Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide.

@article{Diaz2012BacillusSR,
  title={Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide.},
  author={Alejandra R Diaz and Leighton J Core and Min Jiang and Michela Morelli and Christina H. Chiang and Hendrik Szurmant and Marta Perego},
  journal={Journal of bacteriology},
  year={2012},
  volume={194 6},
  pages={1378-88}
}
Rap proteins in Bacillus subtilis regulate the phosphorylation level or the DNA-binding activity of response regulators such as Spo0F, involved in sporulation initiation, or ComA, regulating competence development. Rap proteins can be inhibited by specific peptides generated by the export-import processing pathway of the Phr proteins. Rap proteins have a modular organization comprising an amino-terminal alpha-helical domain connected to a domain formed by six tetratricopeptide repeats (TPR). In… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS

From This Paper

Topics from this paper.
11 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…