Difference between revisions of "PrpC"

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* '''Structure:'''
 
* '''Structure:'''
  
* '''Swiss prot entry:'''
+
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34779 O34779]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15760]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15760]

Revision as of 22:24, 4 May 2009

  • Description: protein phosphatase

Gene name prpC
Synonyms yloO
Essential no
Product protein phosphatase
Function antagonist of PrkC-dependent phosphorylation
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
PrpC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

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:
  • 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:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • 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

  1. 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
  2. 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
  3. 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
  4. 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
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed