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VpsT-like, receiver domain
This domain is found at the N-terminal end of the transcriptional regulator VC_A0952 from Vibrio cholerae (VpsT), in CsgD from Salmonella typhimurium and other proteins predominantly found in proteobacteria. VpsT inversely regulates biofilm formation and motility. Like CsgD, it is organised into two domains: an N-terminal regulatory receiver domain (REC, this entry) and a C-terminal helix-turn-helix domain (Pfam:PF00196). This domain shows five alpha- helices and five beta-strands, with the beta-strands stabilising as a parallel beta-sheet surrounded by the alpha-helices [1,2]. Paper describing PDB structure 3kln. [1]. 20150502. Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Krasteva PV, Fong JC, Shikuma NJ, Beyhan S, Navarro MV, Yildiz FH, Sondermann H;. Science. 2010;327:866-868. Paper describing PDB structure 5xp0. [2]. 28758290. Crystal structure of master biofilm regulator CsgD regulatory domain reveals an atypical receiver domain. Wen Y, Ouyang Z, Devreese B, He W, Shao Y, Lu W, Zheng F;. Protein Sci. 2017;26:2073-2082. (from Pfam)
LuxR C-terminal-related transcriptional regulator
biofilm master transcriptional regulator CsgD
CsgD activates operons involved in the biosynthesis of curli fimbriae, and also of cellulose, for biofilm formation. The N-terminal domain resembles response regulator receiver domains, but is atypical, and no cognate histidine kinase has been indentified.
LuxR family transcriptional regulator
LuxR family transcriptional regulator similar to HTH-type transcriptional regulator EcpR, which regulates the expression of the ecp operon that is involved in early-stage biofilm development and host cell recognition
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