cellulose synthase catalytic subunit (UDP-forming). 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 (pfam03170). 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.

cellulose synthase catalytic subunit; Provisional

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.

ChainA, Cellulose synthase catalytic subunit [UDP-forming] [Escherichia coli K-12]

ChainA, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1]

ChainA, Cellulose Synthase Subunit A [Cereibacter sphaeroides]

ChainA, Cellulose Synthase A subunit [Cereibacter sphaeroides 2.4.1],4P02_A Chain A, Cellulose Synthase subunit A [Cereibacter sphaeroides 2.4.1],5EIY_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1],5EJZ_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1]

Cellulose synthase 1 catalytic subunit [UDP-forming] OS=Komagataeibacter xylinus OX=28448 GN=bcsAI PE=3 SV=1

Cellulose synthase catalytic subunit [UDP-forming] OS=Komagataeibacter xylinus OX=28448 GN=bcsA PE=1 SV=1

Cellulose synthase catalytic subunit [UDP-forming] OS=Pseudomonas fluorescens (strain SBW25) OX=216595 GN=bcsA PE=3 SV=2

Cellulose synthase 1 OS=Komagataeibacter hansenii OX=436 GN=acsAB PE=1 SV=1

Cellulose synthase 1 OS=Komagataeibacter xylinus OX=28448 GN=acsAB PE=1 SV=1