WBNI_ECOLX
ID WBNI_ECOLX Reviewed; 234 AA.
AC Q5JBG6; Q58YW2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=O-antigen biosynthesis glycosyltransferase WbnI {ECO:0000305};
DE EC=2.4.1.309 {ECO:0000269|PubMed:15713070, ECO:0000269|PubMed:20418877};
DE AltName: Full=UDP-Gal:alpha-L-Fuc-1,2-beta-Gal-1,3-alpha-GalNAc-1,3-alpha-GalNAc-diphosphoundecaprenol alpha-1,3-galactosyltransferase {ECO:0000305};
GN Name=wbnI {ECO:0000303|PubMed:15713070};
GN Synonyms=wbwI {ECO:0000303|PubMed:16332778},
GN wcmB {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=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-
CC alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + UDP-
CC alpha-D-galactose = alpha-D-Gal-(1->3)-[alpha-L-Fuc-(1->2)]-beta-D-
CC Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-
CC undecaprenyl diphosphate + H(+) + UDP; Xref=Rhea:RHEA:36775,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:73991, ChEBI:CHEBI:73993; EC=2.4.1.309;
CC Evidence={ECO:0000269|PubMed:15713070, ECO:0000269|PubMed:20418877};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
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 6 family. {ECO:0000305}.
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DR EMBL; AY220982; AAO37716.1; -; Genomic_DNA.
DR EMBL; AY667408; AAV80756.1; -; Genomic_DNA.
DR EMBL; AY670704; AAV85960.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5JBG6; -.
DR SMR; Q5JBG6; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR KEGG; ag:AAV80756; -.
DR BioCyc; MetaCyc:MON-18060; -.
DR BRENDA; 2.4.1.309; 2026.
DR UniPathway; UPA00281; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..234
FT /note="O-antigen biosynthesis glycosyltransferase WbnI"
FT /id="PRO_0000430651"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 8..13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 115..118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CONFLICT 33
FT /note="G -> E (in Ref. 3; AAV85960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 28134 MW; 80CE8D48CF900B8B CRC64;
MVINIFYICT GEYKRFFDKF YLSCEDKFIP EFGKKYYVFT DSDRIYFSKY LNVEVINVEK
NCWPLNTLLR FSYFLKVIDK LQTNSYTFFF NANAVIVKEI PFSTFMESDL IGVIHPGYKN
RISILYPWER RKNATCYLGY LKKGIYYQGC FNGGKTASFK RLIQICNMMT MADLKKNLIA
KVHDESYLNY YYYYNKPLLL SELYSWPEKY GENKDAKIIM RDKERESWYG NIKK
