Difference between revisions of "SrfAC"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[miscellaneous metabolic pathways]]}},
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{{SubtiWiki category|[[biosynthesis of antibacterial compounds]]}},
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{{SubtiWiki category|[[membrane proteins]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
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= This gene is a member of the following [[regulons]] =
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{{SubtiWiki regulon|[[CodY regulon]]}},
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{{SubtiWiki regulon|[[ComA regulon]]}},
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{{SubtiWiki regulon|[[PerR regulon]]}},
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{{SubtiWiki regulon|[[Spx regulon]]}}
  
 
=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[miscellaneous metabolic pathways]]}},
 
{{SubtiWiki category|[[biosynthesis of antibacterial compounds]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
 
{{SubtiWiki category|[[phosphoproteins]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 16:39, 8 December 2010

  • Description: surfactin synthetase / competence

Gene name srfAC
Synonyms comL
Essential no
Product surfactin synthetase / competence
Function antibiotic synthesis
MW, pI 143 kDa, 4.97
Gene length, protein length 3822 bp, 1274 aa
Immediate neighbours comS, srfAD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SrfAC context.gif
This image was kindly provided by SubtiList





Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CodY regulon, ComA regulon, PerR regulon, Spx regulon

The gene

Basic information

  • Locus tag: BSU03510

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: acyl carrier domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-1003 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
    • repressed during hydrogen peroxide stress (PerR) PubMed
    • expressed at high cell density (ComA) PubMed
  • 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

Original publications

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

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)

Alan Tanovic, Stefan A Samel, Lars-Oliver Essen, Mohamed A Marahiel
Crystal structure of the termination module of a nonribosomal peptide synthetase.
Science: 2008, 321(5889);659-63
[PubMed:18583577] [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)

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)