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

@article{Schrter1999TheBS,
  title={The Bacillus subtilis regulator protein SpoIIE shares functional and structural similarities with eukaryotic protein phosphatases 2C.},
  author={Renate Schr{\"o}ter and Susanne Schlisio and Isabelle S Lucet and Michael D. Yudkin and Rainer Borriss},
  journal={FEMS microbiology letters},
  year={1999},
  volume={174 1},
  pages={
          117-23
        }
}
Dephosphorylation of SpoIIAA-P by SpoIIE is strictly dependent on the presence of the bivalent metal ions Mn2+ or Mg2+. Replacement by Ala of one of the four Asp residues, invariant in all representatives of protein phosphatase 2C, completely abolished the SpoIIE phosphatase activity in vitro, whilst replacement of the Asp residues by another acidic amino acid, Glu, had varying effects on the activities of the resulting mutated proteins. D610E and D795E exhibited some residual activity while… CONTINUE READING

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Solution structure of SpoIIAA, a phosphorytable component of the system that regulates trans-cription factor c of Bacillus subtilis

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Solution structure of SpoIIAA , a phosphorytable component of the system that regulates transcription factor c F of Bacillus subtilis

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