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GtfA extended beta-sheet domain
This entry represents the extended beta-sheet domain (EBD, also known as DUF1975) of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit [1,2]. GtfA is the core enzyme of the OGT complex, which also includes the co-activator GtfB, to glycosylate the serine-rich repeat (SRR) of adhesin PsrP in Streptococcus pneumoniae, a protein involved in the infection and pathogenesis [1,2]. The function of this domain is not clear. [1]. 26884191. Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Chen Y, Seepersaud R, Bensing BA, Sullam PM, Rapoport TA;. Proc Natl Acad Sci U S A. 2016;113:E1190-E1199. [2]. 24936067. Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins. Shi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ;. J Biol Chem. 2014;289:20898-20907. (from Pfam)
glycosyltransferase
Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. (from Pfam)
TIGR02918 family protein
accessory Sec system glycosyltransferase GtfA
Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system.
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