| Description | An operon encoding 4 proteins required for bacterial cellulose biosynthesis (bcs) in Acetobacter xylinus (Gluconacetobacter xylinus) has been isolated via genetic complementation with strains lacking cellulose synthase activity [ ]. Nucleotide sequence analysis showed the cellulose synthase operon to consist of 4 genes, designated bcsA, bcsB, bcsC and bcsD, all of which are required for maximal bacterial cellulose synthesis in A. xylinum.The calculated molecular mass of the protein encoded by bcsA is 84.4kDa [ ]. Sequence analysis suggests that the gene product is an integral membrane protein with several transmembrane (TM) domains []. It is postulated that the protein is anchored in the membrane at the N-terminal end by a single hydrophobic helix. Two potential N-glycosylation sites are predicted from sequence analysis, consistent with earlier observations that BcsA is a glycoprotein. The function of BcsA is unknown. The sequence shares a high degree of similarity with Escherichia coli YhjO.Cellulose synthase catalyzes the beta-1,4 polymerisation 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 ( ). 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. | Name | Cellulose synthase, subunit A |
| Short Name | Cell_synth_A | Type | Family |
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