Protein Family Models

This domain is the N-terminal periplasmic domain of the LapD and MoxY receptor proteins [1-2]. [1]. 8392137. Identification of a two-component regulatory system controlling. methanol dehydrogenase synthesis in Paracoccus denitrificans.. Harms N, Reijnders WN, Anazawa H, van der Palen CJ, van Spanning. RJ, Oltmann LF, Stouthamer AH;. Mol Microbiol. 1993;8:457-470.. [2]. 21304926. Structural basis for c-di-GMP-mediated inside-out signaling. controlling periplasmic proteolysis.. Navarro MV, Newell PD, Krasteva PV, Chatterjee D, Madden DR,. O'Toole GA, Sondermann H;. PLoS Biol. 2011;9:e1000588. (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

Date:

2024-08-14

The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity [1][3]. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus[2], and FixL, a heme-containing oxygen sensor protein.

Date:

2021-04-27