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
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

• 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)