GLYF_STRPN
ID GLYF_STRPN Reviewed; 398 AA.
AC A0A0H2URH2;
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 GlyF {ECO:0000303|PubMed:28246170};
DE AltName: Full=Putative PsrP glycosyltransferase GlyF {ECO:0000305};
GN Name=glyF {ECO:0000303|PubMed:28246170}; OrderedLocusNames=SP_1765;
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 hydrolytic activity against UDP-
CC galactose and to a lesser extent against UDP-glucose; no
CC glycosyltransferase activity has been seen with tested substrates.
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 8 family. {ECO:0000305}.
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DR EMBL; AE005672; AAK75840.1; -; Genomic_DNA.
DR RefSeq; WP_001232150.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; A0A0H2URH2; -.
DR SMR; A0A0H2URH2; -.
DR STRING; 170187.SP_1765; -.
DR EnsemblBacteria; AAK75840; AAK75840; SP_1765.
DR KEGG; spn:SP_1765; -.
DR eggNOG; COG1442; Bacteria.
DR OMA; NYMVGVD; -.
DR PhylomeDB; A0A0H2URH2; -.
DR BioCyc; SPNE170187:G1FZB-1790-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..398
FT /note="Glycosyltransferase GlyF"
FT /id="PRO_0000447029"
FT REGION 1..259
FT /note="GT8 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 101..102
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 221..227
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
SQ SEQUENCE 398 AA; 46365 MW; 4404EF544488BB71 CRC64;
MRKSIVLAAD NAYLIPLETT IKSVLYHNRD VDFYILNSDI APEWFKLLGR KMEVVNSTIR
SVHIDKELFE SYKTGPHINY ASYFRFFATE VVESDRVLYL DSDIIVTGEL ATLFEIDLKG
YSIGAVDDVY AYEGRKSGFN TGMLLMDVAK WKEHSIVNSL LELAAEQNQV VHLGDQSILN
IYFEDNWLAL DKTYNYMVGI DIYHLAQECE RLDDNPPTIV HYASHDKPWN TYSISRLREL
WWVYRDLDWS EIAFQRSDLN YFERSNQSKK QVMLVTWSAD IKHLEYLVQR LPDWHFHLAA
PCDCSEELTS LSQYTNVTVY QNVLHSRIDW LLDDSIVYLD INTGGEVFNV VTRAQESGKK
IFAFDITRKS MDDGLYDGIF SVERPDDLVD RMKNIEIE
