prpC

168

protein phosphatase

Locus: BSU_15760

Molecular weight: 27.52 kDa

Isoelectric point: 4.36

Protein length: 254 aa

Gene length: 765 bp

Function: antagonist of PrkC-dependent phosphorylation

Product: protein phosphatase

Essential: no

E.C.: 3.1.3.16

Synonyms: prpC, yloO

Genomic Context

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Categories containing this gene/protein

Information processing, Protein synthesis, modification and degradation, Protein modification, Protein phosphatases

List of homologs in different organisms, belongs to COG0631 (Galperin et al., 2021)

Gene

Coordinates: 1,650,384  1,651,148

Phenotypes of a mutant

A prpC mutant is less lytic in late stationary phase. PubMed
inactivation of ''prpC'' reduces sporulation efficiency to 50.7% that of wild type cells PubMed

The protein

Catalyzed reaction/ biological activity

dephosphorylation of EF-tu]]-Thr63-P PubMed
H₂O + O-phospho-L-seryl-[protein] --> L-seryl-[protein] + phosphate (according to UniProt)
H₂O + O-phospho-L-threonyl-[protein] --> L-threonyl-[protein] + phosphate (according to UniProt)

Domains

PPM-type phosphatase domain (aa 2-243) (according to UniProt)

Cofactors

divalent cations such as magnesium or manganese

Structure

1TXO (PDB) (from Mycobacterium tuberculosis, 34% identity, 54% similarity) PubMed
O34779 (AlphaFold)

Effectors of protein activity

inhibited by inorganic phosphate and glycero-2-phosphate PubMed

Expression and Regulation

Operons

Genes: prpC-prkC-cpgA-rpeA-yloS

Description: PubMed

Biological materials

Mutant

MGNA-B133 (yloO::erm), available at the NBRP B. subtilis, Japan
OMG401 (aphA3), available in Jörg Stülke's lab
1A962 (no resistance), PubMed, available at BGSC
1A964 (no resistance), PubMed, available at BGSC
BKE15760 (prpC::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_TTTTAAGGCTGTTAACAACC,  downstream forward: _UP4_CAAGTTGAAGAGGGTGAAGA
BKK15760 (prpC::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_TTTTAAGGCTGTTAACAACC,  downstream forward: _UP4_CAAGTTGAAGAGGGTGAAGA

References

Reviews

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Original Publications

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