ID   GLY_STRGN               Reviewed;         682 AA.
AC   Q9AEU2;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable glycosyl transferase Gly;
GN   Name=gly;
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, 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, 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: 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   -!- SUBUNIT: Part of the accessory SecA2/SecY2 protein translocation
CC       apparatus required to export cell wall protein GspB.
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 glycosyltransferase 8 family. {ECO:0000305}.
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DR   EMBL; AY028381; AAK16995.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AEU2; -.
DR   SMR; Q9AEU2; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR014869; GT-D.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   Pfam; PF08759; GT-D; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03728; glyco_access_1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Manganese; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..682
FT                   /note="Probable glycosyl transferase Gly"
FT                   /id="PRO_0000414594"
FT   BINDING         21..26
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         112..113
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         230..236
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         230
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
SQ   SEQUENCE   682 AA;  77881 MW;  E44390DFD2AC8F08 CRC64;
     MDKLENKSMA NYDEYRAVVI CASFSDCNQV LTTIKSIVCH NRFIKFYVIN NDFPTEWFVS
     MQKKLAKLDC PIVNARVDAS LVSNFKTDIS YTVFLRYFVA DFVEEEQALY LDCDIVVTRD
     LSEIFAVDLG SHPLVAVRDL GGEVYFGEQI FNSGVLLINV NYWRENDIAG QLIEMTDNLH
     DKVTQDDQSI LNMFFENRWV ELPFPYNCIT LHTTFSDYEP EKGLYPPVIH YLPERKPWKE
     YTQSIYREVW WFYQGLDWSD IQEPVGALTQ KMVEGEDDSS LSCLVYTYSC DLLHINYLIQ
     ALPSCHFYIA APVVVAEPIT RLLQYPNVSV SSDIAGIPAL LESLEAKSQL LLDINAGDEV
     GDIIARFKSS GKPVFAFDST VHGQQGQEVF PADNPEVMVQ AIEKLGLAEP EERQISVLSI
     DQSLDYLLEK GASVVRFGDG EMDLIAGRGI PYQEYDPELS ARLREMMAME SNERLMICLS
     DVFTGLERYS IDAQNFWKAH LQHHLADYLE ICRAPWYGST FISRPYIDLE DKTPSAGYFA
     KLKQLWQDKD LLIVEGLTSR SGVGNDLFDG ARSIKRIICP SRNAYSKLEA IKQAVREHAD
     NRLILTMLGP TAKVLVYDLV QEGYRALDIG HIDSEYEWFQ MGASHKIKLS HKHTAEHNFD
     QDIEYRDDQA YDSQIVANLA QE