Protein Family Models

This domain is found N terminal to Pfam:PF07238, therefore named PilZN. Proteins which contain PilZN (also known as YcgR) are know to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias [3]. This domain exhibits a similar structur as PilZ domains comprising a beta-barrel fold but lack the C-terminal alpha-helix [4]. [1]. 16920715. The PilZ domain is a receptor for the second messenger c-di-GMP:. the PilZ domain protein YcgR controls motility in. enterobacteria.. Ryjenkov DA, Simm R, Romling U, Gomelsky M;. J Biol Chem. 2006;281:30310-30314.. [2]. 20303158. Second messenger-mediated adjustment of bacterial swimming. velocity.. Boehm A, Kaiser M, Li H, Spangler C, Kasper CA, Ackermann M,. Kaever V, Sourjik V, Roth V, Jenal U;. Cell. 2010;141:107-116.. [3]. 20346719. The c-di-GMP binding protein YcgR controls flagellar motor. direction and speed to affect chemotaxis by a "backstop brake". mechanism.. Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM;. Mol Cell. 2010;38:128-139.. [4]. 31740493. Structural Conservation and Diversity of PilZ-Related Domains.. Galperin MY, Chou SH;. J Bacteriol. 2020; [Epub ahead of print] (from Pfam)

Date:

2024-08-14

PilZ is a c-di-GMP binding domain [3] found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP [6]. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias [5]. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix [6]. [1]. 8550441. Identification of a novel gene, pilZ, essential for type 4. fimbrial biogenesis in Pseudomonas aeruginosa.. Alm RA, Bodero AJ, Free PD, Mattick JS;. J Bacteriol 1996;178:46-53.. [2]. 16249258. PilZ domain is part of the bacterial c-di-GMP binding protein.. Amikam D, Galperin MY;. Bioinformatics. 2006;22:3-6.. [3]. 16920715. The PilZ domain is a receptor for the second messenger c-di-GMP:. the PilZ domain protein YcgR controls motility in. enterobacteria.. Ryjenkov DA, Simm R, Romling U, Gomelsky M;. J Biol Chem. 2006;281:30310-30314.. [4]. 18034161. The structural basis of cyclic diguanylate signal transduction. by PilZ domains.. Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta-Stogniew. E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt. JF;. EMBO J. 2007;26:5153-5166.. [5]. 20346719. The c-di-GMP binding protein YcgR controls flagellar motor. direction and speed to affect chemotaxis by a "backstop brake". mechanism.. Paul. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

flagellar brake protein, similar to YcgR, which is known to interact with the flagellar switch-complex proteins FliG and FliM, resulting in a reduction of torque generation and induction of CCW motor bias; it does this in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner via its PilZ domain

Date:

2018-10-15