Difference between revisions of "Bpr"

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* '''Locus tag:''' BSU15300
 
* '''Locus tag:''' BSU15300
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[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bpr_1599283_1603584_1 Expression]
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 09:06, 25 January 2012

  • Description: bacillopeptidase F

Gene name bpr
Synonyms bpf
Essential no
Product bacillopeptidase F
Function protein degradation
MW, pI 154 kDa, 4.976
Gene length, protein length 4299 bp, 1433 aa
Immediate neighbours ftsZ, spoIIGA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Bpr context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of nitrogen sources other than amino acids, proteolysis

This gene is a member of the following regulons

DegU regulon

The gene

Basic information

  • Locus tag: BSU15300

Expression

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

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: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • repressed by glucose (7.7-fold) PubMed
  • Regulatory mechanism:
  • 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)

Jan-Willem Veening, Oleg A Igoshin, Robyn T Eijlander, Reindert Nijland, Leendert W Hamoen, Oscar P Kuipers
Transient heterogeneity in extracellular protease production by Bacillus subtilis.
Mol Syst Biol: 2008, 4;184
[PubMed:18414485] [WorldCat.org] [DOI] (I p)

Kensuke Tsukahara, Mitsuo Ogura
Characterization of DegU-dependent expression of bpr in Bacillus subtilis.
FEMS Microbiol Lett: 2008, 280(1);8-13
[PubMed:18194340] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [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)