PrpC

• Description: protein phosphatase
  
  

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: prpC
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification

The gene

Basic information

• Locus tag: BSU15760

Phenotypes of a mutant

A prpC mutant is less lytic in late stationary phase. PubMed

Database entries

• BsubCyc: BSU15760
• BsubCyc: BSU15760

• DBTBS entry: no entry

• SubtiList entry: [1]

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, YkwC PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors: divalent cations such as magnesium or manganese

• Effectors of protein activity: inhibited by inorganic phosphate and glycero-2-phosphate PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU15760
• BsubCyc: BSU15760

• Structure: 1TXO (from Mycobacterium tuberculosis, 34% identity, 54% similarity) PubMed

• UniProt: O34779

• KEGG entry: [2]

• E.C. number: 3.1.3.16

Expression and regulation

• Operon: prpC-prkC-cpgA PubMed

• Expression browser: prpC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 459 PubMed

Biological materials

• Mutant: OMG401 (aphA3), available in the Stülke lab
  • 1A962 (no resistance), PubMed, available at BGSC
  • 1A964 (no resistance), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Vaishnavi Ravikumar, Lei Shi, Karsten Krug, Abderahmane Derouiche, Carsten Jers, Charlotte Cousin, Ahasanul Kobir, Ivan Mijakovic, Boris Macek
Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.
Mol Cell Proteomics: 2014, 13(8);1965-78
[PubMed:24390483] [WorldCat.org] [DOI] (I p)

Gunjan Arora, Andaleeb Sajid, Mary Diana Arulanandh, Richa Misra, Anshika Singhal, Santosh Kumar, Lalit K Singh, Abid R Mattoo, Rishi Raj, Souvik Maiti, Sharmila Basu-Modak, Yogendra Singh
Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.
Biometals: 2013, 26(5);715-30
[PubMed:23793375] [WorldCat.org] [DOI] (I p)

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)

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)

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)