Structural highlights
Function
MTDRP_MYCTU Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon (PubMed:30642988). Possesses both phosphatase and kinase activities (PubMed:30642988, PubMed:19700407). The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity (PubMed:19700407).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Greenstein AE, Hammel M, Cavazos A, Alber T. Interdomain communication in the Mycobacterium tuberculosis environmental phosphatase Rv1364c. J Biol Chem. 2009 Oct 23;284(43):29828-35. PMID:19700407 doi:10.1074/jbc.M109.056168
- ↑ Misra R, Menon D, Arora G, Virmani R, Gaur M, Naz S, Jaisinghani N, Bhaduri A, Bothra A, Maji A, Singhal A, Karwal P, Hentschker C, Becher D, Rao V, Nandicoori VK, Gandotra S, Singh Y. Tuning the Mycobacterium tuberculosis Alternative Sigma Factor SigF through the Multidomain Regulator Rv1364c and Osmosensory Kinase Protein Kinase D. J Bacteriol. 2019 Mar 13;201(7):e00725-18. PMID:30642988 doi:10.1128/JB.00725-18
