ID   WFAP_ECOLX              Reviewed;         251 AA.
AC   Q077R2;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfaP;
DE            EC=2.4.1.305;
GN   Name=wfaP;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC   STRAIN=O56 / G1068;
RX   PubMed=17072668; DOI=10.1007/s00284-006-0032-7;
RA   Cheng J., Wang Q., Wang W., Wang Y., Wang L., Feng L.;
RT   "Characterization of E. coli O24 and O56 O antigen gene clusters reveals a
RT   complex evolutionary history of the O24 gene cluster.";
RL   Curr. Microbiol. 53:470-476(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, AND SUBCELLULAR LOCATION.
RC   STRAIN=O56 / G1068;
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       O56-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=0.5 mM for UDP-Glc {ECO:0000269|PubMed:18487334};
CC         Vmax=1.5 umol/h/mg enzyme toward UDP-Glc
CC         {ECO:0000269|PubMed:18487334};
CC       pH dependence:
CC         Optimum pH is 6.5. {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; DQ220293; ABB29913.1; -; Genomic_DNA.
DR   RefSeq; WP_074524159.1; NZ_UFYL01000003.1.
DR   AlphaFoldDB; Q077R2; -.
DR   SMR; Q077R2; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; ag:ABB29913; -.
DR   BioCyc; MetaCyc:MON-21518; -.
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..251
FT                   /note="UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-
FT                   1,3-glucosyltransferase WfaP"
FT                   /id="PRO_0000424177"
SQ   SEQUENCE   251 AA;  28706 MW;  DFFC0BD4ED681661 CRC64;
     MELVSIIIAA YNCKDTIYAT VESALSQTYK NIEIIICDDS STDDTWDIIN KIKDSRIICI
     KNNYCKGAAG ARNCALKIAK GRYIAFLDSD DYWVTTKISN QIHFMETEKV FFSYSNYYIE
     KDFVITGVFS SPPEINYGAM LKYCNIACST VILDRTGVKN ISFPYIDKED YALWLNILSK
     GIKARNTNLV DTYYRVHAGS VSANKFKELI RQSNVLKSIG IKAHHRIICL FYYAINGLIK
     HCFSYRDKRN A