Difference between revisions of "PrpC"
(→References) |
|||
Line 8: | Line 8: | ||
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloO '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloO '' | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Essential''' || | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || no |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Product''' || protein phosphatase | |style="background:#ABCDEF;" align="center"| '''Product''' || protein phosphatase |
Revision as of 18:21, 11 February 2009
- Description: write here
Gene name | prpC |
Synonyms | yloO |
Essential | no |
Product | protein phosphatase |
Function | |
MW, pI | 27 kDa, 4.355 |
Gene length, protein length | 762 bp, 254 aa |
Immediate neighbours | |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates:
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- 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
- Obuchowski, M., Madec, E., Delattre, D., Boël, G., Iwanicki, A., Foulger, D. and Séror, S. J. 2000. Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family. J. Bacteriol. 182: 5634-5638. PubMed
- Gaidenko TA, Kim TJ, Price CW: (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol, 184:6109-6114. PubMed
- Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed