GLYAT_STRPN
ID GLYAT_STRPN Reviewed; 696 AA.
AC A0A0H2URH7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Glycosyltransferase GlyA {ECO:0000303|PubMed:28246170};
DE AltName: Full=PsrP glycosyltransferase GlyA {ECO:0000305};
GN Name=glyA {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1771;
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 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: Involved in the polymorphic O-glycosylation of the serine-
CC rich repeat protein PsrP. Catalyzes the fourth step in glycosylation of
CC PsrP in this bacteria. Can transfer the sugar from UDP-galactose to the
CC terminal sugar moiety of PsrP-GlcNAc-Glc-Gal or of PsrP-GlcNAc-Glc-Glc
CC (using truncated substrates with the PsrP SSR1 domain)
CC (PubMed:28246170). Has hydrolytic activity against UDP-galactose and to
CC a lesser extent against UDP-glucose (PubMed:28246170).
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: In the N-terminal section; belongs to the
CC glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the glycosyltransferase
CC 8 family. {ECO:0000305}.
CC -!- CAUTION: This gene name has also been given to serine
CC hydroxymethyltransferase (AC Q97R16) in this organism. {ECO:0000305}.
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DR EMBL; AE005672; AAK75845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2URH7; -.
DR SMR; A0A0H2URH7; -.
DR STRING; 170187.SP_1771; -.
DR EnsemblBacteria; AAK75845; AAK75845; SP_1771.
DR KEGG; spn:SP_1771; -.
DR eggNOG; COG1216; Bacteria.
DR eggNOG; COG1442; Bacteria.
DR OMA; HYLSHRK; -.
DR PhylomeDB; A0A0H2URH7; -.
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; -; 2.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 2.
PE 3: Inferred from homology;
KW Glycosyltransferase; Manganese; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..696
FT /note="Glycosyltransferase GlyA"
FT /id="PRO_0000447025"
FT REGION 1..301
FT /note="GT2 domain"
FT /evidence="ECO:0000305|PubMed:28246170"
FT REGION 302..556
FT /note="GT8 domain"
FT /evidence="ECO:0000305|PubMed:28246170"
FT BINDING 308..313
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 399..400
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 399
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 401
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 518..524
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 518
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
SQ SEQUENCE 696 AA; 81336 MW; ADCA9C01AABB32C7 CRC64;
MLVDDKITVI VPVYNVENYL RKCLDSIITQ TYKNIEIVVV NDGSTDASGE ICKEFSEMDH
RILYIEQENA GLSAARNTGL NNMSGNYVTF VDSDDWIEQD YVETLYKKIV EYQADIAVGN
YYSFNESEGM FYFHILGDSY YEKVYDNVSI FENLYETQEM KSFALISAWG KLYKARLFEQ
LRFDIGKLGE DGYLNQKVYL LSEKVIYLNK SLYAYRIRKG SLSRVWTEKW MHALVDAMSE
RITLLANMGY PLEKHLAVYR QMLEVSLANG QASGLSDTAT YKEFEMKQRL LNQLSRQEES
EKKAIVLAAN YGYVDQVLTT IKSICYHNRS IRFYLIHSDF PNEWIKQLNK RLEKFDSEII
NCRVTSEQIS CYKSDISYTV FLRYFIADFV QEDKALYLDC DLVVTKNLDD LFATDLQDYP
LAAVRDFGGR AYFGQEIFNA GVLLVNNAFW KKENMTQKLI DVTNEWHDKV DQADQSILNM
LFEHKWLELD FDYNHIVIHK QFADYQLPEG QDYPAIIHYL SHRKPWKDLA AQTYREVWWY
YHGLEWTELG QNHHLHPLQR SHIYPIKEPF TCLIYTASDH IEQIETLVQS LPDIQFKIAA
RVIVSDRLAQ MTIYPNVTIF NGIHYLVDVD NELVETSQVL LDINHGEKTE EILDQFANLG
KPILSFENTK TYEVGQEAYA VDQVQAMIEK LREISK
