PrpC

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Gene name prpC
Synonyms yloO
Essential no
Product protein phosphatase
Function antagonist of PrkC-dependent phosphorylation
Gene expression levels in SubtiExpress: prpC
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
Sequences Protein DNA DNA_with_flanks
Genetic context
PrpC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PrpC expression.png




























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

Database entries

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

Additional information

Expression and regulation

  • Sigma factor:
  • 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)