Difference between revisions of "Bpr"
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* '''Locus tag:''' BSU15300  | * '''Locus tag:''' BSU15300  | ||
| + | |||
| + | [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  
  This image was kindly provided by SubtiList 
 | |
Contents
Categories containing this gene/protein
utilization of nitrogen sources other than amino acids, proteolysis
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15300
 
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:
 
- Localization: secreted (according to Swiss-Prot), extracellular (signal peptide) PubMed
 
Database entries
- Structure:
 
- UniProt: P16397
 
- KEGG entry: [2]
 
- E.C. number:
 
Additional information
Expression and regulation
- Operon:
 
-  Regulation: 
- repressed by glucose (7.7-fold) 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)
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)
