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: 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 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

• 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

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

• 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:

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

Additional publications: PubMed