Protein Family Models

GAPES3 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases/phosphodiesterases, including the c-di-GMP phosphodiesterases PdeK (YhjK) of Escherichia coli and HmsP of Yersinia pestis [1,2,3]. [1]. 15935569. The phosphodiesterase activity of the HmsP EAL domain is. required for negative regulation of biofilm formation in. Yersinia pestis.. Bobrov AG, Kirillina O, Perry RD;. FEMS Microbiol Lett. 2005;247:123-130.. [2]. 21219468. Systematic analysis of cyclic di-GMP signalling enzymes and. their role in biofilm formation and virulence in Yersinia. pestis.. Bobrov AG, Kirillina O, Ryjenkov DA, Waters CM, Price PA,. Fetherston JD, Mack D, Goldman WE, Gomelsky M, Perry RD;. Mol Microbiol. 2011;79:533-551.. [3]. 26148715. Systematic Nomenclature for GGDEF and EAL Domain-Containing. Cyclic Di-GMP Turnover Proteins of Escherichia coli.. Hengge R, Galperin MY, Ghigo JM, Gomelsky M, Green J, Hughes KT,. Jenal U, Landini P;. J Bacteriol. 2015;198:7-11. (from Pfam)

Date:

2024-08-14

This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain [1] and has diguanylate cyclase activity [4]. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyses the cyclisation of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule [6,7,8]. [1]. 11119645. GGDEF domain is homologous to adenylyl cyclase.. Pei J, Grishin NV;. Proteins 2001;42:210-216.. [2]. 11557134. Novel domains of the prokaryotic two-component signal. transduction systems.. Galperin MY, Nikolskaya AN, Koonin EV;. FEMS Microbiol Lett 2001;203:11-21.. [3]. 15063857. Cyclic di-guanosine-monophosphate comes of age: a novel. secondary messenger involved in modulating cell surface. structures in bacteria?.. Jenal U;. Curr Opin Microbiol 2004;7:185-191.. [4]. 15075296. Cell cycle-dependent dynamic localization of a bacterial. response regulator with a novel di-guanylate cyclase output. domain.. Paul R, Weiser S, Amiot NC,. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [1]. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site [1]. [1]. 11557134. Novel domains of the prokaryotic two-component signal. transduction systems.. Galperin MY, Nikolskaya AN, Koonin EV;. FEMS Microbiol Lett 2001;203:11-21. (from Pfam)

Date:

2024-08-14

HmsP in Yersinia pestis plays a role in invasion of epithelial cells; the EAL-domain portion of HmsP from Y. pestis shows phosphodiesterase activity which is required for the inhibition of biofilm formation

Gene:

hmsP

Date:

2021-09-10

sensor domain-containing phosphodiesterase with an inactive GGDEF domain and an active EAL domain, similar to Escherichia coli cyclic di-GMP phosphodiesterase PdeK and Yersinia pestis biofilm formation regulator HmsP

Date:

2022-12-14