Open AccessConserved cytoplasmic motifs that distinguish sub‐groups of the polyprenol phosphate: N ‐acetylhexosamine‐1‐phosphate transferase family
Author(s) -
Anderson Matt S.,
Eveland Suzanne S.,
Price Neil P.J.
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09335.x
Subject(s) - transferase , cytoplasm , phosphate , nucleotide , sugar phosphates , biochemistry , biology , transmembrane domain , enzyme , chemistry , membrane , gene
WecA, MraY and WbcO are conserved members of the polyprenol phosphate: N ‐acetylhexosamine‐1‐phosphate transferase family involved in the assembly of bacterial cell walls, and catalyze reactions involving a membrane‐associated polyprenol phosphate acceptor substrate and a cytoplasmically located UDP‐ D ‐amino sugar donor. MraY, WbcO and WecA purportedly utilize different UDP‐sugars, although the molecular basis of this specificity is largely unknown. However, domain variations involved in specificity are predicted to occur on the cytoplasmic side of the membrane, adjacent to conserved domains involved in the mechanistic activity, and with access to the cytoplasmically located sugar nucleotides. Conserved C‐terminal domains have been identified that satisfy these criteria. Topological analyses indicate that they form the highly basic, fifth cytoplasmic loop between transmembrane regions IX and X. Four diverse loops are apparent, for MraY, WecA, WbcO and RgpG, that uniquely characterize these sub‐groups of the transferase family, and a correlation is evident with the known or implied UDP‐sugar specificity.