WFGD_ECOLX
ID WFGD_ECOLX Reviewed; 253 AA.
AC B5L3F2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfgD;
DE EC=2.4.1.305;
GN Name=wfgD;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O152;
RX PubMed=18422615; DOI=10.1111/j.1574-6976.2008.00114.x;
RA Liu B., Knirel Y.A., Feng L., Perepelov A.V., Senchenkova S.N., Wang Q.,
RA Reeves P.R., Wang L.;
RT "Structure and genetics of Shigella O antigens.";
RL FEMS Microbiol. Rev. 32:627-653(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=O152 / G1104;
RX PubMed=18487334; DOI=10.1128/jb.00160-08;
RA Brockhausen I., Hu B., Liu B., Lau K., Szarek W.A., Wang L., Feng L.;
RT "Characterization of two beta-1,3-glucosyltransferases from Escherichia
RT coli serotypes O56 and O152.";
RL J. Bacteriol. 190:4922-4932(2008).
CC -!- FUNCTION: Catalyzes the addition of Glc, the second sugar moiety of the
CC O152-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol.
CC {ECO:0000269|PubMed:18487334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate + UDP-alpha-D-glucose = beta-D-Glc-(1->3)-alpha-D-GlcNAc-
CC di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP;
CC Xref=Rhea:RHEA:36755, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:62959, ChEBI:CHEBI:73986;
CC EC=2.4.1.305; Evidence={ECO:0000269|PubMed:18487334};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18487334};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18487334};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for UDP-Glc {ECO:0000269|PubMed:18487334};
CC Vmax=0.13 umol/h/mg enzyme toward UDP-Glc
CC {ECO:0000269|PubMed:18487334};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:18487334};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:18487334}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18487334}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18487334}; Cytoplasmic side
CC {ECO:0000269|PubMed:18487334}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; EU294170; ACA24822.1; -; Genomic_DNA.
DR RefSeq; WP_040089049.1; NZ_NWAN01000020.1.
DR AlphaFoldDB; B5L3F2; -.
DR SMR; B5L3F2; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; ag:ACA24822; -.
DR BioCyc; MetaCyc:MON-21555; -.
DR BRENDA; 2.4.1.305; 2026.
DR UniPathway; UPA00030; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Magnesium; Manganese; Membrane;
KW Transferase.
FT CHAIN 1..253
FT /note="UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-
FT 1,3-glucosyltransferase WfgD"
FT /id="PRO_0000424178"
SQ SEQUENCE 253 AA; 28987 MW; D11A4B7C435B0B9F CRC64;
MDDYLVSIIM PSYNAEHTIS ASISSVLKQT YANWELLVCD DDSSDNTRFK VLEFSDSRIK
LLTNEYAKGA AGARNTALKY ASGRFIAFLD SDDIWIANKL EMQISMMLKN NISFMYGNYE
IINNNSIVGK FVAPQKITYN KLLKNCGIGC LTVVLDRTLL NPFSFPFVHK EDYYLWLSIL
KDNNISAINC GFICSKYRLS QSSISSNKFK ELKRQWDVLG DFVENPLARI YYLLNYIVIG
IKKHAFDYKN GKK