AC MF_00841; DC Protein; auto TR HAMAP; MF_00841; -; 1; level=0 XX Names: Gtf3 XX ID GTF3 DE RecName: Full=Glucosyltransferase 3; DE EC=2.4.1.-; GN Name=gtf3; XX case CC -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich CC repeat protein in this bacteria. Catalyzes the second step in CC glycosylation by transferring glucose from UDP-glucose to the terminal CC GlcNAc moiety of the 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl- CC [protein] resulting from the first glycosylation step. else CC -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich CC repeat protein in this bacteria. Catalyzes the second step in CC glycosylation by transferring a sugar from a UDP-activated sugar to the CC terminal GlcNAc moiety of the 3-O-(N-acetyl-alpha-D-glucosaminyl)-L- CC seryl-[protein] resulting from the first glycosylation step. end case CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Homotetramer; a dimer of dimers. CC -!- DOMAIN: Dimerizes via the C-terminus; dimerization is required for CC tetramer formation. Binds protein substrate via an exposed loop in the CC N-terminus. CC -!- SIMILARITY: Belongs to the Gtf3 glucosyltransferase family. XX DR PIRSF; PIRSF007023; UDP-Galf_transf; 1; trigger=no XX KW Glycosyltransferase KW Nucleotide-binding KW Transferase XX case GO GO:0035251; F:UDP-glucosyltransferase activity else GO GO:0008194; F:UDP-glycosyltransferase activity end case XX FT From: GTF3_STRPA (B5A7L9) FT BINDING 244..249 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT Condition: [NPS]-[FHY]-K-x-[AGS]-[AIST] FT BINDING 16 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT Optional; Condition: T FT BINDING 179 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT Condition: [KRT] XX Size: 309-345; Related: None; Template: B5A7L9; A0A0H2UR93; A0A0M3KKZ0; B3XPQ7; F8KEJ1; Scope: Bacteria; Bacillota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.7 2023/01/13 //