SrfAA

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  • Description: surfactin synthetase / competence

Gene name srfAA
Synonyms comL
Essential no
Product surfactin synthetase / competence
Function antibiotic synthesis
Gene expression levels in SubtiExpress: srfAA
MW, pI 401 kDa, 4.871
Gene length, protein length 10764 bp, 3588 aa
Immediate neighbours hxlR, srfAB
Sequences Protein DNA DNA_with_flanks
Genetic context
SrfAA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SrfAA expression.png















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: BSU03480

Phenotypes of a mutant

  • altered cell death pattern in colonies PubMed
  • reduced swarming of srfAA mutant of B. subtilis NCIB3610 PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed


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-1006 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • 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

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)

Original publications

Munehiro Asally, Mark Kittisopikul, Pau Rué, Yingjie Du, Zhenxing Hu, Tolga Çağatay, Andra B Robinson, Hongbing Lu, Jordi Garcia-Ojalvo, Gürol M Süel
Localized cell death focuses mechanical forces during 3D patterning in a biofilm.
Proc Natl Acad Sci U S A: 2012, 109(46);18891-6
[PubMed:23012477] [WorldCat.org] [DOI] (I 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)

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [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)

Femke I Kraas, Verena Helmetag, Melanie Wittmann, Matthias Strieker, Mohamed A Marahiel
Functional dissection of surfactin synthetase initiation module reveals insights into the mechanism of lipoinitiation.
Chem Biol: 2010, 17(8);872-80
[PubMed:20797616] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

F Coutte, V Leclère, M Béchet, J-S Guez, D Lecouturier, M Chollet-Imbert, P Dhulster, P Jacques
Effect of pps disruption and constitutive expression of srfA on surfactin productivity, spreading and antagonistic properties of Bacillus subtilis 168 derivatives.
J Appl Microbiol: 2010, 109(2);480-491
[PubMed:20148996] [WorldCat.org] [DOI] (I p)

Thomas E Angelini, Marcus Roper, Roberto Kolter, David A Weitz, Michael P Brenner
Bacillus subtilis spreads by surfing on waves of surfactant.
Proc Natl Acad Sci U S A: 2009, 106(43);18109-13
[PubMed:19826092] [WorldCat.org] [DOI] (I p)

Daniel López, Hera Vlamakis, Richard Losick, Roberto Kolter
Paracrine signaling in a bacterium.
Genes Dev: 2009, 23(14);1631-8
[PubMed:19605685] [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)

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)

A Luttinger, J Hahn, D Dubnau
Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis.
Mol Microbiol: 1996, 19(2);343-56
[PubMed:8825779] [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 Roggiani, D Dubnau
ComA, a phosphorylated response regulator protein of Bacillus subtilis, binds to the promoter region of srfA.
J Bacteriol: 1993, 175(10);3182-7
[PubMed:8387999] [WorldCat.org] [DOI] (P p)

J Hahn, D Dubnau
Growth stage signal transduction and the requirements for srfA induction in development of competence.
J Bacteriol: 1991, 173(22);7275-82
[PubMed:1938922] [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)

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