Protein Family Models

This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80. (from Pfam)

Date:

2024-08-14

Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis [1][2]. [1]. 9515923. Characterization of the gene cassette required for biosynthesis of the (alpha1-->6)-linked N-acetyl-D-mannosamine-1-phosphate capsule of serogroup A Neisseria meningitidis. Swartley JS, Liu LJ, Miller YK, Martin LE, Edupuganti S, Stephens DS;. J Bacteriol. 1998;180:1533-1539. [2]. 11953367. Novel Aeromonas hydrophila PPD134/91 genes involved in O-antigen and capsule biosynthesis. Zhang YL, Arakawa E, Leung KY;. Infect Immun. 2002;70:2326-2335. (from Pfam)

Date:

2024-10-16

Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis [1][2]. [1]. 9515923. Characterization of the gene cassette required for biosynthesis of the (alpha1-->6)-linked N-acetyl-D-mannosamine-1-phosphate capsule of serogroup A Neisseria meningitidis. Swartley JS, Liu LJ, Miller YK, Martin LE, Edupuganti S, Stephens DS;. J Bacteriol. 1998;180:1533-1539. [2]. 11953367. Novel Aeromonas hydrophila PPD134/91 genes involved in O-antigen and capsule biosynthesis. Zhang YL, Arakawa E, Leung KY;. Infect Immun. 2002;70:2326-2335. (from Pfam)

Date:

2024-10-16

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 K, Nieto V, Carl. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesised by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesise cellulose in higher plants differ greatly from the well-characterised genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity [1]. [1]. 8901635. Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase. Pear JR, Kawagoe Y, Schreckengost WE, Delmer DP, Stalker DM;. Proc Natl Acad Sci U S A 1996;93:12637-12642. [2]. 11178255. Higher plant cellulose synthases. Richmond T;. Genome Biol 2000;1:1-6. (from Pfam)

Date:

2024-10-16

Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. (from Pfam)

Date:

2024-08-14

Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (PF03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.

Gene:

bcsA

Date:

2021-09-22