Difference between revisions of "PrpC"
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− | <pubmed>19246764,10986276,17693724 | + | <pubmed>19246764,10986276,17693724 , 12399479, 18757537, 15530359</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:45, 7 March 2011
- Description: protein phosphatase
Gene name | prpC |
Synonyms | yloO |
Essential | no |
Product | protein phosphatase |
Function | antagonist of PrkC-dependent phosphorylation |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 27 kDa, 4.355 |
Gene length, protein length | 762 bp, 254 aa |
Immediate neighbours | yloN, prkC |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15760
Phenotypes of a mutant
A prpC mutant is less lytic in late stationary phase. PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: A phosphoprotein + H2O = a protein + phosphate (according to Swiss-Prot)
- 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): divalent cations such as magnesium or manganese
- Effectors of protein activity: inhibited by inorganic phosphate and glycero-2-phosphate PubMed
- Interactions:
- Localization:
Database entries
- UniProt: O34779
- KEGG entry: [2]
- E.C. number: 3.1.3.16
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: OMG401 (aphA3), available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Sandro F F Pereira, Lindsie Goss, Jonathan Dworkin
Eukaryote-like serine/threonine kinases and phosphatases in bacteria.
Microbiol Mol Biol Rev: 2011, 75(1);192-212
[PubMed:21372323]
[WorldCat.org]
[DOI]
(I p)
Original publications
Additional publications: PubMed