This family of proteins is found in bacteria and includes YfiR from E. coli. YfiR has been shown to regulate YfiN, a diguanylate cyclase and a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiR may serve as a periplasmic redox sensor that regulates YfiN activity in response to reducing conditions [1, 2]. HmsC in Yersinia Pestis is the orthologue of YfiR from E. coli [3]. HmsC is a periplasmic protein that interacts directly with the periplasmic domain (PD) of HmsD and causes proteolytic degradation of HmsD, which in turn negatively regulates Y. pestis biofilm formation [4]. [1]. 25849887. Crystal structures of YfiR from Pseudomonas aeruginosa in two. redox states.. Yang X, Yang XA, Xu M, Zhou L, Fan Z, Jiang T;. Biochem Biophys Res Commun. 2015;461:14-20.. [2]. 27507823. A Diguanylate Cyclase Acts as a Cell Division Inhibitor in a. Two-Step Response to Reductive and Envelope Stresses.. Kim HK, Harshey RM;. MBio. 2016; [Epub ahead of print]. [3]. 25586342. The Yersinia pestis HmsCDE regulatory system is essential for. blockage of the oriental rat flea (Xenopsylla cheopis), a. classic plague vector.. Bobrov AG, Kirillina O, Vadyvaloo V, Koestler BJ, Hinz AK, Mack. D, Waters CM, Perry RD;. Environ Microbiol. 2015;17:947-959.. [4]. 24192006. HmsC, a periplasmic protein, controls biofilm formation via. repression of HmsD, a diguanylate cyclase in Yersinia pestis.. Ren GX, Yan HQ, Zhu H, Guo XP, Sun YC;. Environ Microbiol. 2014;16:1202-1216. (from Pfam)
- Date:
- 2024-08-14