GTF3_STRA6
ID GTF3_STRA6 Reviewed; 331 AA.
AC A0A0M3KKZ0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Glucosyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000303|PubMed:25404702};
DE EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:21653318};
GN Name=gtf3 {ECO:0000255|HAMAP-Rule:MF_00841};
GN Synonyms=gtfC {ECO:0000303|PubMed:25404702};
GN ORFNames=SAN_1476 {ECO:0000312|PDB:4W6Q};
OS Streptococcus agalactiae serotype III (strain COH1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=342616;
RN [1]
RP FUNCTION, AND PATHWAY.
RC STRAIN=COH1;
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 [2] {ECO:0000312|PDB:4W6Q, ECO:0007744|PDB:4W6Q}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-331 IN COMPLEX WITH UDP
RP PRODUCT, FUNCTION, PATHWAY, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 106-MET--PHE-111.
RC STRAIN=COH1;
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).
CC -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich
CC repeat protein Srr2. 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 Srr2; does not use other sugar nucleotides as
CC substrates (PubMed:25404702, PubMed:21653318). Complements deletion of
CC the gtf3 gene from S.parasanguinis strain FW213 (PubMed:21653318).
CC {ECO:0000269|PubMed:21653318, ECO:0000269|PubMed:25404702}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:21653318,
CC ECO:0000269|PubMed:25404702}.
CC -!- SUBUNIT: Homotetramer; a dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00841, ECO:0000269|PubMed:25404702}.
CC -!- DOMAIN: Dimerizes via the C-terminus; dimerization is required for
CC tetramer formation (By similarity). Binds protein substrate via an
CC exposed loop in the N-terminus (PubMed:25404702).
CC {ECO:0000250|UniProtKB:B5A7L9, 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 -!- DISRUPTION PHENOTYPE: Altered modification (probably glycosylation) of
CC Srr2. {ECO:0000269|PubMed:25404702}.
CC -!- SIMILARITY: Belongs to the Gtf3 glucosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00841}.
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DR RefSeq; WP_001261474.1; NZ_HG939456.1.
DR PDB; 4W6Q; X-ray; 2.70 A; A/B/C/D=1-331.
DR PDBsum; 4W6Q; -.
DR AlphaFoldDB; A0A0M3KKZ0; -.
DR SMR; A0A0M3KKZ0; -.
DR GeneID; 66886243; -.
DR KEGG; sagt:GBSCOH1_1238; -.
DR UniPathway; UPA00378; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Nucleotide-binding; Transferase.
FT CHAIN 1..331
FT /note="Glucosyltransferase 3"
FT /id="PRO_0000447238"
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 ECO:0000269|PubMed:25404702, ECO:0007744|PDB:4W6Q"
FT BINDING 179
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00841,
FT ECO:0000269|PubMed:25404702, ECO:0007744|PDB:4W6Q"
FT BINDING 211..214
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:25404702,
FT ECO:0007744|PDB:4W6Q"
FT BINDING 242..246
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:25404702,
FT ECO:0007744|PDB:4W6Q"
FT MUTAGEN 106..111
FT /note="Missing: Loss of binding to Srr2-GlcNAc substrate,
FT loss of glycosyltransferase activity, does not restore
FT correct modification of Srr2 in vivo."
FT /evidence="ECO:0000269|PubMed:25404702"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:4W6Q"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:4W6Q"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:4W6Q"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:4W6Q"
SQ SEQUENCE 331 AA; 37963 MW; 3FAB0B0D84E4B25B CRC64;
MRTYITNLNG HSITSTAQIA QNMVTDIAVS LGFRELGIHS YPIDTDSPEE MSKRLDGICS
GLRKNDIVIF QTPTWNTTTF DEKLFHKLKI FGVKIVIFIH DVVPLMFDGN FYLMDRTIAY
YNEADVLIAP SQAMVDKLQS YGLTVKKILV QGMWDHPTNI TLQAVNHKKL VHFPGNPERF
NFIKNWRIPT ELHVYTDHNM QLPTTVVKEP YQSDEQLIMK MSEGGYGLVW MDDRDKQYQS
LYCPYKLGAY IAAGIPVIIQ KGIANQDIIE KNNLGFIIEK IDDISNIVES TTEEEYMEIV
SDVRRFNPLV RQGYFTRKLL TDAVFSALNS M
