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Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.

ABSTRACT: We cloned the yloO 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 endogenous Bacillus subtilis proteins. The prkC and prpC 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.

SUBMITTER: Obuchowski M

PROVIDER: S-EPMC111016 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature

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Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.

Obuchowski M M Madec E E Delattre D D Boël G G Iwanicki A A Foulger D D Séror S J SJ

Journal of bacteriology 20001001 19

We cloned the yloO 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 endogenous Bacillus subtilis proteins. The prkC and prpC genes are adjacent on the chromosome, and the phosphorylated form of Pr ...[more]

PMID: 10986276

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