Difference between revisions of "Vpr"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=vpr_3907844_3910264_1 vpr] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=vpr_3907844_3910264_1 vpr] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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<pubmed>20735481 </pubmed> | <pubmed>20735481 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>2106512,,16291680,16267290,18957862, </pubmed> | + | <pubmed>2106512, 24115457,16291680,16267290,18957862, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:55, 20 February 2014
- 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
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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: 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:
- Localization:
- extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: P29141
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: vpr PubMed
- Regulation:
- 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
Original publications
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)
