Difference between revisions of "Vpr"

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(Extended information on the protein)
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* '''Operon:''' ''vpr'' {{PubMed|9353933}}
 
* '''Operon:''' ''vpr'' {{PubMed|9353933}}
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=vpr_3907844_3910264_1 vpr] {{PubMed|22383849}}
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* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 08:59, 17 April 2012

  • Description: minor extracellular serine protease

Gene name vpr
Synonyms ipa-45r
Essential no
Product minor extracellular serine protease
Function protein degradation
MW, pI 85 kDa, 5.773
Gene length, protein length 2418 bp, 806 aa
Immediate neighbours ywcI, ywcH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Vpr context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

LexA regulon, PhoP regulon

The gene

Basic information

  • Locus tag: BSU38090

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: peptidase S8 family (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

  • Sigma factor:
  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
    • repressed when no DNA damage is present (LexA) PubMed
  • Additional information:

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

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Nicholas E E Allenby, Nicola O'Connor, Zoltán Prágai, Alan C Ward, Anil Wipat, Colin R Harwood
Genome-wide transcriptional analysis of the phosphate starvation stimulon of Bacillus subtilis.
J Bacteriol: 2005, 187(23);8063-80
[PubMed:16291680] [WorldCat.org] [DOI] (P p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

A Sloma, G A Rufo, C F Rudolph, B J Sullivan, K A Theriault, J Pero
Bacillopeptidase F of Bacillus subtilis: purification of the protein and cloning of the gene.
J Bacteriol: 1990, 172(3);1470-7
[PubMed:2106512] [WorldCat.org] [DOI] (P p)