Difference between revisions of "CapC"
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==Original publications== | ==Original publications== | ||
<pubmed>11751809,19420703, 16233197 20564357 20564574 24296669 21965392</pubmed> | <pubmed>11751809,19420703, 16233197 20564357 20564574 24296669 21965392</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:15, 16 February 2014
- Description: capsular polyglutamate biosynthesis
Gene name | capC |
Synonyms | ywtA, pgsC |
Essential | no |
Product | unknown |
Function | capsule synthesis |
Gene expression levels in SubtiExpress: capC | |
MW, pI | 16 kDa, 9.672 |
Gene length, protein length | 447 bp, 149 aa |
Immediate neighbours | capA, capB |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
capsule biosynthesis and degradation
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35890
Phenotypes of a mutant
no synthesis of the poly-gamma-glutamate capsule PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P96737
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481]
[WorldCat.org]
[DOI]
(I p)
Thomas Candela, Agnès Fouet
Poly-gamma-glutamate in bacteria.
Mol Microbiol: 2006, 60(5);1091-8
[PubMed:16689787]
[WorldCat.org]
[DOI]
(P p)
Original publications
Jia Mun Chan, Sarah B Guttenplan, Daniel B Kearns
Defects in the flagellar motor increase synthesis of poly-γ-glutamate in Bacillus subtilis.
J Bacteriol: 2014, 196(4);740-53
[PubMed:24296669]
[WorldCat.org]
[DOI]
(I p)
Thi-Huyen Do, Yuki Suzuki, Naoki Abe, Jun Kaneko, Yoshifumi Itoh, Keitarou Kimura
Mutations suppressing the loss of DegQ function in Bacillus subtilis (natto) poly-γ-glutamate synthesis.
Appl Environ Microbiol: 2011, 77(23);8249-58
[PubMed:21965392]
[WorldCat.org]
[DOI]
(I p)
Tohru Kamei, Daisuke Yamashiro, Terumi Horiuchii, Yutaka Minouchi, Makoto Ashiuchi
Identification and biochemical characterization of membranous short-chain polyglutamate from Bacillus subtilis.
Chem Biodivers: 2010, 7(6);1563-72
[PubMed:20564574]
[WorldCat.org]
[DOI]
(I p)
Chuan-Mei Yeh, Jyh-Perng Wang, Shih-Ching Lo, Wen-Chia Chan, Ming-Yi Lin
Chromosomal integration of a synthetic expression control sequence achieves poly-gamma-glutamate production in a Bacillus subtilis strain.
Biotechnol Prog: 2010, 26(4);1001-7
[PubMed:20564357]
[WorldCat.org]
[DOI]
(I p)
Keitarou Kimura, Lam-Son Phan Tran, Thi-Huyen Do, Yoshifumi Itoh
Expression of the pgsB encoding the poly-gamma-DL-glutamate synthetase of Bacillus subtilis (natto).
Biosci Biotechnol Biochem: 2009, 73(5);1149-55
[PubMed:19420703]
[WorldCat.org]
[DOI]
(I p)
Yuji Urushibata, Shinji Tokuyama, Yasutaka Tahara
Difference in transcription levels of cap genes for gamma-polyglutamic acid production between Bacillus subtilis IFO 16449 and Marburg 168.
J Biosci Bioeng: 2002, 93(2);252-4
[PubMed:16233197]
[WorldCat.org]
[DOI]
(P p)
Yuji Urushibata, Shinji Tokuyama, Yasutaka Tahara
Characterization of the Bacillus subtilis ywsC gene, involved in gamma-polyglutamic acid production.
J Bacteriol: 2002, 184(2);337-43
[PubMed:11751809]
[WorldCat.org]
[DOI]
(P p)