KR20150000773A - Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법 - Google Patents

Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법 Download PDF

Info

Publication number
KR20150000773A
KR20150000773A KR1020130073309A KR20130073309A KR20150000773A KR 20150000773 A KR20150000773 A KR 20150000773A KR 1020130073309 A KR1020130073309 A KR 1020130073309A KR 20130073309 A KR20130073309 A KR 20130073309A KR 20150000773 A KR20150000773 A KR 20150000773A
Authority
KR
South Korea
Prior art keywords
leu
ala
gly
glu
val
Prior art date
Application number
KR1020130073309A
Other languages
English (en)
Other versions
KR101594156B1 (ko
Inventor
박상희
문준옥
이광호
Original Assignee
씨제이제일제당 (주)
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority to KR1020130073309A priority Critical patent/KR101594156B1/ko
Application filed by 씨제이제일제당 (주) filed Critical 씨제이제일제당 (주)
Priority to EP14817261.2A priority patent/EP3015546B1/en
Priority to HUE14817261A priority patent/HUE050834T2/hu
Priority to JP2016523640A priority patent/JP6195668B2/ja
Priority to CN201910757268.2A priority patent/CN110423734B/zh
Priority to ES14817261T priority patent/ES2802949T3/es
Priority to BR112015032121-6A priority patent/BR112015032121B1/pt
Priority to CN201480036728.8A priority patent/CN105658793B/zh
Priority to PCT/KR2014/005576 priority patent/WO2014208981A1/ko
Priority to US14/392,186 priority patent/US9758771B2/en
Priority to PL14817261T priority patent/PL3015546T3/pl
Publication of KR20150000773A publication Critical patent/KR20150000773A/ko
Application granted granted Critical
Publication of KR101594156B1 publication Critical patent/KR101594156B1/ko

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
    • C12N9/1241—Nucleotidyltransferases (2.7.7)
    • C12N9/1247—DNA-directed RNA polymerase (2.7.7.6)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/52—Genes encoding for enzymes or proenzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
    • C12N15/77—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Corynebacterium; for Brevibacterium
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P13/00—Preparation of nitrogen-containing organic compounds
    • C12P13/04—Alpha- or beta- amino acids
    • C12P13/08—Lysine; Diaminopimelic acid; Threonine; Valine
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y207/00—Transferases transferring phosphorus-containing groups (2.7)
    • C12Y207/07—Nucleotidyltransferases (2.7.7)
    • C12Y207/07006—DNA-directed RNA polymerase (2.7.7.6)

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Biotechnology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
  • Microbiology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Physics & Mathematics (AREA)
  • Biophysics (AREA)
  • Plant Pathology (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

RNA 중합효소의 베타 프라임 서브유닛의 변이체, 이를 코딩하는 폴리뉴클레오티드를 포함하는 코리네박테리움 속 미생물 및 이를 배양하여 L-라이신을 생산하는 방법을 제공한다.

Description

Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 Ｌ-라이신을 생산하는 방법{A microorganism having enhanced L-lysine productivity and a method of producing L-lysine using the same}
본 발명은 L-라이신 생산능이 향상된 미생물 및 이를 배양하여 L-라이신을 생산하는 방법에 관한 것이다.
전 세계적으로 아미노산 등 유용 산물의 대량생산을 위해 미생물을 이용한 다양한 발효 방법이 이용되고 있으며, 특히 이러한 미생물을 이용한 성공적인 발효를 위해 균주개발, 발효조건 확립 등 다양한 기술들이 개발되어 오고 있다. 유용 산물의 대량생산을 위한 균주의 개발을 위해 해당 경로에 상위 단계에서 직간접적으로 관여하는 유전적 요인들을 찾아내어 적절히 이용한다면 좀 더 높은 효율의 균주를 개발할 수 있다. 대표적인 기술로는 RNA 폴리머라제의 recruiting 단백질에 무작위 돌연변이를 일으킴으로써 세포내 모든 유전자의 발현을 조절하는 gTME(global Transcription Machinery Engineering)가 있다.
미생물의 전사단계에서 쓰여지는 RNA 폴리머라제는 5개의 인자로 구성된 거대분자로 알파 2개, 베타, 베타프라임 및 시그마 인자로 구성되어 있으며 완전효소(holoenzyme)는 α2ββ'σ로 표시된다. 이들 중 핵심효소(core enzyme, α2ββ')는 개시 단계를 제외한 전사의 모든 단계에서 사용된다. 미생물에서 전사는 RNA 폴리머라제가 프로모터에 특이적으로 결합함으로써 시작되며, 완전효소는 RNA 합성개시점에서부터 업스트림으로 약 45 염기쌍, 다운스트림으로 10 염기쌍에 이르는 부위에서 DNA와 결합한다.
대장균의 RNA 폴리머라제 베타 프라임 서브 유닛은 A~H의 진화적으로 높은 보존 서열 부위를 가지고 있으며, 이 부위에 변이를 주어 RNA 폴리머라제의 여러 인자들의 결합을 약하게 하거나, 균주의 성장 온도 민감성을 높이는 등의 다양한 변화를 관찰한 연구들이 다수 보고되었다. 그러나, 코리네박테리움 속 균주의 gTME 기술 적용 및 변이에 의한 특성 변화에 관한 연구는 거의 진행되어있지 않았다.
코리네박테리움 속 균주의 RNA 폴리머라제의 구성 요소 중 베타와 베타프라임 인자를 암호화하는 유전자들 즉, rpoB와 rpoC 각각은 서로 오페론을 이루고 있으며 각각 3.5 kb, 4.0 kb의 뉴클레오타이드로 구성되어 있다.
본 발명자들은 상기 코리네박테리움 속 균주 유래의 rpoC에 무작위 변이를 도입하고, L-라이신 생산성 향상에 기여한 변이체를 스크리닝하였고, 대장균 유래의 rpoC의 G와 H 영역에 해당하는 부위에 변이가 도입되었을 경우 라이신 생산능이 크게 향상되는 것을 확인함으로써 본 발명을 완성하였다.
일 양상은 L-라이신의 생산을 증가시킬 수 있는 RNA 중합효소의 베타 프라임 서브유닛 변이체를 제공한다.
다른 양상은 L-라이신의 생산을 증가시킬 수 있는 RNA 중합효소의 베타 프라임 서브유닛 변이체를 코딩하는 뉴클레오티드 서열을 갖는 폴리뉴클레오티드를 제공한다.
다른 양상은 L-라이신의 생산을 증가시킬 수 있는 RNA 중합효소의 베타 프라임 서브유닛 변이체를 코딩하는 뉴클레오티드를 갖는 폴리뉴클레오티드를 포함하는 벡터를 제공한다.
다른 양상은 상기 베타 프라임 서브유닛 변이체를 포함하는 미생물을 제공한다.
다른 양상은 상기 미생물을 배양하여 L-라이신을 생산하는 방법을 제공한다.
일 양상은 서열번호 1의 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 아미노산 서열을 갖는 RNA 폴리머라제의 베타 프라임 서브 유닛(β'-subunit)을 제공한다.
베타 프라임 서브 유닛은 RpoC 아미노산일 수 있다. 상기 RpoC 아미노산은 보존 서열 영역(conserved region)을 포함할 수 있다. 상기 보존 영역은 진화적으로 높게 보존되는 영역일 수 있다. 상기 RpoC 아미노산은 복수의 도메인을 포함할 수 있다. 상기 복수의 도메인은 A 내지 H 도메인일 수 있다. 상기 베타 프라임 서브 유닛은 코리네박테리움 속 미생물로부터 유래할 수 있다. 상기 코리네박테리움 속 미생물 유래 베타 프라임 서브 유닛의 아미노산 서열은 서열번호 1, 또는 상기 서열번호 1에 대하여 약 70% 이상, 약 75% 이상, 약 80% 이상, 약 85%이상, 약 90% 이상, 약 92% 이상, 약 95% 이상, 약 97% 이상, 약 98% 이상, 또는 약 99% 이상의 서열 상동성을 가지는 것일 수 있다. 코리네박테리움 속 미생물 유래 베타 프라임 서브 유닛의 아미노산 서열, 즉 RpoC 아미노산 서열의 975 내지 1284번째 아미노산과 상동성 있는 서열은 대장균 유래 RpoC 아미노산 서열일 수 있다. 상기 대장균 유래 RpoC 아미노산 서열은 서열번호 4의 G 및 H 도메인일 수 있다.
상기 서열번호 1의 베타 프라임 서브 유닛의 G 도메인 및 H 도메인의 아미노산 서열 중 1 내지 5 개의 아미노산이 다른 아미노산으로 치환될 수 있다. 바람직하게는 상기 서열번호 1의 아미노산 서열에서 제975 내지 제1284 번째 아미노산 서열 중 1 내지 5개의 아미노산이 다른 아미노산으로 치환될 수 있다. 더욱 바람직하게는 상기 서열번호 1의 아미노산 서열에서 제1014 내지 제1034 번째 아미노산 또는 제1230 내지 제1255 번째 아미노산 중 1 내지 5개의 아미노산이 다른 아미노산으로 치환될 수 있다. 서열번호 8, 9, 11, 14, 15, 20, 23, 24, 또는 25는 상기 서열번호 1의 아미노산 서열에서 제1014 내지 제1034 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 아미노산 서열일 수 있다. 서열번호 10, 12, 13, 16, 17, 18, 19, 21, 22, 또는 27은 상기 서열번호 1의 아미노산 서열에서 제1230 내지 제1255 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 아미노산 서열일 수 있다. 서열번호 26은 상기 서열번호 1의 아미노산 서열에서 제1014 내지 제1034 중의 아미노산 및 제1230 내지 제1255 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 아미노산 서열일 수 있다.
일 구체예는 서열번호 1로 기재된 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 코딩하는 뉴클레오티드 서열을 갖는 폴리뉴클레오티드를 제공한다.
또 다른 양상은 상기 폴리뉴클레오티드를 포함하는 벡터를 제공한다. 상기 폴리뉴클레오티드는 조절 서열과 작동가능하게 연결될 수 있다. 상기 조절 서열은 프로모터, 터미네이터 또는 인핸서를 포함할 수 있다. 또한, 상기 프로모터는 유전자를 코딩하는 서열과 작동적으로 결합될 수 있다. 본 명세서에서 용어 "작동가능하게 연결된"은 핵산 발현 조절 서열과 다른 뉴클레오티드 서열 사이의 기능적인 결합을 의미할 수 있다. 이로 인해, 상기 조절 서열은 상기 유전자를 코딩하는 뉴클레오티드 서열의 전사 및/또는 번역을 조절할 수 있다.
다른 양상은 서열번호 1로 기재된 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 발현하는 미생물을 제공한다.
서열번호 1로 기재된 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 코딩하는 뉴클레오티드 서열을 갖는 폴리뉴클레오티드를 포함하는 미생물을 제공한다. 또한, 서열번호 1로 기재된 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 코딩하는 뉴클레오티드 서열을 갖는 폴리뉴클레오티드를 포함하는 벡터가 도입된 미생물을 제공한다. 상기 도입된 미생물은 형질전환된 미생물일 수 있다.
상기 유전자의 도입은 어떠한 형태, 예를 들면 발현 카세트(expression cassette)의 형태로의 도입, 상기 유전자 자체의 도입, 또는 폴리뉴클레오티드 구조체 형태로의 도입일 수 있다. 상기 발현 카세트는 상기 유전자가 자체적으로 발현되는데 필요한 모든 요소를 포함할 수 있다. 상기 발현 카세트는 폴리뉴클레오티드의 구조체일 수 있다. 상기 발현 카세트는 상기 유전자에 작동가능하게 연결된 프로모터, 전사 종결 신호, 리보좀 결합 부위 및 번역 종결신호를 포함할 수 있다. 상기 발현 카세트는 자체 복제가 가능한 발현 벡터 형태일 수 있다. 상기 유전자 자체의 도입 또는 폴리뉴클레오티드 구조체 형태로의 도입은 도입된 숙주세포에서 발현에 필요한 서열과 작동가능하게 연결되어 있는 것일 수 있다.
본 명세서에서 사용된 용어 "형질전환"은 유전자를 숙주세포 내에 도입하여 숙주세포 내에서 발현시킬 수 있도록 하는 것을 의미할 수 있다. 형질전환된 유전자는 숙주세포의 염색체 내에 삽입될 수 있거나/있고 상기 염색체 외에 위치할 수 있다. 상기 유전자는 폴리펩티드를 코딩할 수 있는 폴리뉴클레오티드일 수 있다. 상기 유전자는 DNA 또는 RNA를 포함한다.
상기 미생물은 코리네박테리움(Corynebacterium) 속 미생물일 수 있다. 상기 코리네박테리움 속 미생물은 예를 들면, 코리네박테리움 글루타미쿰, 코리네박테리움 이피시언스, 코리네박테리움 디프테리아, 또는 코리네박테리움 암모니아게네스를 포함할 수 있으며, 바람직하게 코리네박테리움 글루타미쿰(Corynebacterium glutamicum)일 수 있다. 구체적으로 실시하는 코리네박테리움 속 미생물은 수탁번호 KCCM11016P, KCCM11347P(KFCC10750의 국제기탁전환), KCCM10770, 또는 CJ3P인 코리네박테리움 글루타미쿰(Corynebacterium glutamicum)일 수 있다. 다른 양상은 서열번호 1로 기재된 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 발현하는 미생물을 배양하여 배양물 중에 L-라이신을 생산하는 단계; 및 배양물로부터 L-라이신을 회수하는 단계를 포함하는, L-라이신을 생산하는 방법을 제공한다. 상기 미생물에 대하여는 상기한 바와 같다.
상기 미생물의 배양은 당업계에 알려진 적당한 배지와 배양조건에 따라 이루어질 수 있다. 이러한 배양 과정은 선택되는 미생물에 따라 용이하게 조정하여 사용할 수 있다. 상기 배양의 방법은 회분식, 연속식, 및 유가식 배양으로 이루어진 군으로부터 선택되는 하나 이상의 배양을 포함할 수 있다.
상기 배양에 사용되는 배지는 특정한 미생물의 요구조건을 만족시킬 수 있는 배지일 수 있다. 상기 배지는 탄소원, 질소원, 미량원소 성분, 및 이들의 조합으로 이루어진 군으로부터 선택되는 배지일 수 있다.
상기 탄소원은 탄수화물, 지방, 지방산, 알코올, 유기산, 및 이들의 조합으로 이루어진 군으로부터 선택되는 탄소원일 수 있다. 상기 탄수화물은 포도당, 자당, 유당, 과당, 말토오스, 전분, 셀룰로오스, 및 이들의 조합일 수 있다. 상기 지방은 대두유, 해바라기유, 파자마유, 코코넛유, 및 이들의 조합일 수 있다. 상기 지방산은 팔미트산, 스테아린산, 리놀레산, 또는 이들의 조합일 수 있다. 상기 알코올은 글리세롤 또는 에탄올일 수 있다. 상기 유기산은 아세트산을 포함할 수 있다.
상기 질소원은 유기 질소원, 무기 질소원, 또는 이들의 조합을 포함할 수 있다. 상기 유기 질소원은 펩톤, 효모 추출물, 육즙, 맥아 추출물, 옥수수 침지액(CSL), 대두밀, 및 이들의 조합으로 이루어진 군으로부터 선택될 수 있다. 상기 무기 질소원은 요소, 황산암모늄, 염화암모늄, 인산암모늄, 탄산암모늄, 질산암모늄, 및 이들의 조합으로 이루어진 군으로부터 선택될 수 있다.
상기 배지는 인, 금속염, 아미노산, 비타민, 전구체 및 이들의 조합으로 이루어진 군으로부터 선택되는 것을 포함할 수 있다. 상기 인의 공급원은 인산이수소칼륨, 인산수소이칼륨, 또는 이들에 상응하는 소듐-함유염을 포함할 수 있다. 상기 금속염은 황산마그네슘 또는 황산철일 수 있다.
상기 배지 또는 이를 이루는 개별 성분은 회분식, 연속식, 또는 유가식 배양으로 첨가될 수 있다.
상기 배양 방법에 있어서, 배양물의 pH를 조정할 수 있다. 상기 pH의 조정은 상기 배양물에 수산화암모늄, 수산화칼륨, 암모니아, 인산, 또는 황산을 첨가하여 이루어질 수 있다. 또한, 상기 배양 방법은 기포 생성 억제를 포함할 수 있다. 상기 기포 생성 억제는 소포제의 사용을 통하여 이루어질 수 있다. 상기 소포제는 지방산 폴리글리콜 에스테르를 포함할 수 있다. 또한, 상기 배양 방법은 배양물 내로 기체의 주입을 포함할 수 있다. 상기 기체는 배양물의 호기 상태를 유지하기 위한 어떤 기체도 포함할 수 있다. 상기 기체는 산소 또는 산소 함유 기체일 수 있다. 상기 산소 함유 기체는 공기를 포함한다. 상기 배양에 있어서, 배양물의 온도는 20 내지 45℃, 예를 들면, 22 내지 42℃, 또는 25 내지 40℃일 수 있다. 배양기간은 원하는 L-라이신의 생성량을 획득할 때까지 지속될 수 있다.
상기 L-라이신을 생산하는 방법에 있어서, 상기 L-라이신은 L-라이신의 염을 포함할 수 있다.
일 양상에 따른 RNA 중합효소의 베타 프라임 서브유닛, 이를 코딩하는 폴리뉴클레오티드, 상기 폴리뉴클레오티드를 포함하는 벡터, 및 미생물을 이용하면 L-라이신의 생산을 증가시킬 수 있다.
일 양상에 따른 L-라이신을 생산하는 방법에 의하면 L-라이신의 생산을 증가시킬 수 있다.
도 1은 대장균 RpoC 아미노산의 보존 서열 구조 및 예측된 코리네 박테리움 RpoC 아미노산의 보존 서열 구조를 나타내는 도면이다.
도 2는 대장균 RpoC와 코리네 박테리움 RpoC의 G와 H 보존 부위의 예상 아미노산 서열을 비교한 도면이다.
이하 본 발명을 실시예를 통하여 보다 상세하게 설명한다. 그러나, 이들 실시예는 본 발명을 예시적으로 설명하기 위한 것으로 본 발명의 범위가 이들 실시예에 한정되는 것은 아니다.
실시예 1: 인공돌연변이법을 이용한 rpoC 변이체 라이브러리 제작
rpoC 유전자 변이체를 획득하기 위하여 아래의 방법으로 벡터 라이브러리를 제작하였다. 코리네박테리움 유래 rpoC 유전자(서열번호 5)의 업스트림 염기서열 (300 bp) 과 rpoC (4002 bp) 유전자를 포함하는 염기서열 (4302 bp)을 KCCM11016P(한국공개특허KR2007-0057093의 KFCC10881의 국제기탁전환) 의 염색체를 주형으로 하여 프라이머 서열번호 6 및 7을 에러-프론(Error-prone) PCR을 이용하여 증폭시켰다. 증폭된 유전자 내 변이가 kb 당 0-4.5개를 도입하기 위한 목적으로 GenemorphII Random Mutagenesis Kit (Stratagene)을 사용하였다. 500 ng의 KCCM11016P 균주의 염색체, 125 ng의 프라이머 1 및 2 각각, 1× Mutazyme II reaction 버퍼, 40 mM의 dNTPs(deoxyNucleotide-Triphosphates) mix, 2.5U의 Mutazyme II DNA 폴리머라제를 포함하는 50 uL의 반응액을 94˚C에서 2분간 변성 후, 94˚C 1분 변성, 56˚C 1분 어닐링, 72˚C 4분 중합을 25회 반복한 후, 72˚C에서 10분간 중합반응을 수행하였다.
증폭된 유전자 단편은 pTOPO TA Cloning Kit (Invitrogen)을 이용하여 pTOPO 벡터에 연결시켰다. 그 후, 상기 벡터를 대장균 DH5α에 형질전환하고 25 mg/l의 카나마이신이 포함된 LB 고체배지에 도말하였다. 형질전환된 콜로니 20종을 선별한 후 플라스미드를 획득하였고, 염기서열을 분석한 결과 0.5 돌연변이/kb 빈도로 서로 다른 위치에 변이가 도입되었음을 확인하였다. 약 10,000 개의 형질전환된 대장균 콜로니를 취하여 플라스미드를 추출하였고, 이를 pTOPO-rpoC(M) 라이브러리로 명명하였다. 대조군으로 사용하기 위한 rpoC 야생형의 유전자를 가진 pTOPO-rpoC(W) 플라스미드도 함께 제작하였다. 서열번호 6 및 7의 프라이머를 이용하여 KCCM11016P의 염색체를 주형으로 한 PCR을 통하여 rpoC 유전자 단편을 증폭한 후, 같은 방법으로 pTOPO-rpoC(W) 플라스미드를 제작하였다.
실시예 2: 라이신 생산능을 기반으로 rpoC 변이주 스크리닝
KCCM11016P 균주를 모균주로 하여 pTOPO-rpoC(M) 라이브러리를 형질전환하고 카나마이신 (25 mg/l)이 포함된 복합평판배지에 도말하여 약 21,500 개의 콜로니를 확보하였다.
<복합평판배지 (pH 7.0)>
포도당 10 g, 펩톤 10 g, 비프 추출물 5 g, 효모추출물 5 g, Brain Heart Infusion 18.5 g, NaCl 2.5 g, 요소 2 g, 소르비톨 91 g, 한천 20 g (증류수 1 리터 기준)
<종배지 (pH 7.0)>
포도당 20 g, 펩톤 10 g, 효모추출물 5 g, 요소 1.5 g, KH2PO4 4 g, K2HPO4 8g, MgSO4ㆍ7H2O 0.5 g, 바이오틴 100 ㎍, 티아민 HCl 1000 ㎍, 칼슘-판토텐산 2000 ㎍, 니코틴아미드 2000 ㎍ (증류수 1 리터 기준)
확보된 약 21,500개의 콜로니를 각각 300 uL의 선별배지에 접종하여 96 웰 플레이트에서 32˚C, 1000 rpm 으로 약 24시간 동안 배양하였다. 배양물에 생산된 L-라이신의 생산량을 분석하기 위하여 닌하이드린 방법을 이용하였다. 배양이 완료된 후 배양 상층액 10 ul 와 닌하드린 반응용액 190 ul를 65˚C에서 30분간 반응시킨 후 파장 570 nm에서 분광광도계로 흡광도를 측정하고 야생형 rpoC를 가진 대조군 KCCM11016P-rpoC(W)와 비교해 높은 흡광도를 보이는 변이 균주 약 2,000개의 콜로니를 선별하였다. 그 외 콜로니들은 대조군으로 이용된 KCCM11016P 혹은 KCCM11016P-rpoC(W) 균주와 유사한 흡광도를 보였다. 선별된 2000개의 균주는 같은 방법으로 닌하이드린 반응을 통하여 KCCM11016P-rpoC(W) 균주 대비 L-라이신 생산능이 향상된 균주로서 상위 183 종을 선별하였다.
<선별배지 (pH 8.0)>
포도당 10 g, 암모늄 설페이트 5.5 g, MgSO4ㆍ7H2O 1.2 g, KH2PO4 0.8 g, K2HPO4 16.4 g, 바이오틴 100 ㎍, 티아민 HCl 1000 ㎍, 칼슘-판토텐산 2000 ㎍, 니코틴아미드 2000 ㎍ (증류수 1 리터 기준)
실시예 3: rpoC 인공돌연변이 라이브러리 선별주의 유전자 변이 확인
실시예 2에서 선별된 균주들의 특성을 확인하기 위하여 염기서열을 분석하였다. 돌연변이를 탐색하기 위하여 KCCM11016P-rpoC(M)의 rpoC 염색체 부위의 염기서열을 결정하고, 미국 국립 보건원의 유전자 은행(NIH GenBank)을 근거로 하여 확인하였다.
도 1b는 대장균 RpoC 아미노산의 보존 서열 구조 및 예측된 코리네 박테리움 RpoC 아미노산의 보존 서열 구조를 나타내는 도면이다. 도 1b에 의하면, 선별된 변이형 rpoC의 염기서열 상동성 분석 결과, 183종의 91%에 해당하는 166종에서 상기 rpoC에 의해 암호화 되는 서열번호 1의 아미노산의 975 내지 1284번째 아미노산에 변이가 집중적으로 존재함을 확인하였다. 상기 166종 균주 중 약 70% 해당하는 116종에서는 1014 내지 1034번째 아미노산 및 1230 내지 1255번째 아미노산의 짧은 부위에 변이가 집중적으로 존재함을 확인하였다.
변이가 집중된 부위의 특성을 알아보기 위하여 코리네박테리움 RpoC와 기존에 활발히 연구된 대장균의 RNA 폴리머라제 베타프라임 인자의 아미노산과 서열 비교를 수행하였다. 도 2는 대장균 RpoC와 코리네 박테리움 RpoC의 G와 H 보존 부위의 예상 아미노산 서열을 비교한 도면이다. 도 2에 의하면, 대장균의 RNA 폴리머라제 베타 프라임 인자의 진화적으로 높은 보존 서열 부위로 알려진 8개의 도메인 중 G와 H 도메인 부위와 각각 68.4%, 77.8%의 상동성을 가짐을 확인하였다. 도 1은 대장균 RpoC 아미노산의 보존 서열 구조 및 예측된 코리네 박테리움 RpoC 아미노산의 보존 서열 구조를 나타내는 도면이다. 도 1에 의하면, 대장균의 RNA 폴리머라제 베타프라임, rpoC의 G 및 H 도메인과 높은 상동성을 보이는 코리네 박테리움 RpoC 아미노산의 975번째 아미노산부터 1284번째 아미노산까지의 부위에 변이가 집중되는 것을 확인하였다. 116종의 균주 중 닌하이드린 반응시 흡광도가 높았던 상위 20개의 균주를 KCCM11016P-rpoC(M1) ~ KCCM11016P-rpoC(M20)으로 명명하였다
실시예 4: KCCM11016P - rpoC (M)의 라이신 생산능 및 분석
실시예 3에서 선별한 20종의 균주 KCCM11016P-rpoC(M1) ~ KCCM11016P-rpoC(M20)의 특성을 알아보고자 아래와 같은 방법으로 배양하여 라이신 생산능을 비교하고 배양액 성분을 분석하였다.
종 배지 25 ㎖을 함유하는 250 ㎖ 코너-바플 플라스크에 각 균주들을 접종하고, 30 ℃에서 20 시간 동안, 200 rpm으로 진탕 배양하였다. 그런 다음, 생산 배지 24 ㎖을 함유하는 250 ㎖ 코너-바플 플라스크에 1 ㎖의 종 배양액을 접종하고 30 ℃에서 72시간 동안, 200 rpm에서 진탕 배양하였다.　 상기 종 배지와 생산 배지의 조성은 각각 하기와 같다.
<종배지 (pH 7.0)>
포도당 20 g, 펩톤 10 g, 효모추출물 5 g, 요소 1.5 g, KH2PO4 4 g, K2HPO4 8 g, MgSO4ㆍ7H2O 0.5 g, 바이오틴 100 ㎍, 티아민 HCl 1000 ㎍, 칼슘-판토텐산 2000 ㎍, 니코틴아미드 2000 ㎍ (증류수 1 리터 기준)
<생산배지 (pH 7.0)>
포도당 100 g, (NH4)2SO4 40 g, 대두 단백질 2.5 g, 옥수수 침지 고형분(Corn Steep Solids) 5 g, 요소 3 g, KH2PO4 1 g, MgSO4ㆍH2O 0.5 g, 바이오틴 100 ㎍, 티아민 염산염 1000 ㎍, 칼슘-판토텐산 2000 ㎍, 니코틴아미드 3000 ㎍, CaCO3 30 g (증류수 1리터 기준).
HPLC를 이용하여 분석한 L-라이신의 농도를 표 1에 나타냈다.
KCCM11016P-rpoC(M)의 L-라이신 생산 농도
균주 L-라이신(g/l)
배치 1 배치 2 배치 3 평균
대조군 KCCM11016P-rpoC(W) 43.2 44.1 43.2 42.8
1 KCCM11016P-rpoC(M1) 46.1 46.5 47.1 43.6
2 KCCM11016P-rpoC(M2) 47.7 46.3 46.8 46.9
3 KCCM11016P-rpoC(M3) 48.2 48.6 48.4 48.4
4 KCCM11016P-rpoC(M4) 49 48.9 48.9 48.9
5 KCCM11016P-rpoC(M5) 48.3 49.8 49.5 49.2
6 KCCM11016P-rpoC(M6) 46.2 46.9 46.7 46.6
7 KCCM11016P-rpoC(M7) 45.3 45.8 45.9 45.7
8 KCCM11016P-rpoC(M8) 46.1 46.5 45.1 45.9
9 KCCM11016P-rpoC(M9) 47.3 47.9 47.9 47.7
10 KCCM11016P-rpoC(M10) 48.3 48.5 47.9 48.2
11 KCCM11016P-rpoC(M11) 45.3 45.8 45.9 45.7
12 KCCM11016P-rpoC(M12) 48.6 48.3 48.3 48.4
13 KCCM11016P-rpoC(M13) 46.6 47 47.1 46.9
14 KCCM11016P-rpoC(M14) 47.3 48.6 48 48.0
15 KCCM11016P-rpoC(M15) 49.2 49.2 49.4 49.3
16 KCCM11016P-rpoC(M16) 46.2 46.5 46 46.2
17 KCCM11016P-rpoC(M17) 46.3 45.2 45.8 45.8
18 KCCM11016P-rpoC(M18) 48.3 48.2 48.3 48.3
19 KCCM11016P-rpoC(M19) 47.3 47.8 47.5 47.5
20 KCCM11016P-rpoC(M20) 48.3 48.7 48.5 48.5
표 1에 나타난 바와 같이, L-라이신 생산 균주 KCCM11016P-rpoC(W)에 비하여 KCCM11016P-rpoC(M)는 L-라이신의 평균 농도가 13%까지 증가함을 확인하였다. 서열번호 8 내지 27에 rpoC 변이주 20종의 아미노산 서열 변화를 나타내었다. 상기 20종의 아미노산 서열을 분석한 결과 RNA 폴리머라제 베타프라임의 대장균의 rpoC의 G 및 H 도메인과 높은 상동성을 보이는 975번째 아미노산부터 1284번째 아미노산까지의 부위에 변이가 도입되었을 경우 라이신 생산능이 크게 향상됨을 확인하였다.
KCCM11016P-rpoC(M1)~(M20)의 rpoC 아미노산 변이
균주 rpoC 아미노산 변이
KCCM11016P-rpoC(M1) Q1016G
KCCM11016P-rpoC(M2) T1029H
KCCM11016P-rpoC(M3) F1247K
KCCM11016P-rpoC(M4) W24G, G995E, I1018C
KCCM11016P-rpoC(M5) G995H, I1231C
KCCM11016P-rpoC(M6) R1252T
KCCM11016P-rpoC(M7) G1022R
KCCM11016P-rpoC(M8) A1015D
KCCM11016P-rpoC(M9) A1237P
KCCM11016P-rpoC(M10) W1241N
KCCM11016P-rpoC(M11) Y36F, T1255C
KCCM11016P-rpoC(M12) E1249Y, G1282F
KCCM11016P-rpoC(M13) G1022S
KCCM11016P-rpoC(M14) S1243G
KCCM11016P-rpoC(M15) E1239T
KCCM11016P-rpoC(M16) G1034K, D1038H
KCCM11016P-rpoC(M17) L340E, A1014D
KCCM11016P-rpoC(M18) A1015H
KCCM11016P-rpoC(M19) S1017R, L1236T
KCCM11016P-rpoC(M20) G1230Y, N1260H
실시예 5: 고농도 L-라이신 생산주의 rpoC 상기 변이의 염색체 도입용 벡터 제작
염기서열이 치환된 rpoC 변이 균주의 실시예 2에서 확인한 변이 중 대장균 rpoC의 G 및 H 도메인과 높은 상동성을 보이는 영역의 변이 효과를 확인하기 위하여 이를 염색체상에 도입할 수 있는 벡터를 제작하였다.
보고된 염기서열에 근거하여 5' 말단에 EcoRⅠ 제한효소 부위를 삽입한 서열번호 29 및 29의 프라이머, 및 3' 말단에 SalⅠ 제한효소 부위를 삽입한 서열번호 30의 프라이머를 합성하였다. 이 중 서열번호 28 및 30의 프라이머를 이용하여, KCCM11016P-rpoC의 M1, M2, M4, M7, M8, M13, M16, M17, M18, 및 M19, 즉 10종의 염색체를 주형으로 한 PCR을 통하여 약 2000 bp의 rpoC(mt) 10종의 유전자 단편을 증폭하였다. PCR 조건은 94 ℃에서 5분간 변성 후, 94 ℃ 30초 변성, 56 ℃ 30초 어닐링, 72 ℃ 2분 중합을 30회 반복한 후, 72 ℃에서 7분간 중합반응을 수행하였다. 또한 서열번호 29 및 30인 프라이머를 이용하여 KCCM11016P-rpoC의 M3, M5, M6, M9, M10, M11, M12, M14, M15, 및 M20, 즉 10종의 염색체를 주형으로 한 PCR을 통하여 약 600 bp의 10종의 rpoC(mt) 유전자 단편을 증폭하였다. 이에 사용한 프라이머는 서열번호 28 내지 30에 나타냈다.
PCR로 증폭된 20종의 유전자 단편을 제한효소 EcoRⅠ과 SalⅠ으로 처리하여 각각의 DNA 절편을 획득한 후, 이를 제한효소 EcoRⅠ 및 SalⅠ말단을 가지는 염색체 도입용 pDZ 벡터(대한민국 특허 제2009-0094433호)에 연결한 후 대장균 DH5α에 형질전환하고 카나마이신(25 mg/l)이 포함된 LB 고체배지에 도말하였다. PCR을 통해 목적한 유전자가 삽입된 벡터로 형질전환된 콜로니를 선별한 후 통상적으로 알려진 플라스미드 추출법을 이용하여 플라스미드를 획득하였고 이 플라스미드를 주형으로 사용된 균주의 번호에 따라 각각 pDZ-rpoC(M1)~(M20)이라 명명하였다.
실시예 6: 고농도 L-라이신 생산주의 KCCM11016P 유래 rpoC 상기 변이의 염색체 도입균주의 제작 및 라이신 생산능 비교
실시예 5에서 제조한 벡터 pDZ-rpoC(M1)~(M20)를 상동염색체 재조합에 의해 L-라이신 생산균주인 코리네박테리움 글루타미쿰 KCCM11016P에 형질전환시켰다. 그 후 염색체 상의 rpoC 변이가 도입된 균주를 염기서열 분석에 의하여 선별하고, 실시예 3과 동일한 방법으로 배양하였다. 이로부터 L-라이신의 농도를 분석하고, 그 결과를 표 3에 나타내었다. 상기 rpoC 변이가 도입된 균주를 코리네박테리움 글루타미쿰 KCCM11016P::rpoC(M1) ~ (M20)라고 명명하였다.
　 균주 L-라이신(g/l)
　 　 배치 1 배치 2 배치 3 평균
대조군 KCCM11016P 42.2 43.4 42.7 42.8
1 KCCM11016P::rpoC(M1) 45.2 45.2 44.9 45.1
2 KCCM11016P::rpoC(M2) 46.2 45.8 46.5 46.2
3 KCCM11016P::rpoC(M3) 47 47.9 47.5 47.5
4 KCCM11016P::rpoC(M4) 47.6 47.2 47.8 47.5
5 KCCM11016P::rpoC(M5) 48.3 49.8 49.5 49.2
6 KCCM11016P::rpoC(M6) 46.3 46.5 46 46.3
7 KCCM11016P::rpoC(M7) 45.8 44.7 45.2 45.2
8 KCCM11016P::rpoC(M8) 46.1 46.5 45.1 45.9
9 KCCM11016P::rpoC(M9) 45.9 46.8 47.1 46.6
10 KCCM11016P::rpoC(M10) 47.2 47.6 47.4 47.4
11 KCCM11016P::rpoC(M11) 45.3 45.8 45.9 45.7
12 KCCM11016P::rpoC(M12) 47.8 47.8 48.2 47.9
13 KCCM11016P::rpoC(M13) 46.3 46 46.6 46.3
14 KCCM11016P::rpoC(M14) 47.2 46.9 46.7 46.9
15 KCCM11016P::rpoC(M15) 50.1 48.7 49.2 49.3
16 KCCM11016P::rpoC(M16) 46.2 45.9 45.8 46
17 KCCM11016P::rpoC(M17) 45.3 45.8 45.9 45.7
18 KCCM11016P::rpoC(M18) 47.8 47.6 47.2 47.5
19 KCCM11016P::rpoC(M19) 46.8 46.3 45.9 46.3
20 KCCM11016P::rpoC(M20) 47.6 47.3 47.8 47.6
표 3에서 확인된 바와 같이, 야생형 rpoC 유전자를 갖는 대조군 KCCM11016P에 비하여, 1개 또는 2개의 염기치환 변이를 가지는 rpoC 유전자가 도입된 KCCM11016P::rpoC(M1) ~ (M20)의 경우, L-라이신의 평균농도가 무려 약 6 ~15%가 증가함을 확인하였고, 이들 중 상위 20% 대표균주로서 KCCM11016P::rpoC(M15), 상위 40% 대표균주로서 KCCM11016P::rpoC(M10), 상위 60% 대표균주로서 KCCM11016P::rpoC(M19)를 각각 CA01-2267, CA01-2268, 및 CA01-2266 2013년 6월 12일에 한국미생물 보존센터 (KCCM)에 기탁하고, 각각 수탁번호 제KCCM11428P호, KCCM11429P호, 및 KCCM11427P호를 부여받았다.
실시예 7: 고농도 L-라이신 생산주의 KCCM11347P 유래 rpoC 상기 변이의 염색체 도입균주의 제작 및 라이신 생산능 비교
코리네박테리움 글루타미쿰에 속하는 다른 균주에서의 효과도 확인하기 위해 실시예 6과 같은 방법으로 L-라이신 생산균주인 코리네박테리움 글루타미쿰 KCCM11347P (대한민국 등록특허 제 1994-0001307호, KFCC10750의 국제기탁전환 미생물)에 rpoC 변이가 도입된 균주를 제작하고 KCCM11347P::rpoC(M1) ~ (M20)라고 명명하였다. 실시예 3과 동일한 방법으로 배양하여, 이로부터 L-라이신의 농도를 분석하여 그 결과를 표 4에 나타내었다.
KFCC10750::rpoC(M1) ~ (M20) 의 L-라이신 생산 농도
　 균주 L-라이신(g/l)
　 　 배치 1 배치 2 배치 3 평균
대조군 KCCM11347P 38.3 38 38.5 38.3
1 KCCM11347P::rpoC(M1) 41.2 41.3 41.8 41.6
2 KCCM11347P::rpoC(M2) 42.8 42.2 42.7 42.5
3 KCCM11347P::rpoC(M3) 42.7 43.7 43.8 43.8
4 KCCM11347P::rpoC(M4) 43.6 45.5 41.9 43.7
5 KCCM11347P::rpoC(M5) 44.2 44.8 44.6 44.5
6 KCCM11347P::rpoC(M6) 42.3 42 42.8 42.4
7 KCCM11347P::rpoC(M7) 42.1 42.3 42 42.2
8 KCCM11347P::rpoC(M8) 42.2 42.6 42.8 42.5
9 KCCM11347P::rpoC(M9) 41.8 42.9 43 43
10 KCCM11347P::rpoC(M10) 43.7 43 42.8 43.2
11 KCCM11347P::rpoC(M11) 42.2 42.7 41.8 42.3
12 KCCM11347P::rpoC(M12) 43.8 43.9 44 43.9
13 KCCM11347P::rpoC(M13) 43.3 43.3 41.3 42.6
14 KCCM11347P::rpoC(M14) 42.4 42.2 43.8 43
15 KCCM11347P::rpoC(M15) 44 44.8 44.2 44.5
16 KCCM11347P::rpoC(M16) 43 42.8 42.3 42.6
17 KCCM11347P::rpoC(M17) 40.8 43.3 41.8 42.6
18 KCCM11347P::rpoC(M18) 43 42.7 43.5 43.1
19 KCCM11347P::rpoC(M19) 42.8 42.7 43 42.8
20 KCCM11347P::rpoC(M20) 44.1 44.4 44.4 44.3
표 4에서 확인된 바와 같이, 야생형 rpoC 유전자를 갖는 대조군 KCCM11347P 에 비하여, 1개 또는 2개의 염기치환 변이를 가지는 rpoC 유전자가 도입된 KCCM11347P::rpoC(M1) ~ (M20)의 경우, 즉, 실험군 1 ~ 20의 경우, L-라이신의 평균농도가 약 8 ~16 %가 증가함을 확인하였다.
실시예 8: 고농도 L-라이신 생산주의 KCCM10770P 유래 rpoC 상기 변이의 염색체 도입균주의 제작 및 라이신 생산능 비교
코리네박테리움 글루타미쿰에 속하는 다른 균주들에서의 효과도 확인하기 위해 실시예 6과 같은 방법으로 L-라이신 생산균주인 코리네박테리움 글루타미쿰 KCCM10770P(대한민국 등록특허 제 0924065호)에 rpoC 변이가 도입된 균주를 제작하고 KCCM10770P::rpoC(M1) ~ (M20)라고 명명하였다. 상기 KCCM10770P 균주는 라이신 생합성경로 구성 유전자들 중　aspB (아스파테이트 아미노트란스퍼라제를 코딩하는 유전자), lysC (아스파테이트 키나제를 코딩하는 유전자), asd (아스파테이트 세미알데히드 디히드로게나제를 코딩하는 유전자), dapA (디히드로디피콜리네이트 신타제를 코딩하는 유전자), dapB (디히드로디피콜리네이트 리덕타제를 코딩하는 유전자) 및 lysA (디아미노디피멜레이트 디카르복실라제를 코딩하는 유전자), 즉, 6종의 유전자를 염색체 상에　1 카피 이상씩 보유한 KCCM11016P 유래의 L-라이신 생산균주이다. 실시예 3과 동일한 방법으로 배양하여, 이로부터 L-라이신의 농도를 분석하고, 그 결과를 표 5에 나타내었다.
KCCM10770P::rpoC(M1) ~ (M20) 의 L-라이신 생산 농도
　 균주 L-라이신(g/l)
　 　 배치 1 배치 2 배치 3 평균
대조군 KCCM10770P 47.8 47.2 47.5 47.5
1 KCCM10770P::rpoC(M1) 50.2 50 48.9 49.7
2 KCCM10770P::rpoC(M2) 50.2 50.8 50.9 50.6
3 KCCM10770P::rpoC(M3) 51.8 51.8 51.2 51.6
4 KCCM10770P::rpoC(M4) 51.8 51.6 51.2 51.5
5 KCCM10770P::rpoC(M5) 52 52.3 52.6 52.3
6 KCCM10770P::rpoC(M6) 50.7 50.4 50.4 50.5
7 KCCM10770P::rpoC(M7) 49.2 49.8 49.5 49.5
8 KCCM10770P::rpoC(M8) 50.2 50.4 50.7 50.4
9 KCCM10770P::rpoC(M9) 51.4 51 51.4 51.3
10 KCCM10770P::rpoC(M10) 51.6 51.3 50.9 51.3
11 KCCM10770P::rpoC(M11) 49.2 49 48 48.7
12 KCCM10770P::rpoC(M12) 52 51.8 52.1 52
13 KCCM10770P::rpoC(M13) 51.2 51.8 51 51.3
14 KCCM10770P::rpoC(M14) 52.2 49.9 51.8 51.3
15 KCCM10770P::rpoC(M15) 52.6 51.8 52.3 52.2
16 KCCM10770P::rpoC(M16) 50.2 50.6 50.4 50.4
17 KCCM10770P::rpoC(M17) 49.8 49.8 49.7 49.8
18 KCCM10770P::rpoC(M18) 51 51.2 52.1 51.4
19 KCCM10770P::rpoC(M19) 50.2 51.6 50.8 50.9
20 KCCM10770P::rpoC(M20) 51.8 51.8 51.8 51.8
표 5에서 확인된 바와 같이, 야생형 rpoC 유전자를 갖는 대조군 KCCM10770P에 비하여, 1개 또는 2개의 염기치환 변이를 가지는 rpoC 유전자가 도입된 KCCM10770P::rpoC(M1) ~ (M20)의 경우, 즉, 실험군 1 ~ 20의 경우, L-라이신의 평균농도가 약 3~10 %가 증가함을 확인하였다.
실시예 9: 고농도 L-라이신 생산주의 CJ3P 유래 rpoC 상기 변이의 염색체 도입균주의 제작 및 라이신 생산능 비교
코리네박테리움 글루타미쿰에 속하는 다른 균주들에서의 효과도 확인하기 위해 실시예 6와 같은 방법으로 L-라이신 생산균주인 코리네박테리움 글루타미쿰 CJ3P(Binder et al. Genome Biology 2012, 13:R40)에 rpoC 변이가 도입된 균주를 제작하고 CJ3P::rpoC(M1) ~ (M20)라고 명명하였다. CJ3P 균주는 공지된 기술을 바탕으로　야생주에 3종의 변이(pyc(Pro458Ser), hom(Val59Ala), lysC(Thr311Ile))를 도입하여 L-라이신 생산능을 갖게된 코리네박테리움 글루타미쿰 균주이다. 실시예 3과 동일한 방법으로 배양하여, 이로부터 L-라이신의 농도를 분석하고, 그 결과를 표 6에 나타내었다.
CJ3P::rpoC(M1) ~ (M20) 의 L-라이신 생산 농도
　 균주 L-라이신(g/l)
　 　 배치 1 배치 2 배치 3 평균
대조군 CJ3P 8.3 8 8.4 8.2
1 CJ3P::rpoC(M1) 8.9 9.1 9.3 9.1
2 CJ3P::rpoC(M2) 10.8 10.1 9.7 10.2
3 CJ3P::rpoC(M3) 11.9 11.7 11.2 11.6
4 CJ3P::rpoC(M4) 11.8 11.9 11 11.6
5 CJ3P::rpoC(M5) 11.8 11.7 12 11.8
6 CJ3P::rpoC(M6) 10.2 10 10.3 10.2
7 CJ3P::rpoC(M7) 8.9 8.7 9.1 8.9
8 CJ3P::rpoC(M8) 9.7 9.7 9.8 9.7
9 CJ3P::rpoC(M9) 11.2 11.3 11.1 11.2
10 CJ3P::rpoC(M10) 11.2 10.9 10.8 11
11 CJ3P::rpoC(M11) 9.2 9.5 8.7 9.1
12 CJ3P::rpoC(M12) 12.9 13 12.7 12.9
13 CJ3P::rpoC(M13) 10.8 10.3 10.3 10.5
14 CJ3P::rpoC(M14) 10.7 10.5 11 10.7
15 CJ3P::rpoC(M15) 12.4 12.2 12.3 12.3
16 CJ3P::rpoC(M16) 9.6 9.9 9.7 9.7
17 CJ3P::rpoC(M17) 8.9 9.8 9.4 9.4
18 CJ3P::rpoC(M18) 10.9 10.9 10.7 10.8
19 CJ3P::rpoC(M19) 10.3 10.3 10.5 10.4
20 CJ3P::rpoC(M20) 11.2 12 11.8 11.7
표 6에서 확인된 바와 같이, 야생형 rpoC 유전자를 갖는 대조군 CJ3P에 비하여, 1개 또는 2개의 염기치환 변이를 가지는 rpoC 유전자가 도입된 CJ3P::rpoC (M1) ~ (M20)의 경우, 즉, 실험군 1 ~ 20의 경우, L-라이신의 평균농도가 최대 57% 증가함을 확인하였다. 따라서, RNA 폴리머라제 베타프라임의 대장균의 rpoC의 G 및 H 도메인과 높은 상동성을 보이는 975번째 아미노산부터 1284번째 아미노산까지의 부위에 변이를 도입할 경우, 라이신 생산량을 대폭 증가시킬 수 있었다.
한국미생물보존센터(국외) KCCM11427P 20130612 한국미생물보존센터(국외) KCCM11428P 20130612 한국미생물보존센터(국외) KCCM11429P 20130612 한국미생물보존센터(국외) KCCM11016P 19951218 한국미생물보존센터(국외) KCCM11347P 19911210
<110> CJ Corporation <120> A microorganism having enhanced L-lysine productivity and a method of producing L-lysine using the same <130> PN099342 <160> 30 <170> KopatentIn 2.0 <210> 1 <211> 1333 <212> PRT <213> Corynebacterium <400> 1 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 2 <211> 60 <212> PRT <213> G domain of Corynebacterium <400> 2 Val Lys Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys 1 5 10 15 Ala Lys Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile 20 25 30 Gly Glu Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly 35 40 45 Thr Gln Leu Thr Met Arg Thr Phe His Gln Gly Gly 50 55 60 <210> 3 <211> 55 <212> PRT <213> H domain of Corynebacterium <400> 3 Gly Ile Thr Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala 1 5 10 15 Ser Phe Gln Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys 20 25 30 Arg Ser Asp Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys 35 40 45 Leu Ile Pro Ala Gly Thr Gly 50 55 <210> 4 <211> 1407 <212> PRT <213> E.coli <400> 4 Met Lys Asp Leu Leu Lys Phe Leu Lys Ala Gln Thr Lys Thr Glu Glu 1 5 10 15 Phe Asp Ala Ile Lys Ile Ala Leu Ala Ser Pro Asp Met Ile Arg Ser 20 25 30 Trp Ser Phe Gly Glu Val Lys Lys Pro Glu Thr Ile Asn Tyr Arg Thr 35 40 45 Phe Lys Pro Glu Arg Asp Gly Leu Phe Cys Ala Arg Ile Phe Gly Pro 50 55 60 Val Lys Asp Tyr Glu Cys Leu Cys Gly Lys Tyr Lys Arg Leu Lys His 65 70 75 80 Arg Gly Val Ile Cys Glu Lys Cys Gly Val Glu Val Thr Gln Thr Lys 85 90 95 Val Arg Arg Glu Arg Met Gly His Ile Glu Leu Ala Ser Pro Thr Ala 100 105 110 His Ile Trp Phe Leu Lys Ser Leu Pro Ser Arg Ile Gly Leu Leu Leu 115 120 125 Asp Met Pro Leu Arg Asp Ile Glu Arg Val Leu Tyr Phe Glu Ser Tyr 130 135 140 Val Val Ile Glu Gly Gly Met Thr Asn Leu Glu Arg Gln Gln Ile Leu 145 150 155 160 Thr Glu Glu Gln Tyr Leu Asp Ala Leu Glu Glu Phe Gly Asp Glu Phe 165 170 175 Asp Ala Lys Met Gly Ala Glu Ala Ile Gln Ala Leu Leu Lys Ser Met 180 185 190 Asp Leu Glu Gln Glu Cys Glu Gln Leu Arg Glu Glu Leu Asn Glu Thr 195 200 205 Asn Ser Glu Thr Lys Arg Lys Lys Leu Thr Lys Arg Ile Lys Leu Leu 210 215 220 Glu Ala Phe Val Gln Ser Gly Asn Lys Pro Glu Trp Met Ile Leu Thr 225 230 235 240 Val Leu Pro Val Leu Pro Pro Asp Leu Arg Pro Leu Val Pro Leu Asp 245 250 255 Gly Gly Arg Phe Ala Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val 260 265 270 Ile Asn Arg Asn Asn Arg Leu Lys Arg Leu Leu Asp Leu Ala Ala Pro 275 280 285 Asp Ile Ile Val Arg Asn Glu Lys Arg Met Leu Gln Glu Ala Val Asp 290 295 300 Ala Leu Leu Asp Asn Gly Arg Arg Gly Arg Ala Ile Thr Gly Ser Asn 305 310 315 320 Lys Arg Pro Leu Lys Ser Leu Ala Asp Met Ile Lys Gly Lys Gln Gly 325 330 335 Arg Phe Arg Gln Asn Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg 340 345 350 Ser Val Ile Thr Val Gly Pro Tyr Leu Arg Leu His Gln Cys Gly Leu 355 360 365 Pro Lys Lys Met Ala Leu Glu Leu Phe Lys Pro Phe Ile Tyr Gly Lys 370 375 380 Leu Glu Leu Arg Gly Leu Ala Thr Thr Ile Lys Ala Ala Lys Lys Met 385 390 395 400 Val Glu Arg Glu Glu Ala Val Val Trp Asp Ile Leu Asp Glu Val Ile 405 410 415 Arg Glu His Pro Val Leu Leu Asn Arg Ala Pro Thr Leu His Arg Leu 420 425 430 Gly Ile Gln Ala Phe Glu Pro Val Leu Ile Glu Gly Lys Ala Ile Gln 435 440 445 Leu His Pro Leu Val Cys Ala Ala Tyr Asn Ala Asp Phe Asp Gly Asp 450 455 460 Gln Met Ala Val His Val Pro Leu Thr Leu Glu Ala Gln Leu Glu Ala 465 470 475 480 Arg Ala Leu Met Met Ser Thr Asn Asn Ile Leu Ser Pro Ala Asn Gly 485 490 495 Glu Pro Ile Ile Val Pro Ser Gln Asp Val Val Leu Gly Leu Tyr Tyr 500 505 510 Met Thr Arg Asp Cys Val Asn Ala Lys Gly Glu Gly Met Val Leu Thr 515 520 525 Gly Pro Lys Glu Ala Glu Arg Leu Tyr Arg Ser Gly Leu Ala Ser Leu 530 535 540 His Ala Arg Val Lys Val Arg Ile Thr Glu Tyr Glu Lys Asp Ala Asn 545 550 555 560 Gly Glu Leu Val Ala Lys Thr Ser Leu Lys Asp Thr Thr Val Gly Arg 565 570 575 Ala Ile Leu Trp Met Ile Val Pro Lys Gly Leu Pro Tyr Ser Ile Val 580 585 590 Asn Gln Ala Leu Gly Lys Lys Ala Ile Ser Lys Met Leu Asn Thr Cys 595 600 605 Tyr Arg Ile Leu Gly Leu Lys Pro Thr Val Ile Phe Ala Asp Gln Ile 610 615 620 Met Tyr Thr Gly Phe Ala Tyr Ala Ala Arg Ser Gly Ala Ser Val Gly 625 630 635 640 Ile Asp Asp Met Val Ile Pro Glu Lys Lys His Glu Ile Ile Ser Glu 645 650 655 Ala Glu Ala Glu Val Ala Glu Ile Gln Glu Gln Phe Gln Ser Gly Leu 660 665 670 Val Thr Ala Gly Glu Arg Tyr Asn Lys Val Ile Asp Ile Trp Ala Ala 675 680 685 Ala Asn Asp Arg Val Ser Lys Ala Met Met Asp Asn Leu Gln Thr Glu 690 695 700 Thr Val Ile Asn Arg Asp Gly Gln Glu Glu Lys Gln Val Ser Phe Asn 705 710 715 720 Ser Ile Tyr Met Met Ala Asp Ser Gly Ala Arg Gly Ser Ala Ala Gln 725 730 735 Ile Arg Gln Leu Ala Gly Met Arg Gly Leu Met Ala Lys Pro Asp Gly 740 745 750 Ser Ile Ile Glu Thr Pro Ile Thr Ala Asn Phe Arg Glu Gly Leu Asn 755 760 765 Val Leu Gln Tyr Phe Ile Ser Thr His Gly Ala Arg Lys Gly Leu Ala 770 775 780 Asp Thr Ala Leu Lys Thr Ala Asn Ser Gly Tyr Leu Thr Arg Arg Leu 785 790 795 800 Val Asp Val Ala Gln Asp Leu Val Val Thr Glu Asp Asp Cys Gly Thr 805 810 815 His Glu Gly Ile Met Met Thr Pro Val Ile Glu Gly Gly Asp Val Lys 820 825 830 Glu Pro Leu Arg Asp Arg Val Leu Gly Arg Val Thr Ala Glu Asp Val 835 840 845 Leu Lys Pro Gly Thr Ala Asp Ile Leu Val Pro Arg Asn Thr Leu Leu 850 855 860 His Glu Gln Trp Cys Asp Leu Leu Glu Glu Asn Ser Val Asp Ala Val 865 870 875 880 Lys Val Arg Ser Val Val Ser Cys Asp Thr Asp Phe Gly Val Cys Ala 885 890 895 His Cys Tyr Gly Arg Asp Leu Ala Arg Gly His Ile Ile Asn Lys Gly 900 905 910 Glu Ala Ile Gly Val Ile Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr 915 920 925 Gln Leu Thr Met Arg Thr Phe His Ile Gly Gly Ala Ala Ser Arg Ala 930 935 940 Ala Ala Glu Ser Ser Ile Gln Val Lys Asn Lys Gly Ser Ile Lys Leu 945 950 955 960 Ser Asn Val Lys Ser Val Val Asn Ser Ser Gly Lys Leu Val Ile Thr 965 970 975 Ser Arg Asn Thr Glu Leu Lys Leu Ile Asp Glu Phe Gly Arg Thr Lys 980 985 990 Glu Ser Tyr Lys Val Pro Tyr Gly Ala Val Leu Ala Lys Gly Asp Gly 995 1000 1005 Glu Gln Val Ala Gly Gly Glu Thr Val Ala Asn Trp Asp Pro His Thr 1010 1015 1020 Met Pro Val Ile Thr Glu Val Ser Gly Phe Val Arg Phe Thr Asp Met 1025 1030 1035 1040 Ile Asp Gly Gln Thr Ile Thr Arg Gln Thr Asp Glu Leu Thr Gly Leu 1045 1050 1055 Ser Ser Leu Val Val Leu Asp Ser Ala Glu Arg Thr Ala Gly Gly Lys 1060 1065 1070 Asp Leu Arg Pro Ala Leu Lys Ile Val Asp Ala Gln Gly Asn Asp Val 1075 1080 1085 Leu Ile Pro Gly Thr Asp Met Pro Ala Gln Tyr Phe Leu Pro Gly Lys 1090 1095 1100 Ala Ile Val Gln Leu Glu Asp Gly Val Gln Ile Ser Ser Gly Asp Thr 1105 1110 1115 1120 Leu Ala Arg Ile Pro Gln Glu Ser Gly Gly Thr Lys Asp Ile Thr Gly 1125 1130 1135 Gly Leu Pro Arg Val Ala Asp Leu Phe Glu Ala Arg Arg Pro Lys Glu 1140 1145 1150 Pro Ala Ile Leu Ala Glu Ile Ser Gly Ile Val Ser Phe Gly Lys Glu 1155 1160 1165 Thr Lys Gly Lys Arg Arg Leu Val Ile Thr Pro Val Asp Gly Ser Asp 1170 1175 1180 Pro Tyr Glu Glu Met Ile Pro Lys Trp Arg Gln Leu Asn Val Phe Glu 1185 1190 1195 1200 Gly Glu Arg Val Glu Arg Gly Asp Val Ile Ser Asp Gly Pro Glu Ala 1205 1210 1215 Pro His Asp Ile Leu Arg Leu Arg Gly Val His Ala Val Thr Arg Tyr 1220 1225 1230 Ile Val Asn Glu Val Gln Asp Val Tyr Arg Leu Gln Gly Val Lys Ile 1235 1240 1245 Asn Asp Lys His Ile Glu Val Ile Val Arg Gln Met Leu Arg Lys Ala 1250 1255 1260 Thr Ile Val Asn Ala Gly Ser Ser Asp Phe Leu Glu Gly Glu Gln Val 1265 1270 1275 1280 Glu Tyr Ser Arg Val Lys Ile Ala Asn Arg Glu Leu Glu Ala Asn Gly 1285 1290 1295 Lys Val Gly Ala Thr Tyr Ser Arg Asp Leu Leu Gly Ile Thr Lys Ala 1300 1305 1310 Ser Leu Ala Thr Glu Ser Phe Ile Ser Ala Ala Ser Phe Gln Glu Thr 1315 1320 1325 Thr Arg Val Leu Thr Glu Ala Ala Val Ala Gly Lys Arg Asp Glu Leu 1330 1335 1340 Arg Gly Leu Lys Glu Asn Val Ile Val Gly Arg Leu Ile Pro Ala Gly 1345 1350 1355 1360 Thr Gly Tyr Ala Tyr His Gln Asp Arg Met Arg Arg Arg Ala Ala Gly 1365 1370 1375 Glu Ala Pro Ala Ala Pro Gln Val Thr Ala Glu Asp Ala Ser Ala Ser 1380 1385 1390 Leu Ala Glu Leu Leu Asn Ala Gly Leu Gly Gly Ser Asp Asn Glu 1395 1400 1405 <210> 5 <211> 3999 <212> DNA <213> Corynebacterium <400> 5 gtgctcgacg taaacgtctt cgatgagctc cgcatcggcc tggccaccgc cgacgacatc 60 cgccgttggt ccaagggtga ggtcaagaag ccggagacca tcaactaccg aaccctcaag 120 cctgagaagg acggtctgtt ctgcgagcgt atcttcggtc caactcgcga ctgggagtgc 180 gcctgcggta agtacaagcg tgtccgctac aagggcatca tctgtgaacg ctgtggcgtt 240 gaggtcacca agtccaaggt gcgccgtgag cgcatgggac acattgagct cgctgcacca 300 gtaacccaca tttggtactt caagggcgtt ccatcacgcc tcggctacct tttggacctt 360 gctccaaagg acctggacct catcatctac ttcggtgcga acatcatcac cagcgtggac 420 gaagaggctc gccacagcga ccagaccact cttgaggcag aaatgcttct ggagaagaag 480 gacgttgagg cagacgcaga gtctgacatt gctgagcgtg ctgaaaagct cgaagaggat 540 cttgctgaac ttgaggcagc tggcgctaag gccgacgctc gccgcaaggt tcaggctgct 600 gccgataagg aaatgcagca catccgtgag cgtgcacagc gcgaaatcga tcgtctcgat 660 gaggtctggc agaccttcat caagcttgct ccaaagcaga tgatccgcga tgagaagctc 720 tacgatgaac tgatcgaccg ctacgaggat tacttcaccg gtggtatggg tgcagagtcc 780 attgaggctt tgatccagaa cttcgacctt gatgctgagg ctgaagagct gcgcgacatc 840 atcaacaatg gcaagggcca gaagaagatg cgtgcactga agcgcctgaa ggttgttgca 900 gccttccagc gttccggcaa cgatcctgcc ggcatggttt tgaacgcgat cccagtgatc 960 ccaccagagc ttcgcccaat ggttcagctt gacggtggtc gcttcgctac ctccgacttg 1020 aacgaccttt accgtcgtgt gatcaaccgc aacaaccgtc tgaagcgcat gattgagctc 1080 ggtgcacctg agatcatcgt gaacaacgag aagcgcatgc tgcaggaatc tgtggacgcg 1140 ctgttcgaca acggtcgtcg tggtcgccca gttaccggac cgggtaaccg tccgctgaag 1200 tctctgtctg acttgctcaa gggcaagcaa ggccgtttcc gtcagaacct tctgggtaag 1260 cgtgttgact actctggtcg ttccgtaatt atcgttggtc ctcagctgcg cctccacgaa 1320 tgtggtctgc ctaagctgat ggctctcgag ctcttcaagc ctttcgtcat gaagcgcttg 1380 gtggagaacg agtacgcaca gaacatcaag tctgcaaagc gcatggttga gcgtcagcgc 1440 cctgaggtgt gggacgtcct cgaagaggcc atctctgagc acccagtgat gctgaaccgt 1500 gcaccaaccc tgcaccgctt gggcattcag gctttcgagc ctgtccttgt tgagggtaag 1560 gctattcagc tgcacccact tgcttgtgaa gctttcaacg ccgacttcga tggtgaccag 1620 atggcagttc acctgccgct gtccgctgaa gctcaggctg aggctcgcgt gctgatgctt 1680 gcatccaaca acattttgtc cccagcttcc ggtaagcctt tggctatgcc tcgtctggat 1740 atggtgaccg gtctgtacta cctgactctg gagaagtctt ccgaggagtt cggtggacag 1800 ggcgcttacc agcctgcaga tgaaaacggt cctgaaaagg gcgtgtattc ctcactggca 1860 gaagcaatca tggcttatga ccgtggtgta cttggcctgc aggccccagt tcgcatccgt 1920 ttgaaccacc tgcgcccacc agctgaggta gaagcagagc agttcccaga tggatggaac 1980 cagggcgaga cttggttggc tcacaccacc ttgggtcgcg ttatgttcaa cgagatcctg 2040 ccttggaact acccatacct tgagggcgtt atggtccgta agggtggcgg ctccgacaag 2100 atcatgcttg gcgacgtagt caatgacctc gctgctaagt acccaatgat caccgtggct 2160 cagaccatgg acaagatgaa ggatgctggc ttctactggt caacccgttc cggtgtgacc 2220 atcgctatgt ctgacgtttt ggttcttcct aacaaggaag aaatgctgga ccgctacgag 2280 gaatctgcac gccagatcga agttaagtac aaccgcggta agctcaccgg ccgtgagcgc 2340 tacgaccgtc tggtcgagct gtggaaggac gcaactgacg aggttggaca ggctgtcgag 2400 gatctgtacc cagacgacaa cccaattcca atgatcgtga agtctggtgc tgccggtaac 2460 atgcgtcaga tctggaccct tgctggtatg aagggcatgg ttgtgaactc gaagggtgac 2520 tacatcaccc gcccgatcaa gacttccttc cgtgaaggct tgaccgttct cgagtacttc 2580 aacaactccc acggttcccg taagggcctg gccgataccg cgctgcgtac cgctgactcc 2640 ggttacctga cccgtcgtct tgttgacgtc gctcaggacg tcatcgtgcg tgttgaggac 2700 tgtggcaccc gccagggtgt tcgcgttcct gtcgctgctg aggttctgga tgcaactggt 2760 gctgtcaccg gctacacccg ccatgacctg atcgagactt ctgtctccgg tcgtgttctg 2820 gctggcgatg caaccaacgc tgcaggcgag gttgtgcttg ctgctggtac cgacctgacc 2880 gagctcaaca ttgaccttct ggtcgaggct ggcatcaagg acgtcaaggt tcgttccgta 2940 cttacctgcc agaccccaac cggtgtttgt gctaagtgct acggcaagtc catggcttcc 3000 ggccagcagg ttgatatcgg agaggctgtc ggtattgttg ctgcacagtc cattggtgag 3060 cctggtaccc agctgaccat gcgtaccttc caccagggtg gtgtcggtgg cgatattacc 3120 ggcggtctgc ctcgtgttca ggagctgttt gaggcacgtg ttcctaagaa ctgtgcacca 3180 attgcttctg ttgaaggtgt tatccacctt gaggatgaag gcaacttcta cactctgacc 3240 atcgttcctg acgatggctc cgacaacgtt gtctacgaga agctgtccaa gcgacagggt 3300 cttgcatcca ctcgcgtggc tatggagtcc aacgctggtg cgttcattga gcgcaccttg 3360 accgaaggtg accgcgtcac cgttggtcag cgtctgctcc gtggtgcagc tgatccacac 3420 gacgtgctcg agatcctcgg tcgccgtggt gtggagcagc acctcatcga tgaggtgcag 3480 gctgtttacc gtgcacaggg tgtggccatc cacgacaagc acatcgaaat catcattcgt 3540 cagatgctgc gtcgcggtac cgtcattgag tccggttcca ccgagttcct tcctggttct 3600 ttggttgacc tctctgaggc gaagctggct aactctgagg caatcggtgc gggcggtcag 3660 cctgcagagc tgcgttctga gatcatgggt atcaccaagg cctctctcgc aactgagtct 3720 tggctgtctg cagcgtcctt ccaggagacc actcgtgtcc tgactgatgc tgctatcaac 3780 aagcgctccg ataagctcat cggcctgaag ggaacgctca tcggtaagct gatcccagct 3840 ggtactggta tttcccgtta ccgcaacatc tccatcaagc caaccgaggc tgctcgcaac 3900 gccgcatact cgatcccaac ttatggtgag tcgatttacg gtgacgatgg attcggtgag 3960 ttcaccggcg catccgtccc attggatgag gctttctag 3999 <210> 6 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> primer <400> 6 aattgtgaag ggcgagaaca 20 <210> 7 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> primer <400> 7 cagggcctca acttctcagc 20 <210> 8 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M1) <400> 8 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gly Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 9 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M2) <400> 9 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu His Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 10 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M3) <400> 10 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Lys Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 11 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M4) <400> 11 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Gly Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Glu Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Cys Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 12 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M5) <400> 12 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr His Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Cys Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Cys Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 13 <211> 1334 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M6) <400> 13 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Thr Thr Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser 1250 1255 1260 Asp Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile 1265 1270 1275 1280 Pro Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro 1285 1290 1295 Thr Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu 1300 1305 1310 Ser Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val 1315 1320 1325 Pro Leu Asp Glu Ala Phe 1330 <210> 14 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M7) <400> 14 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Arg Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 15 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M8) <400> 15 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Asp Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 16 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M9) <400> 16 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Pro Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 17 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M10) <400> 17 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Asn Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 18 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M11) <400> 18 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Phe Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Cys Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 19 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M12) <400> 19 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Phe Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Tyr Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Phe Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 20 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M13) <400> 20 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Ser Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 21 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M14) <400> 21 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Gly Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 22 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M15) <400> 22 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Thr Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 23 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M16) <400> 23 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Lys Val Gly Gly His Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 24 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M17) <400> 24 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Glu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Asp Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 25 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M18) <400> 25 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala His Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 26 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M19) <400> 26 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Arg Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Gly Ile Thr 1220 1225 1230 Lys Ala Ser Thr Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile Asn Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 27 <211> 1333 <212> PRT <213> Artificial Sequence <220> <223> RpoC of KCCM11016P-rpoC(M20) <400> 27 Met Leu Asp Val Asn Val Phe Asp Glu Leu Arg Ile Gly Leu Ala Thr 1 5 10 15 Ala Asp Asp Ile Arg Arg Trp Ser Lys Gly Glu Val Lys Lys Pro Glu 20 25 30 Thr Ile Asn Tyr Arg Thr Leu Lys Pro Glu Lys Asp Gly Leu Phe Cys 35 40 45 Glu Arg Ile Phe Gly Pro Thr Arg Asp Trp Glu Cys Ala Cys Gly Lys 50 55 60 Tyr Lys Arg Val Arg Tyr Lys Gly Ile Ile Cys Glu Arg Cys Gly Val 65 70 75 80 Glu Val Thr Lys Ser Lys Val Arg Arg Glu Arg Met Gly His Ile Glu 85 90 95 Leu Ala Ala Pro Val Thr His Ile Trp Tyr Phe Lys Gly Val Pro Ser 100 105 110 Arg Leu Gly Tyr Leu Leu Asp Leu Ala Pro Lys Asp Leu Asp Leu Ile 115 120 125 Ile Tyr Phe Gly Ala Asn Ile Ile Thr Ser Val Asp Glu Glu Ala Arg 130 135 140 His Ser Asp Gln Thr Thr Leu Glu Ala Glu Met Leu Leu Glu Lys Lys 145 150 155 160 Asp Val Glu Ala Asp Ala Glu Ser Asp Ile Ala Glu Arg Ala Glu Lys 165 170 175 Leu Glu Glu Asp Leu Ala Glu Leu Glu Ala Ala Gly Ala Lys Ala Asp 180 185 190 Ala Arg Arg Lys Val Gln Ala Ala Ala Asp Lys Glu Met Gln His Ile 195 200 205 Arg Glu Arg Ala Gln Arg Glu Ile Asp Arg Leu Asp Glu Val Trp Gln 210 215 220 Thr Phe Ile Lys Leu Ala Pro Lys Gln Met Ile Arg Asp Glu Lys Leu 225 230 235 240 Tyr Asp Glu Leu Ile Asp Arg Tyr Glu Asp Tyr Phe Thr Gly Gly Met 245 250 255 Gly Ala Glu Ser Ile Glu Ala Leu Ile Gln Asn Phe Asp Leu Asp Ala 260 265 270 Glu Ala Glu Glu Leu Arg Asp Ile Ile Asn Asn Gly Lys Gly Gln Lys 275 280 285 Lys Met Arg Ala Leu Lys Arg Leu Lys Val Val Ala Ala Phe Gln Arg 290 295 300 Ser Gly Asn Asp Pro Ala Gly Met Val Leu Asn Ala Ile Pro Val Ile 305 310 315 320 Pro Pro Glu Leu Arg Pro Met Val Gln Leu Asp Gly Gly Arg Phe Ala 325 330 335 Thr Ser Asp Leu Asn Asp Leu Tyr Arg Arg Val Ile Asn Arg Asn Asn 340 345 350 Arg Leu Lys Arg Met Ile Glu Leu Gly Ala Pro Glu Ile Ile Val Asn 355 360 365 Asn Glu Lys Arg Met Leu Gln Glu Ser Val Asp Ala Leu Phe Asp Asn 370 375 380 Gly Arg Arg Gly Arg Pro Val Thr Gly Pro Gly Asn Arg Pro Leu Lys 385 390 395 400 Ser Leu Ser Asp Leu Leu Lys Gly Lys Gln Gly Arg Phe Arg Gln Asn 405 410 415 Leu Leu Gly Lys Arg Val Asp Tyr Ser Gly Arg Ser Val Ile Ile Val 420 425 430 Gly Pro Gln Leu Arg Leu His Glu Cys Gly Leu Pro Lys Leu Met Ala 435 440 445 Leu Glu Leu Phe Lys Pro Phe Val Met Lys Arg Leu Val Glu Asn Glu 450 455 460 Tyr Ala Gln Asn Ile Lys Ser Ala Lys Arg Met Val Glu Arg Gln Arg 465 470 475 480 Pro Glu Val Trp Asp Val Leu Glu Glu Ala Ile Ser Glu His Pro Val 485 490 495 Met Leu Asn Arg Ala Pro Thr Leu His Arg Leu Gly Ile Gln Ala Phe 500 505 510 Glu Pro Val Leu Val Glu Gly Lys Ala Ile Gln Leu His Pro Leu Ala 515 520 525 Cys Glu Ala Phe Asn Ala Asp Phe Asp Gly Asp Gln Met Ala Val His 530 535 540 Leu Pro Leu Ser Ala Glu Ala Gln Ala Glu Ala Arg Val Leu Met Leu 545 550 555 560 Ala Ser Asn Asn Ile Leu Ser Pro Ala Ser Gly Lys Pro Leu Ala Met 565 570 575 Pro Arg Leu Asp Met Val Thr Gly Leu Tyr Tyr Leu Thr Leu Glu Lys 580 585 590 Ser Ser Glu Glu Phe Gly Gly Gln Gly Ala Tyr Gln Pro Ala Asp Glu 595 600 605 Asn Gly Pro Glu Lys Gly Val Tyr Ser Ser Leu Ala Glu Ala Ile Met 610 615 620 Ala Tyr Asp Arg Gly Val Leu Gly Leu Gln Ala Pro Val Arg Ile Arg 625 630 635 640 Leu Asn His Leu Arg Pro Pro Ala Glu Val Glu Ala Glu Gln Phe Pro 645 650 655 Asp Gly Trp Asn Gln Gly Glu Thr Trp Leu Ala His Thr Thr Leu Gly 660 665 670 Arg Val Met Phe Asn Glu Ile Leu Pro Trp Asn Tyr Pro Tyr Leu Glu 675 680 685 Gly Val Met Val Arg Lys Gly Gly Gly Ser Asp Lys Ile Met Leu Gly 690 695 700 Asp Val Val Asn Asp Leu Ala Ala Lys Tyr Pro Met Ile Thr Val Ala 705 710 715 720 Gln Thr Met Asp Lys Met Lys Asp Ala Gly Phe Tyr Trp Ser Thr Arg 725 730 735 Ser Gly Val Thr Ile Ala Met Ser Asp Val Leu Val Leu Pro Asn Lys 740 745 750 Glu Glu Met Leu Asp Arg Tyr Glu Glu Ser Ala Arg Gln Ile Glu Val 755 760 765 Lys Tyr Asn Arg Gly Lys Leu Thr Gly Arg Glu Arg Tyr Asp Arg Leu 770 775 780 Val Glu Leu Trp Lys Asp Ala Thr Asp Glu Val Gly Gln Ala Val Glu 785 790 795 800 Asp Leu Tyr Pro Asp Asp Asn Pro Ile Pro Met Ile Val Lys Ser Gly 805 810 815 Ala Ala Gly Asn Met Arg Gln Ile Trp Thr Leu Ala Gly Met Lys Gly 820 825 830 Met Val Val Asn Ser Lys Gly Asp Tyr Ile Thr Arg Pro Ile Lys Thr 835 840 845 Ser Phe Arg Glu Gly Leu Thr Val Leu Glu Tyr Phe Asn Asn Ser His 850 855 860 Gly Ser Arg Lys Gly Leu Ala Asp Thr Ala Leu Arg Thr Ala Asp Ser 865 870 875 880 Gly Tyr Leu Thr Arg Arg Leu Val Asp Val Ala Gln Asp Val Ile Val 885 890 895 Arg Val Glu Asp Cys Gly Thr Arg Gln Gly Val Arg Val Pro Val Ala 900 905 910 Ala Glu Val Leu Asp Ala Thr Gly Ala Val Thr Gly Tyr Thr Arg His 915 920 925 Asp Leu Ile Glu Thr Ser Val Ser Gly Arg Val Leu Ala Gly Asp Ala 930 935 940 Thr Asn Ala Ala Gly Glu Val Val Leu Ala Ala Gly Thr Asp Leu Thr 945 950 955 960 Glu Leu Asn Ile Asp Leu Leu Val Glu Ala Gly Ile Lys Asp Val Lys 965 970 975 Val Arg Ser Val Leu Thr Cys Gln Thr Pro Thr Gly Val Cys Ala Lys 980 985 990 Cys Tyr Gly Lys Ser Met Ala Ser Gly Gln Gln Val Asp Ile Gly Glu 995 1000 1005 Ala Val Gly Ile Val Ala Ala Gln Ser Ile Gly Glu Pro Gly Thr Gln 1010 1015 1020 Leu Thr Met Arg Thr Phe His Gln Gly Gly Val Gly Gly Asp Ile Thr 1025 1030 1035 1040 Gly Gly Leu Pro Arg Val Gln Glu Leu Phe Glu Ala Arg Val Pro Lys 1045 1050 1055 Asn Cys Ala Pro Ile Ala Ser Val Glu Gly Val Ile His Leu Glu Asp 1060 1065 1070 Glu Gly Asn Phe Tyr Thr Leu Thr Ile Val Pro Asp Asp Gly Ser Asp 1075 1080 1085 Asn Val Val Tyr Glu Lys Leu Ser Lys Arg Gln Gly Leu Ala Ser Thr 1090 1095 1100 Arg Val Ala Met Glu Ser Asn Ala Gly Ala Phe Ile Glu Arg Thr Leu 1105 1110 1115 1120 Thr Glu Gly Asp Arg Val Thr Val Gly Gln Arg Leu Leu Arg Gly Ala 1125 1130 1135 Ala Asp Pro His Asp Val Leu Glu Ile Leu Gly Arg Arg Gly Val Glu 1140 1145 1150 Gln His Leu Ile Asp Glu Val Gln Ala Val Tyr Arg Ala Gln Gly Val 1155 1160 1165 Ala Ile His Asp Lys His Ile Glu Ile Ile Ile Arg Gln Met Leu Arg 1170 1175 1180 Arg Gly Thr Val Ile Glu Ser Gly Ser Thr Glu Phe Leu Pro Gly Ser 1185 1190 1195 1200 Leu Val Asp Leu Ser Glu Ala Lys Leu Ala Asn Ser Glu Ala Ile Gly 1205 1210 1215 Ala Gly Gly Gln Pro Ala Glu Leu Arg Ser Glu Ile Met Tyr Ile Thr 1220 1225 1230 Lys Ala Ser Leu Ala Thr Glu Ser Trp Leu Ser Ala Ala Ser Phe Gln 1235 1240 1245 Glu Thr Thr Arg Val Leu Thr Asp Ala Ala Ile His Lys Arg Ser Asp 1250 1255 1260 Lys Leu Ile Gly Leu Lys Glu Asn Val Ile Ile Gly Lys Leu Ile Pro 1265 1270 1275 1280 Ala Gly Thr Gly Ile Ser Arg Tyr Arg Asn Ile Ser Ile Lys Pro Thr 1285 1290 1295 Glu Ala Ala Arg Asn Ala Ala Tyr Ser Ile Pro Thr Tyr Gly Glu Ser 1300 1305 1310 Ile Tyr Gly Asp Asp Gly Phe Gly Glu Phe Thr Gly Ala Ser Val Pro 1315 1320 1325 Leu Asp Glu Ala Phe 1330 <210> 28 <211> 29 <212> DNA <213> Artificial Sequence <220> <223> primer <400> 28 tttgaattct accttgaggg cgttatggt 29 <210> 29 <211> 29 <212> DNA <213> Artificial Sequence <220> <223> primer <400> 29 tttgaattcc cgttggtcag cgtctgctc 29 <210> 30 <211> 29 <212> DNA <213> Artificial Sequence <220> <223> primer <400> 30 tttgtcgacc agggcctcaa cttctcagc 29

Claims (7)

  1. 서열번호 1의 아미노산 서열에서 제975 내지 제1284 중의 아미노산에서 1 내지 5 개의 아미노산이 다른 아미노산으로 치환된 아미노산 서열을 갖는 RNA 폴리머라제의 베타 프라임 서브 유닛(β'-subunit) 변이체.
  2. 청구항 1에 있어서, 상기 서열번호 1의 아미노산 서열에서 제975 내지 제1284 중의 아미노산은 제1014 내지 제1034 중의 아미노산 및 제1230 내지 제1255 중의 아미노산 중 하나 이상인 것인 RNA 폴리머라제 베타 프라임 서브 유닛 변이체.　
  3. 청구항 1의 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 코딩하는 뉴클레오티드 서열을 갖는 폴리뉴클레오티드.
  4. 조절 서열과 작동가능하게 연결된 청구항 3의 폴리뉴클레오티드를 포함하는 벡터.
  5. 청구항 1의 RNA 폴리머라제의 베타 프라임 서브 유닛 변이체를 발현하는 코리네박테리움(Corynebacterium) 미생물.
  6. 청구항 5에 있어서, 상기 코리네박테리움 속 미생물은 코리네박테리움 글루타미쿰(Corynebacterium glutamicum)인 것인 미생물.
  7. 청구항 5의 미생물을 배양하여 배양물 중에 L-라이신을 생산하는 단계; 및
    배양물로부터 L-라이신을 회수하는 단계를 포함하는, L-라이신을 생산하는 방법.
KR1020130073309A 2013-06-25 2013-06-25 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법 KR101594156B1 (ko)

Priority Applications (11)

Application Number Priority Date Filing Date Title
KR1020130073309A KR101594156B1 (ko) 2013-06-25 2013-06-25 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법
HUE14817261A HUE050834T2 (hu) 2013-06-25 2014-06-24 Mikroorganizmus fokozott L-lizin termelékenységgel, és eljárás L-lizin termelésére ennek alkalmazásával
JP2016523640A JP6195668B2 (ja) 2013-06-25 2014-06-24 Ｌ−リジン生産能が向上した微生物、及びそれを利用してｌ−リジンを生産する方法
CN201910757268.2A CN110423734B (zh) 2013-06-25 2014-06-24 具有增强的l-赖氨酸生产力的微生物和用于通过使用该微生物产生l-赖氨酸的方法
EP14817261.2A EP3015546B1 (en) 2013-06-25 2014-06-24 Microorganism with enhanced l-lysine productivity and method for producing l-lysine by using same
ES14817261T ES2802949T3 (es) 2013-06-25 2014-06-24 Microorganismo con productividad de l-lisina aumentada y procedimiento para producir l-lisina utilizando el mismo
BR112015032121-6A BR112015032121B1 (pt) 2013-06-25 2014-06-24 Mutante de subunidade beta-prime (subunidade ?) de rna polimerase, microrganismo do gênero corynebacterium e método para produzir l-lisina
CN201480036728.8A CN105658793B (zh) 2013-06-25 2014-06-24 具有增强的l-赖氨酸生产力的微生物和用于通过使用该微生物产生l-赖氨酸的方法
PCT/KR2014/005576 WO2014208981A1 (ko) 2013-06-25 2014-06-24 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법
US14/392,186 US9758771B2 (en) 2013-06-25 2014-06-24 Microorganism with enhanced L-lysine productivity and method for producing L-lysine by using same
PL14817261T PL3015546T3 (pl) 2013-06-25 2014-06-24 Mikoorganizm o ulepszonej zdolności wytwarzania l-lizyny i sposób wytwarzania l-lizyny z jego użyciem

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
KR1020130073309A KR101594156B1 (ko) 2013-06-25 2013-06-25 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법

Related Child Applications (1)

Application Number Title Priority Date Filing Date
KR1020150044392A Division KR20150040837A (ko) 2015-03-30 2015-03-30 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법

Publications (2)

Publication Number Publication Date
KR20150000773A true KR20150000773A (ko) 2015-01-05
KR101594156B1 KR101594156B1 (ko) 2016-02-15

Family

ID=52142246

Family Applications (1)

Application Number Title Priority Date Filing Date
KR1020130073309A KR101594156B1 (ko) 2013-06-25 2013-06-25 Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법

Country Status (10)

Country Link
US (1) US9758771B2 (ko)
EP (1) EP3015546B1 (ko)
JP (1) JP6195668B2 (ko)
KR (1) KR101594156B1 (ko)
CN (1) CN110423734B (ko)
BR (1) BR112015032121B1 (ko)
ES (1) ES2802949T3 (ko)
HU (1) HUE050834T2 (ko)
PL (1) PL3015546T3 (ko)
WO (1) WO2014208981A1 (ko)

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2020032590A1 (en) * 2018-08-07 2020-02-13 Cj Cheiljedang Corporation Nucleic acid molecules comprising a variant rpoc coding sequence
KR102303747B1 (ko) * 2021-04-12 2021-09-16 씨제이제일제당 (주) 신규한 주요 촉진제 수퍼패밀리 퍼미에이즈 변이체 및 이를 이용한 l-라이신 생산 방법
KR102314885B1 (ko) * 2021-04-12 2021-10-18 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법
KR102314882B1 (ko) * 2021-01-29 2021-10-19 씨제이제일제당 (주) 신규한 막단백질 TerC 변이체 및 이를 이용한 L-라이신 생산 방법
KR102344057B1 (ko) * 2021-01-29 2021-12-27 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법
WO2022154172A1 (ko) * 2021-01-15 2022-07-21 씨제이제일제당 (주) 신규한 dna 중합효소 ⅲ 감마 및 타우 서브유닛 변이체 및 이를 이용한 l-라이신 생산 방법

Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR101793328B1 (ko) * 2015-07-03 2017-11-03 씨제이제일제당 (주) Ｌ-라이신 생산능을 갖는 미생물 및 이를 이용한 ｌ-라이신 생산 방법
CN108473946B (zh) * 2015-10-30 2023-01-03 丹尼斯科美国公司 增强的蛋白质表达及其方法
CN114008206B (zh) * 2019-12-23 2024-05-17 Cj第一制糖株式会社 具有增强的细胞色素c活性的l-氨基酸生产微生物及使用其的l-氨基酸生产方法

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6927046B1 (en) 1999-12-30 2005-08-09 Archer-Daniels-Midland Company Increased lysine production by gene amplification using coryneform bacteria
CN101851599B (zh) 2001-12-29 2016-01-20 诺维信公司 具有改变产物产量特性的真细菌rna聚合酶突变体
BRPI0716980A2 (pt) 2006-09-15 2013-10-22 Cj Cheiljedang Corp Corynebacteria com produtividade de l-lisina aumentada e método de produção da l-lisina usando a mesma
JP5048996B2 (ja) 2006-11-10 2012-10-17 昭和電工株式会社 加工性に優れた耐摩耗性アルミニウム合金材およびその製造方法
KR20070057093A (ko) 2007-01-16 2007-06-04 씨제이 주식회사 카나마이신 내성을 갖고 ｌ-라이신 생산능이 향상된코리네형 미생물 및 그를 이용하여 ｌ-라이신을 생산하는방법
KR101012590B1 (ko) * 2008-06-25 2011-02-07 씨제이제일제당 (주) 라이신 생산능이 향상된 코리네박테리움 및 이를 이용한 라이신 생산방법
KR20160114184A (ko) 2009-11-18 2016-10-04 미리안트 코포레이션 화합물들의 효과적인 생산을 위한 미생물 엔지니어링

Cited By (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2020032590A1 (en) * 2018-08-07 2020-02-13 Cj Cheiljedang Corporation Nucleic acid molecules comprising a variant rpoc coding sequence
WO2022154172A1 (ko) * 2021-01-15 2022-07-21 씨제이제일제당 (주) 신규한 dna 중합효소 ⅲ 감마 및 타우 서브유닛 변이체 및 이를 이용한 l-라이신 생산 방법
KR102314882B1 (ko) * 2021-01-29 2021-10-19 씨제이제일제당 (주) 신규한 막단백질 TerC 변이체 및 이를 이용한 L-라이신 생산 방법
KR102344057B1 (ko) * 2021-01-29 2021-12-27 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법
WO2022163914A1 (ko) * 2021-01-29 2022-08-04 씨제이제일제당 (주) 신규한 미코티온 리덕타제 변이체 및 이를 이용한 l-라이신 생산 방법
WO2022163915A1 (ko) * 2021-01-29 2022-08-04 씨제이제일제당 (주) 신규한 Co/Zn/Cd 유출 시스템 컴포넌트 변이체 및 이를 이용한 L-라이신 생산 방법
WO2022163913A1 (ko) * 2021-01-29 2022-08-04 씨제이제일제당 (주) 신규한 막단백질 TerC 변이체 및 이를 이용한 L-라이신 생산 방법
WO2022163909A1 (ko) * 2021-01-29 2022-08-04 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법
KR102303747B1 (ko) * 2021-04-12 2021-09-16 씨제이제일제당 (주) 신규한 주요 촉진제 수퍼패밀리 퍼미에이즈 변이체 및 이를 이용한 l-라이신 생산 방법
KR102314885B1 (ko) * 2021-04-12 2021-10-18 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법
WO2022220329A1 (ko) * 2021-04-12 2022-10-20 씨제이제일제당 (주) 신규한 주요 촉진제 수퍼패밀리 퍼미에이즈 변이체 및 이를 이용한 l-라이신 생산 방법
WO2022220328A1 (ko) * 2021-04-12 2022-10-20 씨제이제일제당 (주) 신규한 단백질 변이체 및 이를 이용한 l-라이신 생산 방법

Also Published As

Publication number Publication date
CN110423734A (zh) 2019-11-08
HUE050834T2 (hu) 2021-01-28
CN110423734B (zh) 2023-10-24
ES2802949T3 (es) 2021-01-22
BR112015032121B1 (pt) 2022-12-27
JP6195668B2 (ja) 2017-09-13
EP3015546A1 (en) 2016-05-04
KR101594156B1 (ko) 2016-02-15
WO2014208981A1 (ko) 2014-12-31
JP2016523543A (ja) 2016-08-12
EP3015546A4 (en) 2017-01-04
US20160230151A1 (en) 2016-08-11
EP3015546B1 (en) 2020-05-27
PL3015546T3 (pl) 2020-11-16
BR112015032121A2 (pt) 2017-08-29
CN105658793A (zh) 2016-06-08
US9758771B2 (en) 2017-09-12

Similar Documents

Publication Publication Date Title
KR101594156B1 (ko) Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법
KR101904666B1 (ko) Atp 포스포리보실기 전이효소 변이체 및 이를 이용한 l-히스티딘 생산방법
KR101483396B1 (ko) Ｌ-라이신 생산능을 갖는 미생물을 이용하여 ｌ-라이신을 생산하는 방법
CN103243042B (zh) 具有增强的l-赖氨酸产率的棒状杆菌属微生物以及使用所述微生物生产l-赖氨酸的方法
US8058036B2 (en) Microorganism of Corynebacterium genus having enhanced L-lysine productivity and a method of producing L-lysine using the same
KR101498630B1 (ko) Ｌ-라이신 생산능이 향상된 코리네박테리움 속 미생물 및 이를 이용한 l-라이신 생산방법
US11104925B2 (en) Microorganism producing L-lysine and method for producing L-lysine using the same
KR101766964B1 (ko) L-라이신 생산능을 가지는 코리네박테리움 속 미생물 및 이를 이용한 l-라이신 생산방법
CN107849576A (zh) 用于产生腐胺或鸟氨酸的微生物以及使用这些微生物产生腐胺或鸟氨酸的方法
KR101565770B1 (ko) L-라이신 생산능이 향상된 코리네박테리움 속 미생물 및 이를 이용한 l-라이신을 생산하는 방법
KR101740807B1 (ko) L-라이신 생산능을 가지는 코리네박테리움 속 미생물 및 이를 이용한 l-라이신 생산방법
KR102617168B1 (ko) 쉬와넬라 오네이덴시스 유래 단백질을 발현하는 미생물, 및 이를 이용한 l-아미노산 생산 방법
KR101768390B1 (ko) L-라이신 생산능이 향상된 미생물 및 이를 이용한 l-라이신 생산방법
KR101760219B1 (ko) L-라이신 생산능이 향상된 미생물 및 이를 이용한 l-라이신 생산방법
KR101768391B1 (ko) L-라이신 생산능이 향상된 미생물 및 이를 이용한 l-라이신 생산방법
KR101755767B1 (ko) L-라이신 생산능이 향상된 미생물 및 이를 이용한 l-라이신 생산방법
CN105658793B (zh) 具有增强的l-赖氨酸生产力的微生物和用于通过使用该微生物产生l-赖氨酸的方法
KR20150040837A (ko) Ｌ-라이신 생산능이 향상된 미생물 및 그를 이용하여 ｌ-라이신을 생산하는 방법
KR102616694B1 (ko) 쉬와넬라 아틀란티카 유래 단백질을 발현하는 미생물, 및 이를 이용한 l-아미노산 생산 방법

Legal Events

Date Code Title Description
A201 Request for examination
E902 Notification of reason for refusal
E90F Notification of reason for final refusal
A107 Divisional application of patent
E90F Notification of reason for final refusal
E701 Decision to grant or registration of patent right
GRNT Written decision to grant
FPAY Annual fee payment

Payment date: 20181126

Year of fee payment: 4

FPAY Annual fee payment

Payment date: 20191125

Year of fee payment: 5