WBNJ_ECOLX
ID WBNJ_ECOLX Reviewed; 254 AA.
AC Q4KXC9; Q58YW0; Q5JBG4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=O-antigen biosynthesis glycosyltransferase WbnJ {ECO:0000305};
DE EC=2.4.1.122 {ECO:0000269|PubMed:15713070, ECO:0000269|PubMed:20418877};
DE AltName: Full=UDP-Gal:alpha-D-GalNAc-1,3-alpha-D-GalNAc-diphosphoundecaprenol beta-1,3-galactosyltransferase {ECO:0000305};
GN Name=wbnJ {ECO:0000303|PubMed:15713070};
GN Synonyms=wbwJ {ECO:0000303|PubMed:16332778},
GN wcmC {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=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000269|PubMed:15713070, ECO:0000269|PubMed:20418877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-
CC undecaprenyl diphosphate + UDP-alpha-D-galactose = beta-D-Gal-(1->3)-
CC alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl
CC diphosphate + H(+) + UDP; Xref=Rhea:RHEA:36763, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:73987,
CC ChEBI:CHEBI:73988; 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 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV85962.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY220982; AAO37718.1; -; Genomic_DNA.
DR EMBL; AY667408; AAV80758.1; -; Genomic_DNA.
DR EMBL; AY670704; AAV85962.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q4KXC9; -.
DR SMR; Q4KXC9; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; ag:AAV80758; -.
DR BioCyc; MetaCyc:MON-18062; -.
DR BRENDA; 2.4.1.122; 2026.
DR UniPathway; UPA00281; -.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009243; P:O antigen 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 Glycosyltransferase; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..254
FT /note="O-antigen biosynthesis glycosyltransferase WbnJ"
FT /id="PRO_0000430649"
FT CONFLICT 16
FT /note="H -> R (in Ref. 1; AAO37718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29849 MW; 020B6B53F78899F9 CRC64;
MSLRILDMIS VIMAVHRYDK YVDISIDSIL NQTYSDFELI IIANGGDCFE IAKQLKHYTE
LDNRVKIYTL EIGQLSFALN YAVTKCKYSI IARMDSDDVS LPLRLEKQYM YMLQNDLEMV
GTGIRLINEN GEFIKELKYP NHNKINKILP FKNCFAHPTL MFKKDVILKQ RGYCGGFNSE
DYDLWLRILN ECPNIRWDNL SECLLNYRIH NKSTQKSALA YYECASYSLR EFLKKRTITN
FLSCLYHFCK ALIK
