Difference between revisions of "SigV"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sigV_2769850_2770350_1 sigV] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sigV_2769850_2770350_1 sigV] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigV]] {{PubMed|21856855}}
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* '''[[Sigma factor]]:''' [[SigV]] {{PubMed|21856855}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
'''Additional publications:''' {{PubMed|20817771, 21926231,21856855}}
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<pubmed>14993308,16274938,17675383,19745567 22362028 23687273 20817771, 21926231,21856855</pubmed>
<pubmed>14993308,16274938,17675383,19745567 22362028</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:30, 27 May 2013

Gene name sigV
Synonyms
Essential no
Product RNA polymerase ECF-type sigma factor SigV
Function response to lysozyme
Gene expression levels in SubtiExpress: sigV
Interactions involving this protein in SubtInteract: SigV
MW, pI 19 kDa, 9.037
Gene length, protein length 498 bp, 166 aa
Immediate neighbours yrhO, rsiV
Sequences Protein DNA DNA_with_flanks
Genetic context
SigV context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SigV expression.png















Categories containing this gene/protein

transcription, sigma factors and their control, cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigV regulon

The SigV regulon:

The gene

Basic information

  • Locus tag: BSU27120

Phenotypes of a mutant

    • increased sensitivity to lysozyme, this can be suppressed by overexpression of oatA PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ECF subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Thomas Wiegert, University of Bayreuth, Germany Homepage

Your additional remarks

References

Jessica L Hastie, Kyle B Williams, Craig D Ellermeier
The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV.
J Bacteriol: 2013, 195(14);3135-44
[PubMed:23687273] [WorldCat.org] [DOI] (I p)

Satoshi Matsuoka, Minako Chiba, Yu Tanimura, Michihiro Hashimoto, Hiroshi Hara, Kouji Matsumoto
Abnormal morphology of Bacillus subtilis ugtP mutant cells lacking glucolipids.
Genes Genet Syst: 2011, 86(5);295-304
[PubMed:22362028] [WorldCat.org] [DOI] (I p)

Veronica Guariglia-Oropeza, John D Helmann
Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids.
J Bacteriol: 2011, 193(22);6223-32
[PubMed:21926231] [WorldCat.org] [DOI] (I p)

Theresa D Ho, Jessica L Hastie, Peter J Intile, Craig D Ellermeier
The Bacillus subtilis extracytoplasmic function σ factor σ(V) is induced by lysozyme and provides resistance to lysozyme.
J Bacteriol: 2011, 193(22);6215-22
[PubMed:21856855] [WorldCat.org] [DOI] (I p)

Yun Luo, Kei Asai, Yoshito Sadaie, John D Helmann
Transcriptomic and phenotypic characterization of a Bacillus subtilis strain without extracytoplasmic function σ factors.
J Bacteriol: 2010, 192(21);5736-45
[PubMed:20817771] [WorldCat.org] [DOI] (I p)

Michihiro Hashimoto, Hiroaki Takahashi, Yoshinori Hara, Hiroshi Hara, Kei Asai, Yoshito Sadaie, Kouji Matsumoto
Induction of extracytoplasmic function sigma factors in Bacillus subtilis cells with membranes of reduced phosphatidylglycerol content.
Genes Genet Syst: 2009, 84(3);191-8
[PubMed:19745567] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Anna-Barbara Hachmann, John D Helmann
Regulatory overlap and functional redundancy among Bacillus subtilis extracytoplasmic function sigma factors.
J Bacteriol: 2007, 189(19);6919-27
[PubMed:17675383] [WorldCat.org] [DOI] (P p)

Stephan Zellmeier, Claudia Hofmann, Sylvia Thomas, Thomas Wiegert, Wolfgang Schumann
Identification of sigma(V)-dependent genes of Bacillus subtilis.
FEMS Microbiol Lett: 2005, 253(2);221-9
[PubMed:16274938] [WorldCat.org] [DOI] (P p)

Mika Yoshimura, Kei Asai, Yoshito Sadaie, Hirofumi Yoshikawa
Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors.
Microbiology (Reading): 2004, 150(Pt 3);591-599
[PubMed:14993308] [WorldCat.org] [DOI] (P p)