Difference between revisions of "Mpr"
| Line 59: | Line 59: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| − | |||
=The protein= | =The protein= | ||
| Line 77: | Line 74: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| Line 108: | Line 105: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mpr_245190_246131_1 mpr] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mpr_245190_246131_1 mpr] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' repressed by casamino acids {{PubMed|12107147}} | * '''Regulation:''' repressed by casamino acids {{PubMed|12107147}} | ||
| Line 138: | Line 135: | ||
<pubmed>20735481 </pubmed> | <pubmed>20735481 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>15375126,,18957862 12107147, </pubmed> | + | <pubmed>15375126, 24115457,18957862 12107147, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:55, 20 February 2014
- Description: extracellular metalloprotease
| Gene name | mpr |
| Synonyms | |
| Essential | no |
| Product | extracellular metalloprotease |
| Function | protein degradation |
| Gene expression levels in SubtiExpress: mpr | |
| MW, pI | 33 kDa, 8.967 |
| Gene length, protein length | 939 bp, 313 aa |
| Immediate neighbours | purT, ybfJ |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
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: BSU02240
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 S1B 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: P39790
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation: repressed by casamino acids 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
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)
Chi Hye Park, Sang Jun Lee, Sung Gu Lee, Weon Sup Lee, Si Myung Byun
Hetero- and autoprocessing of the extracellular metalloprotease (Mpr) in Bacillus subtilis.
J Bacteriol: 2004, 186(19);6457-64
[PubMed:15375126]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
