Difference between revisions of "PrpC"

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(References)
(Proteins dephosphorylated by 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
PrpC context.gif



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

  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