v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Glucosyltransferase 3 (also known as Glucosyltransferase C, GtfC) catalyses the second step of glycosylation of Serine-rich repeat glycoproteins (SRRPs) in Gram-positive bacteria and transfers glucosyl residues to GlcNAc-modified SRRPs. SRRPs have been first identified in pathogenic bacteria but they are also in gut commensal bacteria. These proteins are O-glycosylated on serine or threonine residues to be exported via an specialised accessory secretion (SecA2/Y2) system. This secretion system is encoded in a gene cluster that includes the motor protein SecA2, the channel SecY2 and three to five accessory Sec proteins, but it also contains genes encoding a variable number of glycosyltransferases (GTs), among them Gft3 [ , , ].Structural analysis revealed that Gft3 forms a tetramer and has structural homology with other glycosyltransferases. The conserved residues Phe315 and Leu320 at the C-terminal are critical for oligomerisation and UDP- or UDP-glucose binding. Gft3 homologs constitutes a unique subfamiliy of glycosyltransferases as they are highly conserved and only found in SRRP-containing bacteria [ ]. |
| Short Name | Gtf3 |