WBNH_ECOLX
ID WBNH_ECOLX Reviewed; 338 AA.
AC P0DMP6; Q5J7D6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=O-antigen biosynthesis glycosyltransferase WbnH {ECO:0000305};
DE EC=2.4.1.306 {ECO:0000269|PubMed:16630548, ECO:0000269|PubMed:20418877};
DE AltName: Full=UDP-GalNAc:alpha-D-GalNAc-diphosphoundecaprenol alpha-1,3-N-acetylgalactosaminyltransferase {ECO:0000305};
GN Name=wbnH {ECO:0000303|PubMed:15713070};
GN Synonyms=wbwH {ECO:0000303|PubMed:16332778},
GN wcmA {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].
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:H2;
RX PubMed=16630548; DOI=10.1016/j.bbrc.2006.03.181;
RA Yi W., Yao Q., Zhang Y., Motari E., Lin S., Wang P.G.;
RT "The wbnH gene of Escherichia coli O86:H2 encodes an alpha-1,3-N-
RT acetylgalactosaminyl transferase involved in the O-repeating unit
RT biosynthesis.";
RL Biochem. Biophys. Res. Commun. 344:631-639(2006).
RN [5]
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:16630548,
CC ECO:0000269|PubMed:20418877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate + UDP-N-acetyl-alpha-D-galactosamine = alpha-D-GalNAc-
CC (1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate +
CC H(+) + UDP; Xref=Rhea:RHEA:36759, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:73987,
CC ChEBI:CHEBI:74214; EC=2.4.1.306;
CC Evidence={ECO:0000269|PubMed:16630548, ECO:0000269|PubMed:20418877};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:16630548,
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 group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AY220982; AAO37709.1; -; Genomic_DNA.
DR EMBL; AY667408; AAV80749.1; -; Genomic_DNA.
DR EMBL; AY670704; AAV85953.1; -; Genomic_DNA.
DR RefSeq; WP_000799972.1; NZ_WSXE01000068.1.
DR PDB; 4XYW; X-ray; 2.20 A; A=1-338.
DR PDBsum; 4XYW; -.
DR AlphaFoldDB; P0DMP6; -.
DR SMR; P0DMP6; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR KEGG; ag:AAV80749; -.
DR BioCyc; MetaCyc:MON-18063; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Lipopolysaccharide biosynthesis;
KW Transferase.
FT CHAIN 1..338
FT /note="O-antigen biosynthesis glycosyltransferase WbnH"
FT /id="PRO_0000430647"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:4XYW"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4XYW"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4XYW"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:4XYW"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4XYW"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:4XYW"
SQ SEQUENCE 338 AA; 38148 MW; C3A813A3EE248251 CRC64;
MKNVGFIVTK SEIGGAQTWV NEISNLIKEE CNIFLITSEE GWLTHKDVFA GVFVIPGIKK
YFDFLTLFKL RKILKENNIS TLIASSANAG VYARLVRLLV DFKCIYVSHG WSCLYNGGRL
KSIFCIVEKY LSLLTDVIWC VSKSDEKKAI ENIGIKEPKI ITVSNSVPQM PRCNNKQLQY
KVLFVGRLTH PKRPELLANV ISKKPQYSLH IVGGGERLES LKKQFSECEN IHFLGEVNNF
YNYHEYDLFS LISDSEGLPM SGLEAHTAAI PLLLSDVGGC FELIEGNGLL VENTEDDIGY
KLDKIFDDYE NYREQAIRAS GKFVIENYAS AYKSIILG
