RFAJ_ECOLI
ID RFAJ_ECOLI Reviewed; 338 AA.
AC P27129; Q2M7U0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Lipopolysaccharide 1,2-glucosyltransferase;
DE EC=2.4.1.58;
GN Name=rfaJ; Synonyms=waaJ; OrderedLocusNames=b3626, JW3601;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1624461; DOI=10.1128/jb.174.14.4736-4745.1992;
RA Pradel E., Parker C.T., Schnaitman C.A.;
RT "Structures of the rfaB, rfaI, rfaJ, and rfaS genes of Escherichia coli K-
RT 12 and their roles in assembly of the lipopolysaccharide core.";
RL J. Bacteriol. 174:4736-4745(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Adds the glucose(II) group on the galactose(I) group of LPS.
CC {ECO:0000250|UniProtKB:P19817}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-glucose + [lipopolysaccharide] = UDP + D-glucosyl-
CC [lipopolysaccharide].; EC=2.4.1.58;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; M80599; AAA24087.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18603.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76650.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77666.1; -; Genomic_DNA.
DR PIR; S47847; S47847.
DR RefSeq; NP_418083.1; NC_000913.3.
DR RefSeq; WP_000376841.1; NZ_LN832404.1.
DR AlphaFoldDB; P27129; -.
DR SMR; P27129; -.
DR BioGRID; 4261893; 196.
DR DIP; DIP-10671N; -.
DR IntAct; P27129; 6.
DR STRING; 511145.b3626; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR jPOST; P27129; -.
DR PaxDb; P27129; -.
DR PRIDE; P27129; -.
DR EnsemblBacteria; AAC76650; AAC76650; b3626.
DR EnsemblBacteria; BAE77666; BAE77666; BAE77666.
DR GeneID; 948142; -.
DR KEGG; ecj:JW3601; -.
DR KEGG; eco:b3626; -.
DR PATRIC; fig|1411691.4.peg.3080; -.
DR EchoBASE; EB1328; -.
DR eggNOG; COG1442; Bacteria.
DR HOGENOM; CLU_050833_5_0_6; -.
DR InParanoid; P27129; -.
DR OMA; HFTGHDK; -.
DR PhylomeDB; P27129; -.
DR BioCyc; EcoCyc:EG11353-MON; -.
DR BioCyc; MetaCyc:EG11353-MON; -.
DR UniPathway; UPA00958; -.
DR PRO; PR:P27129; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008918; F:lipopolysaccharide 3-alpha-galactosyltransferase activity; IEA:InterPro.
DR GO; GO:0008919; F:lipopolysaccharide glucosyltransferase I activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR013645; Glyco_transf_8N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR Pfam; PF08437; Glyco_transf_8C; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Manganese;
KW Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..338
FT /note="Lipopolysaccharide 1,2-glucosyltransferase"
FT /id="PRO_0000206066"
FT BINDING 33..38
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 130..131
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 264..270
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT CONFLICT 310..338
FT /note="RYKHLLVQHHYISGIIAGVCYLCRKYYRK -> DINIF (in Ref. 1;
FT AAA24087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 39040 MW; 819428EA13F1959A CRC64;
MDSFPAIEID KVKAWDFRLA NINTSECLNV AYGVDANYLD GVGVSITSIV LNNRHINLDF
YIIADVYNDG FFQKIAKLAE QNQLRITLYR INTDKLQCLP CTQVWSRAMY FRLFAFQLLG
LTLDRLLYLD ADVVCKGDIS QLLHLGLNGA VAAVVKDVEP MQEKAVSRLS DPELLGQYFN
SGVVYLDLKK WADAKLTEKA LSILMSKDNV YKYPDQDVMN VLLKGMTLFL PREYNTIYTI
KSELKDKTHQ NYKKLITEST LLIHYTGATK PWHKWAIYPS VKYYKIALEN SPWKDDSPRD
AKSIIEFKKR YKHLLVQHHY ISGIIAGVCY LCRKYYRK
