Open AccessCharacterization of PrpC fromBacillus subtilis, a Member of the PPM Phosphatase Family
Author(s) -
Michał Obuchowski,
Edwige Madec,
Delphine Delattre,
Grégory Boël,
Adam Iwanicki,
D. Foulger,
Simone J. Séror
Publication year - 2000
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.182.19.5634-5638.2000
Subject(s) - bacillus subtilis , biology , phosphatase , biochemistry , phosphorylation , gene , microbiology and biotechnology , gene product , in vitro , peptide sequence , alkaline phosphatase , protein phosphatase 2 , bacillus (shape) , enzyme , genetics , bacteria , gene expression
We cloned theyloO gene and purified a His-tagged form of its product, the putative protein phosphatase YloO, which we now designate PrpC. This closely resembles the human protein phosphatase PP2C, a member of the PPM family, in sequence and predicted secondary structure. PrpC has phosphatase activity in vitro against a synthetic substrate,p -nitrophenol phosphate, and endogenousBacillus subtilis proteins. TheprkC andprpC genes are adjacent on the chromosome, and the phosphorylated form of PrkC is a substrate for PrpC. These findings suggest that PrkC and PrpC may function as a couple in vivo.