Difference between revisions of "PrpC"
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=== Proteins dephosphorylated by PrpC === | === Proteins dephosphorylated by PrpC === | ||
| − | [[CpgA]], [[tufA | EF-Tu]], [[YezB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed] | + | [[CpgA]], [[tufA | EF-Tu]], [[YezB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed], [[ptsH | HPr]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed] |
| − | |||
=== Extended information on the protein === | === Extended information on the protein === | ||
Revision as of 10:00, 3 March 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 | yloN, prkC |
| 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):
Proteins dephosphorylated by PrpC
CpgA, EF-Tu, YezB PubMed, HPr PubMed
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
- Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, Séror SJ (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155: 932-943. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
