| Literature DB >> 10986276 |
M Obuchowski1, E Madec, D Delattre, G Boël, A Iwanicki, D Foulger, S J Séror.
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.Entities:
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Year: 2000 PMID: 10986276 PMCID: PMC111016 DOI: 10.1128/JB.182.19.5634-5638.2000
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490