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The spo0E locus of Bacillus subtilis codes for anegative regulator of sporulation that, when overproduced, represses sporulationand, if deleted, results in inappropriate timing of sporulation. The product ofthis locus, Spo0E, was purified and found to be a protein phosphatase, whichspecifically dephosphorylated the sporulation transcription factor Spo0A-P,converting it to an inactive form. Spo0E was not significantly active as aphosphatase on other components of the phosphorelay signal-transduction pathwayproducing Spo0A-P. A mutant Spo0E protein that results in sporulation deficiencywas purified and found to be hyperactive as a phosphatase. The Spo0E phosphatasemay provide an additional control point for environmental, metabolic, orcell-cycle regulation of phosphate flow in the phosphorelay. These resultsreinforce the concept that the phosphorelay is subject to a host of positive andnegative signals for sporulation that are recognized and interpreted as signalintegration circuit that has the role of regulating the cellular level of activephosphorylated Spo0A sporulation transcription factor.

Deactivation of the sporulation transcription factorSpo0A by the Spo0E protein phosphatase.