The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport.

@article{MartinVerstraete1999TheQM,
  title={The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport.},
  author={Isabelle Martin-Verstraete and Anne Galinier and Emmanuelle Darbon and Yves Quentin and M C Kilhoffer and V{\'e}ronique Charrier and Jacques Haiech and George N. Rapoport and Sigr{\'u}n Hreinsd{\'o}ttir},
  journal={Microbiology},
  year={1999},
  volume={145 ( Pt 11)},
  pages={
          3195-204
        }
}
Crh of Bacillus subtilis exhibits 45% sequence identity when compared to histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS). Crh can be phosphorylated by ATP at the regulatory Ser-46 and similar to P-Ser-HPr, P-Ser-Crh plays a role in carbon-catabolite repression. The sequence around the phosphorylatable Ser-46 in Crh exhibits strong similarity to the corresponding sequence of HPr of Gram-positive and a few Gram… CONTINUE READING

Citations

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SHOWING 1-10 OF 11 CITATIONS

Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh.

  • Journal of molecular microbiology and biotechnology
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CcpA-dependent carbon catabolite repression in bacteria.

  • Microbiology and molecular biology reviews : MMBR
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