PrpC

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Revision as of 09:45, 7 March 2011 by Jstuelk (talk | contribs) (Original publications)
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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







Categories containing this gene/protein

protein modification

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

  • Structure: 1TXO (from Mycobacterium tuberculosis, 34% identity, 54% similarity) PubMed
  • KEGG entry: [2]

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

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)

Kalpana D Singh, Sven Halbedel, Boris Görke, Jörg Stülke
Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC.
J Mol Microbiol Biotechnol: 2007, 13(1-3);165-71
[PubMed:17693724] [WorldCat.org] [DOI] (P p)

Kristi E Pullen, Ho-Leung Ng, Pei-Yi Sung, Matthew C Good, Stephen M Smith, Tom Alber
An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase.
Structure: 2004, 12(11);1947-54
[PubMed:15530359] [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)