Protein Domain : GtrA/DPMS, transmembrane domain IPR007267

Type	Domain
Description	This entry represents a domain found in prokaryotic members of the GtrA family, which are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. GtrA is involved in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane [ ]. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyses the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b) []. This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and Listeria monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose [].This domain usually covers most of the length of these sequences.This domain is also found at the C terminus of the glycosyltransferase 2 (GH2) family member Dolichol-phosphate mannosyltransferase from Pyrococcus furiosus (DPMS) and similar prokaryotic proteins. This protein transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins. This entry represents the transmembrane (TM) domain that shows four TM helices (TMHs) arranged as two TMH dimers [ ].
Short Name	GtrA_DPMS_TM