ID   GLYG_STRPN              Reviewed;         301 AA.
AC   A0A0H2UR96;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Glycosyltransferase GlyG {ECO:0000303|PubMed:28246170};
DE   AltName: Full=PsrP glycosyltransferase GlyG {ECO:0000305};
GN   Name=glyG {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1764;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=16861665; DOI=10.1128/iai.00316-06;
RA   Obert C., Sublett J., Kaushal D., Hinojosa E., Barton T., Tuomanen E.I.,
RA   Orihuela C.J.;
RT   "Identification of a candidate Streptococcus pneumoniae core genome and
RT   regions of diversity correlated with invasive pneumococcal disease.";
RL   Infect. Immun. 74:4766-4777(2006).
RN   [3]
RP   FUNCTION, PATHWAY, AND MUTAGENESIS OF ASP-93.
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=28246170; DOI=10.1074/jbc.m116.770446;
RA   Jiang Y.L., Jin H., Yang H.B., Zhao R.L., Wang S., Chen Y., Zhou C.Z.;
RT   "Defining the enzymatic pathway for polymorphic O-glycosylation of the
RT   pneumococcal serine-rich repeat protein PsrP.";
RL   J. Biol. Chem. 292:6213-6224(2017).
CC   -!- FUNCTION: Involved in the polymorphic O-glycosylation of the serine-
CC       rich repeat protein PsrP. Catalyzes the third step in glycosylation
CC       PsrP in this bacteria. Transfers glucose from UDP-glucose to the
CC       terminal glucose moiety of already-glycosylated PsrP (using truncated
CC       substrates with PsrP SSR1-GlcNAc-Glc). Has a marked preference for PsrP
CC       substrate that has already been modified by GlcNAc and glucose. In
CC       vitro has hydrolytic activity against UDP-glucose and to a lesser
CC       extent against UDP-galactose. {ECO:0000269|PubMed:28246170}.
CC   -!- FUNCTION: Also catalyzes the fourth step in glycosylation of the
CC       serine-rich repeat protein PsrP in this bacteria. Can transfer the
CC       sugar from UDP-glucose (and much less well from UDP-galactose) to the
CC       terminal sugar moiety of PsrP-GlcNAc-Glc-Gal or of PsrP-GlcNAc-Glc-Glc.
CC       {ECO:0000269|PubMed:28246170}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:28246170}.
CC   -!- MISCELLANEOUS: Encoded in RD10, a pathogenicity island with an atypical
CC       GC content that is associated with invasive pneumococcal disease.
CC       Pathogenicity islands account for greater than half the genomic
CC       diversity observed between isolates (PubMed:11463916, PubMed:16861665).
CC       The main function of this island seems to be correct synthesis and
CC       export of pneumococcal serine-rich repeat protein PsrP (Probable).
CC       {ECO:0000303|PubMed:11463916, ECO:0000303|PubMed:16861665,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AE005672; AAK75839.1; -; Genomic_DNA.
DR   RefSeq; WP_001292326.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; A0A0H2UR96; -.
DR   SMR; A0A0H2UR96; -.
DR   STRING; 170187.SP_1764; -.
DR   EnsemblBacteria; AAK75839; AAK75839; SP_1764.
DR   KEGG; spn:SP_1764; -.
DR   eggNOG; COG1215; Bacteria.
DR   OMA; ARMIVNC; -.
DR   PhylomeDB; A0A0H2UR96; -.
DR   BioCyc; SPNE170187:G1FZB-1789-MON; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..301
FT                   /note="Glycosyltransferase GlyG"
FT                   /id="PRO_0000447130"
FT   MUTAGEN         93
FT                   /note="D->A: No longer transfers glucose to an acceptor
FT                   protein."
FT                   /evidence="ECO:0000269|PubMed:28246170"
SQ   SEQUENCE   301 AA;  35011 MW;  D7E6BD9C6EBF8B5D CRC64;
     MSELISVVVP IYNTGKYLVE CVEHILKQTY QNIEIILVDD GSTDNSGEIC DAFMMQDNRV
     RVLHQENKGG AAQAKNMGIS VAKGEYITIV DSDDIVKENM IETLYQQVQE KDADVVIGNY
     YNYDESDGNF YFYVTGQDFC VEELAIQEIM NRQAGDWKFN SSAFILPTFK LIKKELFNEV
     HFSNGRRFDD EATMHRFYLL ASKIVFINDN LYLYRRRSGS IMRTEFDLSW ARDIVEVFSK
     KISDCVLAGL DVSVLRIRFV NLLKDYKQTL EYHQLTDTEE YKDICFRLKL FFDAEQRNGK
     S