ID   GTF3_STRGN              Reviewed;         334 AA.
AC   Q9AEU1;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Glucosyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00841};
DE            EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_00841};
DE   AltName: Full=Sugar transferase Nss {ECO:0000303|PubMed:15049820};
GN   Name=gtf3 {ECO:0000255|HAMAP-Rule:MF_00841};
GN   Synonyms=nss {ECO:0000303|PubMed:15049820};
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M99;
RX   PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA   Bensing B.A., Sullam P.M.;
RT   "An accessory sec locus of Streptococcus gordonii is required for export of
RT   the surface protein GspB and for normal levels of binding to human
RT   platelets.";
RL   Mol. Microbiol. 44:1081-1094(2002).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Genes in the accessory sec locus of Streptococcus gordonii have three
RT   functionally distinct effects on the expression of the platelet-binding
RT   protein GspB.";
RL   Mol. Microbiol. 52:189-203(2004).
RN   [3]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=15489421; DOI=10.1128/jb.186.21.7100-7111.2004;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii
RT   mediate the intracellular glycosylation of the platelet-binding protein
RT   GspB.";
RL   J. Bacteriol. 186:7100-7111(2004).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00841}.
CC   -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC       required to export GspB, a serine-rich repeat cell wall protein encoded
CC       upstream in the same operon. {ECO:0000269|PubMed:15049820,
CC       ECO:0000269|PubMed:15489421}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:15049820,
CC       ECO:0000269|PubMed:15489421}.
CC   -!- SUBUNIT: Homotetramer; a dimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00841}.
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. {ECO:0000255|HAMAP-Rule:MF_00841}.
CC   -!- DISRUPTION PHENOTYPE: Alters carbohydrate composition of cell wall
CC       protein GspB, about 20% reduction in platelet binding by whole cells.
CC       {ECO:0000269|PubMed:15049820, ECO:0000269|PubMed:15489421}.
CC   -!- SIMILARITY: Belongs to the Gtf3 glucosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00841}.
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DR   EMBL; AY028381; AAK16996.1; -; Genomic_DNA.
DR   RefSeq; WP_045634950.1; NZ_RJPG01000001.1.
DR   AlphaFoldDB; Q9AEU1; -.
DR   SMR; Q9AEU1; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00841; Gtf3; 1.
DR   InterPro; IPR043676; Gtf3.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Nucleotide-binding; Transferase.
FT   CHAIN           1..334
FT                   /note="Glucosyltransferase 3"
FT                   /id="PRO_0000414203"
FT   BINDING         16
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         179
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         249..254
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
SQ   SEQUENCE   334 AA;  38007 MW;  0484487596247052 CRC64;
     MKVNITNLYG MSGQSTALIA QNDVTKLAKQ LGFNELSFYF YDIYSDSQSE LSRRLDGIMA
     SVGYGDVVIY QSPTWNGREF DQAFISKLKI LQAKLITFIH DVPPLMFPSN YYLMPEYIDM
     YNQSDAVIVP SEQMRDKLLA EGLTVNKILI QRMWDHPYDL PLHQPQFAPK LYFAGSVERF
     PHLINWSYAT PLEIFSPEEE SNPEANVSYC GWVSRPELLL ELSKGGLGLV WGVEDNPADE
     PEYYGLNISH KSATYLAAGI PVIVPSYLSN AELIRERGLG FVVDSLEEAS RIVENLTVEE
     YQDMVERVRK FSFLLKEGYF SKKVLIDAVM EVLS