Difference between revisions of "SrfAB"
| Line 97: | Line 97: | ||
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/8830686 PubMed] | ** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/8830686 PubMed] | ||
** repressed during hydrogen peroxide stress ([[PerR]]) {{PubMed|16166527}} | ** repressed during hydrogen peroxide stress ([[PerR]]) {{PubMed|16166527}} | ||
| + | ** expressed at high cell density ([[ComA]]) {{PubMed|16091051}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/8830686 PubMed] | ** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/8830686 PubMed] | ||
| − | ** [[ComA]]: transcription activation {{PubMed|1715856}} | + | ** [[ComA]]: transcription activation {{PubMed|1715856,16091051}} |
** [[PerR]]: transcription activation {{PubMed|16166527}} | ** [[PerR]]: transcription activation {{PubMed|16166527}} | ||
** [[Spx]]: transcription repression {{PubMed|12642660}} | ** [[Spx]]: transcription repression {{PubMed|12642660}} | ||
| Line 127: | Line 128: | ||
=References= | =References= | ||
| − | <pubmed>17227471,16166527,8288534,10960106, 12642660,8830686,18763711 17218307, 17190806 1715856 </pubmed> | + | <pubmed>17227471,16166527,8288534,10960106, 12642660,8830686,18763711 17218307, 17190806 1715856 16091051</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:47, 15 February 2010
- Description: surfactin synthetase / competence
| Gene name | srfAB |
| Synonyms | comL |
| Essential | no |
| Product | surfactin synthetase / competence |
| Function | antibiotic synthesis |
| MW, pI | 400 kDa, 4.903 |
| Gene length, protein length | 10761 bp, 3587 aa |
| Immediate neighbours | srfAA, comS |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU03490
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Ser-999 AND Ser-2045 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: membrane PubMed
Database entries
- Structure:
- UniProt: Q04747
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Mitsuo Ogura, Yasutaro Fujita
Bacillus subtilis rapD, a direct target of transcription repression by RghR, negatively regulates srfA expression.
FEMS Microbiol Lett: 2007, 268(1);73-80
[PubMed:17227471]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
Paul D Straight, Michael A Fischbach, Christopher T Walsh, David Z Rudner, Roberto Kolter
A singular enzymatic megacomplex from Bacillus subtilis.
Proc Natl Acad Sci U S A: 2007, 104(1);305-10
[PubMed:17190806]
[WorldCat.org]
[DOI]
(P p)
Kentaro Hayashi, Taku Ohsawa, Kazuo Kobayashi, Naotake Ogasawara, Mitsuo Ogura
The H2O2 stress-responsive regulator PerR positively regulates srfA expression in Bacillus subtilis.
J Bacteriol: 2005, 187(19);6659-67
[PubMed:16166527]
[WorldCat.org]
[DOI]
(P p)
Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051]
[WorldCat.org]
[DOI]
(P p)
Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660]
[WorldCat.org]
[DOI]
(P p)
M S Turner, J D Helmann
Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis.
J Bacteriol: 2000, 182(18);5202-10
[PubMed:10960106]
[WorldCat.org]
[DOI]
(P p)
P Serror, A L Sonenshein
CodY is required for nutritional repression of Bacillus subtilis genetic competence.
J Bacteriol: 1996, 178(20);5910-5
[PubMed:8830686]
[WorldCat.org]
[DOI]
(P p)
D Vollenbroich, N Mehta, P Zuber, J Vater, R M Kamp
Analysis of surfactin synthetase subunits in srfA mutants of Bacillus subtilis OKB105.
J Bacteriol: 1994, 176(2);395-400
[PubMed:8288534]
[WorldCat.org]
[DOI]
(P p)
M M Nakano, L A Xia, P Zuber
Transcription initiation region of the srfA operon, which is controlled by the comP-comA signal transduction system in Bacillus subtilis.
J Bacteriol: 1991, 173(17);5487-93
[PubMed:1715856]
[WorldCat.org]
[DOI]
(P p)
