GTF3_STRPN
ID GTF3_STRPN Reviewed; 336 AA.
AC A0A0H2UR93;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Glucosyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000303|PubMed:28246170};
DE EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:21653318};
GN Name=gtf3 {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000303|PubMed:21653318};
GN Synonyms=gtfC {ECO:0000303|PubMed:25404702}; OrderedLocusNames=SP_1768;
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 PATHWAY.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=21653318; DOI=10.1074/jbc.m110.208629;
RA Zhu F., Erlandsen H., Ding L., Li J., Huang Y., Zhou M., Liang X., Ma J.,
RA Wu H.;
RT "Structural and functional analysis of a new subfamily of
RT glycosyltransferases required for glycosylation of serine-rich
RT streptococcal adhesins.";
RL J. Biol. Chem. 286:27048-27057(2011).
RN [4]
RP FUNCTION, PATHWAY, DOMAIN, AND MUTAGENESIS OF 106-MET--TYR-111.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=25404702; DOI=10.1128/jb.02267-14;
RA Zhu F., Zhang H., Wu H.;
RT "A conserved domain is crucial for acceptor substrate binding in a family
RT of glucosyltransferases.";
RL J. Bacteriol. 197:510-517(2015).
RN [5]
RP FUNCTION, AND PATHWAY.
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: Required for polymorphic O-glycosylation of the serine-rich
CC repeat protein PsrP. Catalyzes the second step in glycosylation of the
CC serine-rich repeat protein in this bacteria. Transfers glucose from
CC UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-
CC glucosaminyl)-L-seryl-[protein] which results from the first
CC glycosylation step of PsrP (using the short substrate SRR1-GlcNAc)
CC (PubMed:28246170, PubMed:25404702, PubMed:21653318). Has weak
CC hydrolytic activity against UDP-glucose and even weaker activity on
CC UDP-galactose (PubMed:28246170). Does not complement deletion of the
CC gtf3 gene from S.parasanguinis strain FW213 (PubMed:21653318).
CC {ECO:0000269|PubMed:21653318, ECO:0000269|PubMed:25404702,
CC ECO:0000269|PubMed:28246170}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:21653318,
CC ECO:0000269|PubMed:25404702, ECO:0000269|PubMed:28246170}.
CC -!- SUBUNIT: Homotetramer; a dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00841}.
CC -!- DOMAIN: Binds protein substrate via an exposed loop in the N-terminus.
CC {ECO:0000269|PubMed:25404702}.
CC -!- DOMAIN: Dimerizes via the C-terminus; dimerization is required for
CC tetramer formation. Binds protein substrate via an exposed loop in the
CC N-terminus. {ECO:0000255|HAMAP-Rule:MF_00841}.
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: Belongs to the Gtf3 glucosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00841}.
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DR EMBL; AE005672; AAK75843.1; -; Genomic_DNA.
DR RefSeq; WP_000766254.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; A0A0H2UR93; -.
DR SMR; A0A0H2UR93; -.
DR STRING; 170187.SP_1768; -.
DR EnsemblBacteria; AAK75843; AAK75843; SP_1768.
DR KEGG; spn:SP_1768; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; YGMAGDS; -.
DR BioCyc; SPNE170187:G1FZB-1793-MON; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00841; Gtf3; 1.
DR InterPro; IPR043676; Gtf3.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Nucleotide-binding; Transferase.
FT CHAIN 1..336
FT /note="Glucosyltransferase 3"
FT /id="PRO_0000447237"
FT REGION 106..111
FT /note="Substrate protein-binding loop"
FT /evidence="ECO:0000269|PubMed:25404702"
FT BINDING 16
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT BINDING 179
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT BINDING 250..255
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT MUTAGEN 106..111
FT /note="Missing: Loss of binding to PsrP-GlcNAc substrate,
FT loss of glycosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:25404702"
SQ SEQUENCE 336 AA; 38368 MW; 8E8E900BB976D0C1 CRC64;
MKLHLTNLYG MAGDSTVILA QNAVQKIASQ LGFREVGIYF YNIASDSPSE MNKRLDGIMA
SISIGDILVF QSPTWNGFEF DRLLFDKLKD MQVKIICFIH DVVPLMFDSN YYLMKDYLYM
YNLSDVLIVP SERMKTRLME EGLTTKKILV QGMWDHPHDL SLYTPAFKKE LFFAGSLERF
PDLQNWSQDT PLRVFSNKGE ASSSARSLSI EGWKKDEELL LELSKGGFGL VWGTHQNEGE
SNQYYTLNIS HKVSTYLTAG IPVIVPSSLS TAKFIVDQGL GFMADSLEEV HEIVDKMNLQ
EYQEMTNRIK TFSYLLKEGY FTKKLLVDAI YHLGID
