Difference between revisions of "SrfAA"
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=== Additional information=== | === Additional information=== | ||
* A mutation was found in this gene after evolution under relaxed selection for sporulation {{PubMed|21821766}} | * A mutation was found in this gene after evolution under relaxed selection for sporulation {{PubMed|21821766}} | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' phosphorylation on Ser-1006 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed] | * '''Modification:''' phosphorylation on Ser-1006 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed] | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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<pubmed>20735481 </pubmed> | <pubmed>20735481 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>8288534,8387999,1938922,16166527,17227471,8825779, 8830686,18763711 17218307, 17190806 1715856 19605685 19826092 12642660 20148996 16091051 20797616 20525796 21821766 23012477 22511326,20817675,15066026</pubmed> | + | <pubmed>8288534,8387999,1938922,16166527,17227471,8825779, 8830686,18763711 17218307, 17190806 1715856 19605685 19826092 12642660 20148996 16091051 20797616 20525796 21821766 23012477 22511326,20817675,15066026 24425772 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:18, 17 January 2014
- 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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:
- Modification: phosphorylation on Ser-1006 PubMed
- Effectors of protein activity:
- Localization: membrane PubMed
Database entries
- Structure:
- UniProt: P27206
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
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
Anna Oslizlo, Polonca Stefanic, Iztok Dogsa, Ines Mandic-Mulec
Private link between signal and response in Bacillus subtilis quorum sensing.
Proc Natl Acad Sci U S A: 2014, 111(4);1586-91
[PubMed:24425772]
[WorldCat.org]
[DOI]
(I p)
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)
Daniel B Kearns, Frances Chu, Rivka Rudner, Richard Losick
Genes governing swarming in Bacillus subtilis and evidence for a phase variation mechanism controlling surface motility.
Mol Microbiol: 2004, 52(2);357-69
[PubMed:15066026]
[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)
