WBNK_ECOLX
ID WBNK_ECOLX Reviewed; 302 AA.
AC Q58YV9; Q5JBG3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=O-antigen biosynthesis glycosyltransferase WbnK {ECO:0000305};
DE EC=2.4.1.308 {ECO:0000269|PubMed:15713070, ECO:0000269|PubMed:20418877};
DE AltName: Full=GDP-Fuc:beta-D-Gal-1,3-alpha-D-GalNAc-1,3-alpha-GalNAc-diphosphoundecaprenol alpha-1,2-fucosyltransferase {ECO:0000305};
GN Name=wbnK {ECO:0000303|PubMed:15713070};
GN Synonyms=wbwK {ECO:0000303|PubMed:16332778},
GN wcmD {ECO:0000303|PubMed:15778030};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O86:K61:B7 / ATCC 12701;
RX PubMed=16332778; DOI=10.1128/aem.71.12.7995-8001.2005;
RA Guo H., Yi W., Shao J., Lu Y., Zhang W., Song J., Wang P.G.;
RT "Molecular analysis of the O-antigen gene cluster of Escherichia coli
RT O86:B7 and characterization of the chain length determinant gene (wzz).";
RL Appl. Environ. Microbiol. 71:7995-8001(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=O86:K62:H2;
RX PubMed=15713070; DOI=10.1021/ja045021y;
RA Yi W., Shao J., Zhu L., Li M., Singh M., Lu Y., Lin S., Li H., Ryu K.,
RA Shen J., Guo H., Yao Q., Bush C.A., Wang P.G.;
RT "Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise
RT enzymatic synthesis of human blood group B antigen tetrasaccharide.";
RL J. Am. Chem. Soc. 127:2040-2041(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O86;
RX PubMed=15778030; DOI=10.1016/j.vetmic.2004.12.021;
RA Feng L., Han W., Wang Q., Bastin D.A., Wang L.;
RT "Characterization of Escherichia coli O86 O-antigen gene cluster and
RT identification of O86-specific genes.";
RL Vet. Microbiol. 106:241-248(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=O86:K61:B7 / ATCC 12701;
RX PubMed=20418877; DOI=10.1038/nchembio.351;
RA Woodward R., Yi W., Li L., Zhao G., Eguchi H., Sridhar P.R., Guo H.,
RA Song J.K., Motari E., Cai L., Kelleher P., Liu X., Han W., Zhang W.,
RA Ding Y., Li M., Wang P.G.;
RT "In vitro bacterial polysaccharide biosynthesis: defining the functions of
RT Wzy and Wzz.";
RL Nat. Chem. Biol. 6:418-423(2010).
CC -!- FUNCTION: Involved in the assembly of the O-repeating unit during O-
CC antigen biosynthesis. {ECO:0000269|PubMed:15713070,
CC ECO:0000269|PubMed:20418877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-
CC trans,octa-cis-undecaprenyl diphosphate + GDP-beta-L-fucose = alpha-
CC L-Fuc-(1->2)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-
CC di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+);
CC Xref=Rhea:RHEA:36771, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:73988, ChEBI:CHEBI:73991;
CC EC=2.4.1.308; Evidence={ECO:0000269|PubMed:15713070,
CC ECO:0000269|PubMed:20418877};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:15713070,
CC ECO:0000269|PubMed:20418877}.
CC -!- MISCELLANEOUS: O86:H2 and O86:B7 subtypes share the same O unit, but
CC the O units are polymerized from different terminal sugars in different
CC glycosidic linkages. {ECO:0000269|PubMed:16332778}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; AY220982; AAO37719.1; -; Genomic_DNA.
DR EMBL; AY667408; AAV80759.1; -; Genomic_DNA.
DR EMBL; AY670704; AAV85963.1; -; Genomic_DNA.
DR RefSeq; WP_000286642.1; NZ_WSXE01000046.1.
DR AlphaFoldDB; Q58YV9; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR KEGG; ag:AAV80759; -.
DR BioCyc; MetaCyc:MON-18061; -.
DR BRENDA; 2.4.1.308; 2026.
DR UniPathway; UPA00281; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002516; Glyco_trans_11.
DR PANTHER; PTHR11927; PTHR11927; 1.
DR Pfam; PF01531; Glyco_transf_11; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..302
FT /note="O-antigen biosynthesis glycosyltransferase WbnK"
FT /id="PRO_0000430650"
FT CONFLICT 151
FT /note="N -> H (in Ref. 1; AAO37719)"
SQ SEQUENCE 302 AA; 35584 MW; FC9479A2E4B75C80 CRC64;
MYSCLSGGLG NQMFQYAAAY ILQRKLKQRS LVLDDSYFLD CSNRDTRRRF ELNQFNICYD
RLTTSKEKKE ISIIRHVNRY RLPLFVTNSI FGVLLKKNYL PEAKFYEFLN NCKLQVKNGY
CLFSYFQDAT LIDSHRDMIL PLFQINEDLL NLCNDLHIYK KVICENANTT SLHIRRGDYI
TNPHASKFHG VLPMDYYEKA IRYIEDVQGE QVIIVFSDDV KWAENTFANQ PNYYVVNNSE
CEYSAIDMFL MSKCKNNIIA NSTYSWWGAW LNTFEDKIVV SPRKWFAGNN KSKLTMDSWI
NL
