SrfAC

• Description: surfactin synthetase / competence
  
  

Gene name	srfAC
Synonyms	comL
Essential	no
Product	surfactin synthetase / competence
Function	antibiotic synthesis
Gene expression levels in SubtiExpress: srfAC
MW, pI	143 kDa, 4.97
Gene length, protein length	3822 bp, 1274 aa
Immediate neighbours	comS, srfAD
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

This gene is a member of the following regulons

Abh regulon, CodY regulon, ComA regulon, PerR regulon, Spx regulon

The gene

Basic information

• Locus tag: BSU03510

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Structure: 2VSQ

• UniProt: Q08787

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: srfAA-srfAB-comS-srfAC-srfAD PubMed

• Expression browser: srfAC PubMed

• Sigma factor: SigA PubMed

• 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

• Regulatory mechanism:
  • CodY: transcription repression PubMed
  • ComA: transcription activation PubMed
  • PerR: transcription activation PubMed
  • Spx: transcription repression PubMed
  • Abh: transcription repressionPubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Lixia Liu, Zhaoxin Lu, Fengxia Lv, Chong Zhang, Xiaomei Bie
[Activity of the SrfAC-A domain from Bacillus subtilis fmbj].
Wei Sheng Wu Xue Bao: 2013, 53(5);437-43
[PubMed:23957147] [WorldCat.org] (P p)

Ju Jung, Kyung Ok Yu, Ahmad Bazli Ramzi, Se Hoon Choe, Seung Wook Kim, Sung Ok Han
Improvement of surfactin production in Bacillus subtilis using synthetic wastewater by overexpression of specific extracellular signaling peptides, comX and phrC.
Biotechnol Bioeng: 2012, 109(9);2349-56
[PubMed:22511326] [WorldCat.org] [DOI] (I p)

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)