GLYE_STRPN
ID GLYE_STRPN Reviewed; 406 AA.
AC A0A0H2URJ6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Glycosyltransferase GlyE {ECO:0000303|PubMed:28246170};
DE AltName: Full=PsrP glycosyltransferase GlyE {ECO:0000305};
GN Name=glyE {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1766;
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] {ECO:0007744|PDB:5GVV, ECO:0007744|PDB:5GVW}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-406 IN COMPLEX WITH MANGANESE
RP WITH OR WITHOUT UDP, FUNCTION, COFACTOR, PATHWAY, DOMAIN, AND MUTAGENESIS
RP OF ARG-90; ASP-106; ASP-108; ASP-177; GLN-178; 285-ASN--TRP-287 AND
RP 311-ASN--ALA-313.
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 of
CC PsrP in this bacteria. Transfers galactose from UDP-galactose to the
CC terminal glucose moiety of already-glycosylated PsrP (using the short
CC substrate PsrP-GlcNAc-Glc). Has a very marked preference for PsrP
CC substrate that has already been modified by GlcNAc and glucose. Has
CC hydrolytic activity against UDP-galactose but none against UDP-glucose.
CC {ECO:0000269|PubMed:28246170}.
CC -!- FUNCTION: Also catalyzes the fourth step in glycosylation of PsrP in
CC this bacteria. Can transfer the sugar from UDP-galactose to the
CC terminal sugar moiety of PsrP-GlcNAc-Glc-Glc and of PsrP-GlcNAc-Glc-
CC Gal. {ECO:0000269|PubMed:28246170}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28246170};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:28246170}.
CC -!- DOMAIN: Has 2 domains, the N-terminal GT8 domain that binds UDP and
CC Mn(2+) and a C-terminal domain that assumes a Rossmann-like fold. The
CC GT8 domain has UDP-galactose hydrolysis activity but no galactose
CC transferase activity (PubMed:28246170). The C-terminal domain probably
CC binds the partially glycosylated protein acceptor in a continuous,
CC surface-exposed groove that can possibly bind proteins with varying
CC degrees of glycosylation (Probable). {ECO:0000269|PubMed:28246170,
CC ECO:0000305|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; AAK75841.1; -; Genomic_DNA.
DR RefSeq; WP_001808456.1; NZ_AKVY01000001.1.
DR PDB; 5GVV; X-ray; 1.95 A; A/F=3-406.
DR PDB; 5GVW; X-ray; 2.40 A; A/B/C/D=3-406.
DR PDBsum; 5GVV; -.
DR PDBsum; 5GVW; -.
DR AlphaFoldDB; A0A0H2URJ6; -.
DR SMR; A0A0H2URJ6; -.
DR STRING; 170187.SP_1766; -.
DR EnsemblBacteria; AAK75841; AAK75841; SP_1766.
DR KEGG; spn:SP_1766; -.
DR eggNOG; COG1442; Bacteria.
DR OMA; KSLCYHN; -.
DR PhylomeDB; A0A0H2URJ6; -.
DR BioCyc; SPNE170187:G1FZB-1791-MON; -.
DR UniPathway; UPA00378; -.
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 GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Manganese; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..406
FT /note="Glycosyltransferase GlyE"
FT /id="PRO_0000447028"
FT REGION 3..265
FT /note="GT8 domain"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 11..16
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 106..107
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 227..233
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28246170"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 90
FT /note="R->A: Loss of UDP-galactose hydrolysis."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 106
FT /note="D->A: Loss of UDP-galactose hydrolysis."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 108
FT /note="D->A: Loss of UDP-galactose hydrolysis."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 177
FT /note="D->A: Loss of UDP-galactose hydrolysis."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 178
FT /note="Q->A: Loss of UDP-galactose hydrolysis."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 285..287
FT /note="NSW->ASA: Significantly decreased
FT glycosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 311..313
FT /note="NMA->AMR: Decreased glycosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28246170"
SQ SEQUENCE 406 AA; 47412 MW; D14D56036CFBC690 CRC64;
MRNTKRAVVF AGDYAYIRQI ETAMKSLCRH NSHLKIYLLN QDIPQEWFSQ IRIYLQEMGG
DLIDCKLIGS QFQMNWSNKL PHINHMTFAR YFIPDFVTED KVLYLDSDLI VTGDLTDLFE
LDLGENYLAA ARSCFGAGVG FNAGVLLINN KKWGSETIRQ KLIDLTEKEH ENVEEGDQSI
LNMLFKDQYS SLEDQYNFQI GYDYGAATFK HQFIFDIPLE PLPLILHYIS QDKPWNQFSV
GRLREVWWEY SLMDWSVILN EWFSKSVKYP SKSQIFKLQC VNLTNSWCVE KIDYLAEQLP
EVHFHIVAYT NMANELLALT RFPNVTVYPN SLPMLLEQIV IASDLYLDLN HDRKLEDAYE
FVLKYKKPMI AFDNTCSENL SEISYEGIYP SSIPKKMVAA IRSYMR
