SrfAD

• Description: surfactin synthetase / competence
  
  

Gene name	srfAD
Synonyms	comL
Essential	no
Product	surfactin synthetase / competence
Function	antibiotic synthesis
MW, pI	27 kDa, 5.22
Gene length, protein length	726 bp, 242 aa
Immediate neighbours	srfAC, ycxA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU03520

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: thioesterase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2RON, 2K2Q

• UniProt: Q08788

• KEGG entry: [3]

• E.C. number:

Expression and regulation

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alexander Koglin, Frank Löhr, Frank Bernhard, Vladimir V Rogov, Dominique P Frueh, Eric R Strieter, Mohammad R Mofid, Peter Güntert, Gerhard Wagner, Christopher T Walsh, Mohamed A Marahiel, Volker Dötsch
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.
Nature: 2008, 454(7206);907-11
[PubMed:18704089] [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)

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)

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)