Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions.

Abstract

During the past decade, numerous Mn2+-dependent protein serine, threonine and/or tyrosine phosphatases (O-phosphatases) from prokaryotes have been characterized. Based on their amino acid sequences, they belong to PPP, PPM or PHP superfamilies. Both the PPP and PPM families of protein phosphatases are metalloenzymes which active centers contain two metal ions that function as cofactors. Results from sequence analysis also suggest that PHP family protein phosphatase is a metalloenzyme. The identified functions for PPP family protein phosphatases from different prokaryotic organisms include regulation of stress-response, nitrogen fixation and vegetative growth. At least one phosphatase, PrpB from Escherichia coli, is also implicated in bacterial pathogenesis. Prokaryotic PPM family protein phosphatases are involved in controlling spore formation, stress-response, cell density during stationary phase, carbon and nitrogen assimilation, vegetative growth, development of fruiting bodies and cell segregation. The function of CpsB, a PHP family protein tyrosine phosphatase from Streptococcus pneumonia, is to regulate biosynthesis of capsular polysaccharide, an important virulence determinant. Thus, this group of functionally diverse protein phosphatases plays an important role in prokaryotes. Discovery of Mn2+-dependent prokaryotic protein O-phosphatases and their functions also contributes to new insight into Mn2+ homeostasis and many roles played by Mn2+ and protein O-phosphorylation in prokaryotic cells.