4etn

Structural highlights

Function

PAP_BACSU Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.^{[1] [2] [3]}

See Also

• Tyrosine phosphatase 3D structures

References

1. ↑ Elsholz AK, Turgay K, Michalik S, Hessling B, Gronau K, Oertel D, Mader U, Bernhardt J, Becher D, Hecker M, Gerth U. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Proc Natl Acad Sci U S A. 2012 May 8;109(19):7451-6. doi:, 10.1073/pnas.1117483109. Epub 2012 Apr 19. PMID:22517742 doi:http://dx.doi.org/10.1073/pnas.1117483109
2. ↑ Fuhrmann J, Mierzwa B, Trentini DB, Spiess S, Lehner A, Charpentier E, Clausen T. Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria. Cell Rep. 2013 Jun 27;3(6):1832-9. doi: 10.1016/j.celrep.2013.05.023. Epub 2013, Jun 13. PMID:23770242 doi:10.1016/j.celrep.2013.05.023
3. ↑ Schmidt A, Trentini DB, Spiess S, Fuhrmann J, Ammerer G, Mechtler K, Clausen T. Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response. Mol Cell Proteomics. 2014 Feb;13(2):537-50. doi: 10.1074/mcp.M113.032292. Epub, 2013 Nov 20. PMID:24263382 doi:http://dx.doi.org/10.1074/mcp.M113.032292