Protein Family Models

This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways. [1]. 9423846. Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans. Yoshida Y, Nakano Y, Yamashita Y, Koga T;. Infect Immun 1998;66:107-114. (from Pfam)

Date:

2024-10-16

sugar transferase catalyzes the transfer of a sugar from a donor such as UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate

Date:

2024-08-27

Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (PF02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP) [1], E. coli WcaJ [2], Methylobacillus EpsB [3], Xanthomonas GumD [4], Vibrio CpsA [5], Erwinia AmsG [6], Group B Streptococcus CpsE (originally CpsD) [7], and Streptococcus suis Cps2E [8]. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes such as Sinorhizobium ExoY [9] and Lactococcus EpsD [10] lack the N-terminal domain and are not found by this model.

Date:

2021-08-23