GLYB_STRPN
ID GLYB_STRPN Reviewed; 404 AA.
AC A0A0H2URA3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Glycosyltransferase GlyB {ECO:0000303|PubMed:28246170};
DE AltName: Full=Putative PsrP glycosyltransferase GlyB {ECO:0000305};
GN Name=glyB {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1770;
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, AND DOMAIN.
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: May be involved in the polymorphic O-glycosylation of the
CC serine-rich repeat protein PsrP. Has equal hydrolytic activity against
CC both UDP-galactose and UDP-glucose; no glycosyltransferase activity has
CC been seen with tested substrates. {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: In the N-terminal section; belongs to the
CC glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AE005672; AAK75844.1; -; Genomic_DNA.
DR RefSeq; WP_001093470.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; A0A0H2URA3; -.
DR SMR; A0A0H2URA3; -.
DR STRING; 170187.SP_1770; -.
DR EnsemblBacteria; AAK75844; AAK75844; SP_1770.
DR KEGG; spn:SP_1770; -.
DR eggNOG; COG1442; Bacteria.
DR OMA; NRFRDIW; -.
DR PhylomeDB; A0A0H2URA3; -.
DR BioCyc; SPNE170187:G1FZB-1796-MON; -.
DR Proteomes; UP000000585; Chromosome.
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; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Manganese; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..404
FT /note="Glycosyltransferase GlyB"
FT /id="PRO_0000447026"
FT REGION 1..267
FT /note="GT8 domain"
FT /evidence="ECO:0000305|PubMed:28246170"
FT BINDING 9..14
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 103..104
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 105
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 228..233
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 228
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
SQ SEQUENCE 404 AA; 47250 MW; EEF8E206C278DC98 CRC64;
MNTKSIVFNA DNDYVDKLET AIKSICCYNN CLKFYVFNDD IASEWFLMMN KRLKTIQSEI
VNVKIVDHVL KKFHLPLKNL SYATFFRYFI PNFVKESRAL YLDSDIIVTG SLDYLFDIEL
DGYALAAVED SFGDVPSTNF NSGMLLVNVD TWRDEDACSK LLELTNQYHE TAYGDQGILN
MLFHDRWKRL DRNFNFMVGM DSVAHIEGNH KWYEISELKN GDLPSVIHYT GVKPWEIISN
NRFREVWWFY NLLEWSDILL RKDIISRSFE ELVYSPKAHT AIFTASCEME HVEYLIENLP
EVHFSILAHT YFASSVVALL RYSNVTIYPC FSPFDYRKIL DNLDFYLDIN HYKEVDNIVS
VVQQLSKPIF TFENTSHDIG NQTNIFSSTE PNKMVEAIRQ FIGE
