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

We cloned the yloO gene and purified a sis-tagged form of its product, the putative protein phosphatase YloO, which we nom designate PrpC. This closel y resembles the human protein phosphatase PP2C, a member of the PPM family, in sequence and predicted secondary structure, PrpC has phosphatase activi ty in vitro against a synthetic substrate, p-nitrophenol phosphate, and end ogenous Bacillus subtilis proteins. The prkC and prpC genes are adjacent on the chromosome, and the phosphorylated form of PrkC is a substrate for Prp C, These findings suggest that PrkC and PrpC may function as a couple in vi vo.