GLYD_STRPN
ID GLYD_STRPN Reviewed; 814 AA.
AC A0A0H2URB1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Glycosyltransferase GlyD {ECO:0000303|PubMed:28246170};
DE AltName: Full=PsrP glycosyltransferase GlyD {ECO:0000305};
GN Name=glyD {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1767;
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, DOMAIN, AND MUTAGENESIS OF ASP-572 AND GLU-789.
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); the C-terminal GT-D domain is
CC sufficient for this reaction in vitro. Also transfers galactose from
CC UDP-galactose to the terminal glucose moiety of already-glycosylated
CC PsrP; the C-terminal GT-D domain is also sufficient for this reaction
CC in vitro. Activity is much higher with UDP-glucose, and the enzyme has
CC a very marked preference for PsrP substrate that has already been
CC modified by GlcNAc and glucose. In vitro has hydrolytic activity
CC against UDP-galactose and to a lesser extent 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 both UDP-glucose and UDP-
CC galactose to the terminal sugar moiety of PsrP-GlcNAc-Glc-Glc and PsrP-
CC GlcNAc-Glc-Gal; the C-terminal GT-D domain is also sufficient for this
CC reaction in vitro (using truncated substrates with glycosylated PsrP
CC SSR1). The N-terminal GT-D domain can transfer galactose from UDP-
CC galactose to PsrP-GlcNAc-Glc-Gal or PsrP-GlcNAc-Glc-Glc in the fourth
CC step. {ECO:0000269|PubMed:28246170}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:28246170}.
CC -!- DOMAIN: Has an N-terminal GT8 domain and a C-terminal GT-D domain. The
CC GT8 has very little glucose transferase activity in the third
CC glycosylation step, but is able to transfer galactose from UDP-
CC galactose to PsrP-GlcNAc-Glc-Gal or PsrP-GlcNAc-Glc-Glc in the fourth
CC step. The C-terminal GT-D domain catalyzes transfer of galactose and
CC glucose to the acceptor protein (PsrP-GlcNAc-Glc) in both the third and
CC fourth glycosylation steps. {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|PubMed:28246170}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GT-D family.
CC {ECO:0000305}.
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DR EMBL; AE005672; AAK75842.1; -; Genomic_DNA.
DR RefSeq; WP_001044136.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; A0A0H2URB1; -.
DR SMR; A0A0H2URB1; -.
DR STRING; 170187.SP_1767; -.
DR EnsemblBacteria; AAK75842; AAK75842; SP_1767.
DR KEGG; spn:SP_1767; -.
DR eggNOG; COG1442; Bacteria.
DR OMA; GDQTIFN; -.
DR BioCyc; SPNE170187:G1FZB-1792-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; 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 1: Evidence at protein level;
KW Glycosyltransferase; Manganese; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..814
FT /note="Glycosyltransferase GlyD"
FT /id="PRO_0000447027"
FT REGION 1..264
FT /note="GT8 domain"
FT /evidence="ECO:0000305|PubMed:28246170"
FT REGION 542..814
FT /note="GT-D domain"
FT /evidence="ECO:0000305|PubMed:28246170"
FT BINDING 8..13
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 102..103
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 226..232
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 226
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT MUTAGEN 572
FT /note="D->A: Isolated GT-D domain no longer transfers
FT glucose to an acceptor protein."
FT /evidence="ECO:0000269|PubMed:28246170"
FT MUTAGEN 789
FT /note="E->A: Isolated GT-D domain no longer transfers
FT glucose to an acceptor protein."
FT /evidence="ECO:0000269|PubMed:28246170"
SQ SEQUENCE 814 AA; 94615 MW; FCB283B8BD595954 CRC64;
MNKTIVLAGD RNYTRQLETT IKSILYHNRD VKIYILNQDI MPDWFRKPRK IARMLGSEII
DVKLPEQTVF QDWEKQDHIS SITYARYFIA DYIQEDKVLY LDSDLIVNTS LEKLFSICLE
EKSLAAVKDT DGITFNAGVL LINNKKWRQE KLKERLIEQS IVTMKEVEEG RFEHFNGDQT
IFNQVLQDDW LELGRAYNLQ VGHDIVALYN NWQEHLAFND KPVVIHFTTY RKPWTTLTAN
RYRDLWWEFH DLEWSQILQH HMGEFELISP LDKEFSCLTL TNSQDLEGIE ELVTALPEVV
FHIAAWTDMG DKLKKLAVYN NVRLHPQIVP PVLDKLKKST NLYLDINHGS ADENFLKSLQ
EQEKTLLAFQ STQHGELGQI VFENGKVSFM IDTIKDFKKN GHLTCFRQLP SLTCLTFTAS
QYIEQLDYLA GQLPNVVFQI AAWTAMGPKL YDLSNRYPNI QLYPAISRDK LDELKEKMDA
YLDINLLTST SDIVAEMAHL SKPILAFYKS QNGNNGQRLY SSEHPERMLA DLQKLITKDM
LEKPLDIIQV KGIDETLDYI IEHNSSLVRF GDGEINMLAG HSIPYQDYDE ELVSIMRDII
GQESREDLVV CLPDAFTDRF RFTSWAIPFW KDHMDHYMDF YRELCSDSWY GSTFVSRPYI
DFEDKSQAKA QFEKLKSIWE NRDLLIVEGA TSRSGVGNDL FDEANSIKRI ICPSHSAFSR
VHELEQEIEK YAGGRLILCM LGPTAKVLSY NLCQMGYQVL DVGHIDSEYE WMKMGAKTKV
KFSHKHTAEH NFDQDIEFID DETYNSQIVA RILN
