Difference between revisions of "Vpr"

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= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[CodY regulon]]}},
 
{{SubtiWiki regulon|[[LexA regulon]]}},
 
{{SubtiWiki regulon|[[LexA regulon]]}},
 
{{SubtiWiki regulon|[[PhoP regulon]]}}
 
{{SubtiWiki regulon|[[PhoP regulon]]}}
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** expressed under conditions of phosphate limitation ([[PhoP]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16291680 PubMed]
 
** expressed under conditions of phosphate limitation ([[PhoP]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16291680 PubMed]
 
** repressed when no DNA damage is present ([[LexA]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16267290 PubMed]
 
** repressed when no DNA damage is present ([[LexA]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16267290 PubMed]
 +
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) {{PubMed|25666135}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[CodY]]: transcription repression {{PubMed|25666135}}
 
** [[PhoP]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/16291680 PubMed]
 
** [[PhoP]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/16291680 PubMed]
 
** [[LexA]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/16267290 PubMed]
 
** [[LexA]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/16267290 PubMed]
Line 144: Line 147:
 
<pubmed>20735481 </pubmed>
 
<pubmed>20735481 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>2106512, 24115457,16291680,16267290,18957862, </pubmed>
+
<pubmed>2106512, 24115457,16291680,16267290,18957862, 25666135</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:26, 11 February 2015

  • Description: minor extracellular serine protease

Gene name vpr
Synonyms ipa-45r
Essential no
Product minor extracellular serine protease
Function protein degradation
Gene expression levels in SubtiExpress: vpr
MW, pI 85 kDa, 5.773
Gene length, protein length 2418 bp, 806 aa
Immediate neighbours ywcI, ywcH
Sequences Protein DNA DNA_with_flanks
Genetic context
Vpr context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Vpr expression.png















Categories containing this gene/protein

utilization of nitrogen sources other than amino acids, proteolysis

This gene is a member of the following regulons

CodY regulon, 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:
  • Modification:
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
    • repressed when no DNA damage is present (LexA) PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 248 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 175 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 224 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

Giulia Barbieri, Birgit Voigt, Dirk Albrecht, Michael Hecker, Alessandra M Albertini, Abraham L Sonenshein, Eugenio Ferrari, Boris R Belitsky
CodY regulates expression of the Bacillus subtilis extracellular proteases Vpr and Mpr.
J Bacteriol: 2015, 197(8);1423-32
[PubMed:25666135] [WorldCat.org] [DOI] (I p)

Susanne Pohl, Gaurav Bhavsar, Joanne Hulme, Alexandra E Bloor, Goksel Misirli, Matthew W Leckenby, David S Radford, Wendy Smith, Anil Wipat, E Diane Williamson, Colin R Harwood, Rocky M Cranenburgh
Proteomic analysis of Bacillus subtilis strains engineered for improved production of heterologous proteins.
Proteomics: 2013, 13(22);3298-308
[PubMed:24115457] [WorldCat.org] [DOI] (I p)

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)