Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors.

We have devised a coupled radiochemical assay for detecting phosphatidylglycerolphosphate (PGP) phosphatase activity in Escherichia coli colonies immobilized on filter paper. There appeared to be at least two enzymes capable of dephosphorylating PGP, as judged by the characterization of mutations in two genes designated pgpA and pgpB. The former is located near min 10 and is cotransducible with proC and dnaZ. The latter is situated near min 28 and is closely linked to cysB. The available mutant alleles of pgpA reduced the specific activity of PGP phosphatase in crude extracts by about 30%, but they had no effect on phosphatidic acid (or lysophosphatidic acid) phosphatase. Mutants altered in the pgpB locus inactivated most of the residual PGP phosphatase activity present in single-step pgpA mutants, and the level of phosphatidic acid phosphatase was also reduced 20-fold. The available mutations in pgpA and pgpB elevated the cellular PGP pool by 10- to 50-fold. The maximal PGP levels never exceeded 5%, and these strains were not conditionally lethal. The simplest interpretation of our findings is that there are at least two membrane-associated phosphatases in E. coli, both distinct from alkaline phosphatase. The pgpA gene product is specific for PGP, whereas the pgpB gene product also acts on phosphatidic acid and lysophosphatidic acid.