val Ser Val Gln Asp Met
85 90 95
Arg Met Ala Leu Trp Phe Phe Glu Tyr Ala Leu Gly Gln Ala Glu Asp
100 105 110
Ile Ala Ile Arg Met Arg Gln Tyr Thr Asp Glu Tyr Leu Asp Asn Ile
115 120 125
Thr Pro Pro Phe Thr Lys Ala Leu Phe Thr Tyr Val Lys Glu Arg Lys
130 135 140
Tyr Thr Phe Cys Thr Pro Gly His Met Gly Gly Thr Ala Tyr Gln Lys
145 150 155 160
Ser Pro Val Gly Cys Leu Phe Tyr Asp Phe Phe Gly Gly Asn Thr Leu
165 170 175
Lys Ala Asp Val Ser Ile Ser Val Thr Glu Leu Gly Ser Leu Leu Asp
180 185 190
His Thr Gly Pro His Leu Glu Ala Glu Glu Tyr Ile Ala Arg Thr Phe
195 200 205
Gly Ala Glu Gln Ser Tyr Ile Val Thr Asn Gly Thr Ser Thr Ser Asn
210 215 220
Lys Ile Val Gly Met Tyr Ala Ala Pro Ser Gly Ser Thr Leu Leu Ile
225 230 235 240
Asp Arg Asn Cys His Lys Ser Leu Ala His Leu Leu Met Met Asn Asp
245 250 255
Val Val Pro Val Trp Leu Lys Pro Thr Arg Asn Ala Leu Gly Ile Leu
260 265 270
Gly Gly Ile Pro Arg Arg Glu Phe Thr Arg Asp Ser Ile Glu Glu Lys
275 280 285
Val Ala Ala Thr Thr Gln Ala Gln Trp Pro Val His Ala Val Ile Thr
290 295 300
Asn Ser Thr Tyr Asp Gly Leu Leu Tyr Asn Thr Asp Trp Ile Lys Gln
305 310 315 320
Thr Leu Asp Val Pro Ser Ile His Phe Asp Ser Ala Trp Val Pro Tyr
325 330 335
Thr His Phe His Pro Ile Tyr Gln Gly Lys Ser Gly Met Ser Gly Glu
340 345 350
Arg Val Ala Gly Lys Val Ile Phe Glu Thr Gln Ser Thr His Lys Met
355 360 365
Leu Ala Ala Leu Ser Gln Ala Ser Leu Ile His Ile Lys Gly Glu Tyr
370 375 380
Asp Glu Glu Ala Phe Asn Glu Ala Phe Met Met His Thr Thr Thr Ser
385 390 395 400
Pro Ser Tyr Pro Ile Val Ala Ser Val Glu Thr Ala Ala Ala Met Leu
405 410 415
Arg Gly Asn Pro Gly Lys Arg Leu Ile Asn Arg Ser Val Glu Arg Ala
420 425 430
Leu His Phe Arg Lys Glu Val Gln Arg Leu Arg Glu Glu Ser Asp Gly
435 440 445
Trp Phe Phe Asp Ile Trp Gln Pro Pro Gln Val Asp Glu Ala Glu Cys
450 455 460
Trp Pro Val Ala Pro Gly Glu Gln Trp His Gly Phe Asn Asp Ala Asp
465 470 475 480
Ala Asp His Met Phe Leu Asp Pro Val Lys Val Thr Ile Leu Thr Pro
485 490 495
Gly Met Asp Glu Gln Gly Asn Met Ser Glu Glu Gly Ile Pro Ala Ala
500 505 510
Leu Val Ala Lys Phe Leu Asp Glu Arg Gly Ile Val Val Glu Lys Thr
515 520 525
Gly Pro Tyr Asn Leu Leu Phe Leu Phe Ser Ile Gly Ile Asp Lys Thr
530 535 540
Lys Ala Met Gly Leu Leu Arg Gly Leu Thr Glu Phe Lys Arg Ser Tyr
545 550 555 560
Asp Leu Asn Leu Arg Ile Lys Asn Met Leu Pro Asp Leu Tyr Ala Glu
565 570 575
Asp Pro Asp Phe Tyr Arg Asn Met Arg Ile Gln Asp Leu Ala Gln Gly
580 585 590
Ile His Lys Leu Ile Arg Lys His Asp Leu Pro Gly Leu Met Leu Arg
595 600 605
Ala Phe Asp Thr Leu Pro Glu Met Ile Met Thr Pro His Gln Ala Trp
610 615 620
Gln Arg Gln Ile Lys Gly Glu Val Glu Thr Ile Ala Leu Glu Gln Leu
625 630 635 640
Val Gly Arg Val Ser Ala Asn Met Ile Leu Pro Tyr Pro Pro Gly Val
645 650 655
Pro Leu Leu Met Pro Gly Glu Met Leu Thr Lys Glu Ser Arg Thr Val
660 665 670
Leu Asp Phe Leu Leu Met Leu Cys Ser Val Gly Gln His Tyr Pro Gly
675 680 685
Phe Glu Thr Asp Ile His Gly Ala Lys Gln Asp Glu Asp Gly Val Tyr
690 695 700
Arg Val Arg Val Leu Lys Met Ala Gly
705 710
<210> 35
<211> 54
<212> DNA
<213> Artificial
<220>
<223> 5'-primer for cadA
<400> 35
tttgctttct tctttcaata ccttaacggt atagcgtgaa gcctgctttt ttat 54
<210> 36
<211> 54
<212> DNA
<213> Artificial
<220>
<223> 3'-primer for cadA
<400> 36
agatatgact atgaacgtta ttgcaatatt gaatcacgct caagttagta taaa 54
<210> 37
<211> 54
<212> DNA
<213> Artificial
<220>
<223> 5'-primer for ldc
<400> 37
ggaggaacac atgaacatca ttgccattat gggacctgaa gcctgctttt ttat 54
<210> 38
<211> 53
<212> DNA
<213> Artificial
<220>
<223> 3'-primer for ldc
<400> 38
cgccattttt aggactcgta cgcggtaaac gccgtccgtc aagttagtat aaa 53
Claims (13)
- EvgAS 2-성분 시스템 레귤론(regulon)에 관여하는 전사 인자를 암호화하는 evgA 유전자, gadE 유전자, ydeO 유전자 또는 이의 조합으로 이루어진 그룹으로부터 선택되는 유전자의 발현량이 증가되도록 변형되고 L-아미노산 생산 능력을 갖는 엔테로박테리아세애 과의 세균을 배지에서 배양하는 단계; 및 배지로부터 L-아미노산을 수거하는 단계를 포함하는, L-아미노산의 생산 방법.
- 제1항에 있어서, 하나 이상의 유전자의 발현이 유전자 각각의 카피수를 증가시키거나 당해 유전자의 발현 조절 서열을 변형시킴에 의해 증가된 방법.
- 제1항 또는 제2항에 있어서, 하나 이상의 유전자의 발현이 센서 키나제를 암호화하는 evgS 유전자의 발현이 증가되도록 세균을 변형시켜 증가된 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, evgA 유전자가(a) 서열번호 23의 뉴클레오타이드 서열을 포함하는 DNA 및(b) 서열번호 23의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있는, 전사 인자 활성을 갖는 단백질을 암호화하는 DNA로 이루어진 그룹으로부터 선택되는 DNA인 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, gadE 유전자가(c) 서열번호 27의 뉴클레오타이드 서열을 포함하는 DNA 및(d) 서열번호 27의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있는, 전사 인자 활성을 갖는 단백질을 암호화하는 DNA로 이루어진 그룹으로부터 선택되는 DNA인 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, ydeO 유전자가(e) 서열번호 29의 뉴클레오타이드 서열을 포함하는 DNA 및(f) 서열번호 29의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있는, 전사 인자 활성을 갖는 단백질을 암호화하는 DNA로 이루어진 그룹으로부터 선택되는 DNA인 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, evgS 유전자가(g) 서열번호 25의 뉴클레오타이드 서열을 포함하는 DNA 및(h) 서열번호 25의 뉴클레오타이드 서열과 상보적인 뉴클레오타이드 서열 또는 당해 뉴클레오타이드 서열로부터 제조될 수 있는 프로브와 엄중조건하에서 하이브리드화할 수 있는, 인 전달 활성을 갖는 단백질을 암호화하는 DNA로 이루어진 그룹으로부터 선택되는 DNA인 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, evgA 유전자가(A) 서열번호 24의 아미노산 서열을 포함하는 단백질 및(B) 하나 또는 여러 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 24의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질로 이루어진 그룹으로부터 선택되는 단백질을 암호화하는 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, gadE 유전자가(C) 서열번호 28의 아미노산 서열을 포함하는 단백질 및(D) 하나 또는 여러 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 28의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질로 이루어진 그룹으로부터 선택되는 단백질을 암호화하는 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, ydeO 유전자가(E) 서열번호 30의 아미노산 서열을 포함하는 단백질 및(F) 하나 또는 여러 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 30의 아미노산 서열을 포함하고 전사 인자 활성을 갖는 단백질로 이루어진 그룹으로부터 선택되는 단백질을 암호화하는 방법.
- 제1항 내지 제3항 중 어느 한 항에 있어서, evgS 유전자가(G) 서열번호 26의 아미노산 서열을 포함하는 단백질 및(H) 하나 또는 여러 아미노산 잔기의 치환, 결실, 삽입, 부가 또는 역위를 포함하는 서열번호 26의 아미노산 서열을 포함하고 인전달 활성을 갖는 단백질로 이루어진 그룹으로부터 선택되는 단백질을 암호화하는 방법.
- 제1항 내지 제11항 중 어느 한 항에 있어서, 세균이 엔테로박테리아세애(Enterobacteriaceae) 과에 속하고 에스케리치아(Escherichia), 엔테로박터(Enterobacter), 판토에아(Pantoea), 클렙시엘라(Klebsiella), 및 세라티아(Serratia) 속으로 이루어진 그룹으로부터 선택되는 방법.
- 제1항 내지 제12항 중 어느 한 항에 있어서, L-아미노산이 L-라이신, L-트레오닌, L-트립토판, 및 이의 조합으로 이루어진 그룹으로부터 선택되는 방법.
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| WO2010101359A2 (ko) * | 2009-03-03 | 2010-09-10 | 씨제이 제일제당(주) | Ｌ-아미노산 생산 미생물 및 이를 이용한 ｌ-아미노산 생산 방법 |
| WO2010101360A3 (ko) * | 2009-03-03 | 2010-12-09 | 씨제이 제일제당(주) | Ｌ-아미노산 생산 미생물 및 이를 이용한 ｌ-아미노산 생산 방법 |
| WO2010093182A3 (ko) * | 2009-02-13 | 2010-12-09 | 씨제이제일제당 주식회사 | Ｌ-아미노산 생산용 미생물 및 이를 이용하여 ｌ-아미노산을 생산하는 방법 |
| KR102287112B1 (ko) * | 2021-01-25 | 2021-08-06 | 씨제이제일제당 주식회사 | 신규한 쿠퍼익스포팅 P-type 에이티피에이즈 A 변이체 및 이를 이용한 L-트립토판 생산 방법 |
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| JP2010017081A (ja) | 2006-10-10 | 2010-01-28 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| KR101999454B1 (ko) | 2017-12-19 | 2019-07-11 | 씨제이제일제당 (주) | L-아르기닌을 생산하는 코리네박테리움 속 미생물 및 이를 이용한 l-아르기닌 생산방법 |
| CN111484963A (zh) | 2019-01-28 | 2020-08-04 | 味之素株式会社 | 用于生产l-氨基酸的方法 |
| KR102433234B1 (ko) | 2020-09-29 | 2022-08-18 | 대상 주식회사 | L-시트룰린 생산능이 향상된 코리네박테리움 글루타미쿰 변이주 및 이를 이용한 l-시트룰린의 생산 방법 |
| KR20220129797A (ko) | 2021-03-17 | 2022-09-26 | 대상 주식회사 | L-시트룰린 생산능이 향상된 코리네박테리움 글루타미쿰 변이주 및 이를 이용한 l-시트룰린의 생산 방법 |
| CN114585732A (zh) * | 2021-04-28 | 2022-06-03 | Cj第一制糖株式会社 | 新型异柠檬酸脱氢酶激酶/磷酸酶变体及使用其生产l-色氨酸的方法 |
| KR20230161245A (ko) | 2022-05-18 | 2023-11-27 | 씨제이제일제당 (주) | 글루코네이트 리프레서 단백질 활성이 약화된 미생물 및 이를 이용한 l-아르기닌 생산 방법 |
| KR20230161244A (ko) | 2022-05-18 | 2023-11-27 | 씨제이제일제당 (주) | 신규한 글루타메이트 글루코네이트 리프레서 변이체 및 이를 이용한 l-아르기닌 생산 방법 |
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| DE10116518A1 (de) * | 2001-04-03 | 2002-10-17 | Degussa | Verfahren zur fermentativen Herstellung von L-Aminosäuren unter Verwendung von Stämmen der Familie Enterobacteriaceae |
| EP1483392B1 (en) * | 2002-03-13 | 2010-12-01 | Evonik Degussa GmbH | Process for the preparation of l-amino acids using strains of the family enterobacteriaceae |
| EP1483394B1 (en) * | 2002-03-13 | 2009-04-15 | Evonik Degussa GmbH | Process for the preparation of l-amino acids using strains of the enterobacteriaceae family |
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| WO2010093182A3 (ko) * | 2009-02-13 | 2010-12-09 | 씨제이제일제당 주식회사 | Ｌ-아미노산 생산용 미생물 및 이를 이용하여 ｌ-아미노산을 생산하는 방법 |
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| WO2010101360A3 (ko) * | 2009-03-03 | 2010-12-09 | 씨제이 제일제당(주) | Ｌ-아미노산 생산 미생물 및 이를 이용한 ｌ-아미노산 생산 방법 |
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| CN102365363A (zh) * | 2009-03-03 | 2012-02-29 | Cj第一制糖株式会社 | 产生l-氨基酸的微生物和利用其生产l-氨基酸的方法 |
| US8623620B2 (en) | 2009-03-03 | 2014-01-07 | CJ Chieljedang Corporation | Microorganism which produces L-amino acid and method for producing L-amino acid using the same |
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| EP1928899B1 (en) | 2012-10-24 |
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