The Bacillus subtilis regulator protein SpoIIE shares functional and structural similarities with eukaryotic protein phosphatases 2C

Dephosphorylation of SpoIIAA-P by SpoIIE is strictly dependent on the prese nce of the bivalent metal ions Mn2+ or Mg2+ Replacement by Ala of one of th e four Asp residues, invariant in all representatives of protein phosphatas e 2C, completely abolished the SpoIIE phosphatase activity in vitro, whilst replacement of the Asp residues by another acidic amino acid, Glu, had var ying effects on the activities of the resulting mutated proteins. D610E and D795E exhibited some residual activity while D628E and D745E were without enzymatic activity. The results suggest that the functional model in which metal-associated water molecules are involved in the dephosphorylation reac tion catalyzed by human protein phosphatase 2C alpha can also be applied to the bacterial protein phosphatase 2C-like protein. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.