PrpC

From SubtiWiki
Revision as of 11:22, 14 June 2009 by Sroppel (talk | contribs)
Jump to: navigation, search
  • 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
PrpC context.gif
This image was kindly provided by SubtiList



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

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • 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

Cédric Absalon, Michal Obuchowski, Edwige Madec, Delphine Delattre, I Barry Holland, Simone J Séror
CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 3);932-943
[PubMed:19246764] [WorldCat.org] [DOI] (P p)

Kalpana D Singh, Matthias H Schmalisch, Jörg Stülke, Boris Görke
Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.
J Bacteriol: 2008, 190(21);7275-84
[PubMed:18757537] [WorldCat.org] [DOI] (I p)

Adam Iwanicki, Krzysztof Hinc, Simone Seror, Grzegorz Wegrzyn, Michal Obuchowski
Transcription in the prpC-yloQ region in Bacillus subtilis.
Arch Microbiol: 2005, 183(6);421-30
[PubMed:16025310] [WorldCat.org] [DOI] (P p)

Tatiana A Gaidenko, Tae-Jong Kim, Chester W Price
The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells.
J Bacteriol: 2002, 184(22);6109-14
[PubMed:12399479] [WorldCat.org] [DOI] (P p)

M Obuchowski, E Madec, D Delattre, G Boël, A Iwanicki, D Foulger, S J Séror
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
J Bacteriol: 2000, 182(19);5634-8
[PubMed:10986276] [WorldCat.org] [DOI] (P p)


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