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RFAJ_SALTY
ID   RFAJ_SALTY              Reviewed;         336 AA.
AC   P19817; O68266;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 4.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Lipopolysaccharide 1,2-glucosyltransferase;
DE            EC=2.4.1.58;
GN   Name=rfaJ; Synonyms=waaJ; OrderedLocusNames=STM3717;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2235496; DOI=10.1093/nar/18.20.6128;
RA   Carstenius P., Flock J.-I., Lindberg A.;
RT   "Nucleotide sequence of rfaI and rfaJ genes encoding lipopolysaccharide
RT   glycosyl transferases from Salmonella typhimurium.";
RL   Nucleic Acids Res. 18:6128-6128(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=9535865; DOI=10.1074/jbc.273.15.8849;
RA   Heinrichs D.E., Monteiro M.A., Perry M.B., Whitfield C.;
RT   "The assembly system for the lipopolysaccharide R2 core-type of Escherichia
RT   coli is a hybrid of those found in Escherichia coli K-12 and Salmonella
RT   enterica. Structure and function of the R2 WaaK and WaaL homologs.";
RL   J. Biol. Chem. 273:8849-8859(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Adds the glucose(II) group on the galactose(I) group of LPS.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA37842.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X53847; CAA37842.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AF026386; AAC16411.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22576.1; -; Genomic_DNA.
DR   PIR; S12098; S12098.
DR   RefSeq; NP_462617.1; NC_003197.2.
DR   RefSeq; WP_000376865.1; NC_003197.2.
DR   AlphaFoldDB; P19817; -.
DR   SMR; P19817; -.
DR   STRING; 99287.STM3717; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; P19817; -.
DR   EnsemblBacteria; AAL22576; AAL22576; STM3717.
DR   GeneID; 1255241; -.
DR   KEGG; stm:STM3717; -.
DR   PATRIC; fig|99287.12.peg.3931; -.
DR   HOGENOM; CLU_050833_5_0_6; -.
DR   OMA; YMNEICE; -.
DR   PhylomeDB; P19817; -.
DR   BioCyc; MetaCyc:STM3717-MON; -.
DR   BioCyc; SENT99287:STM3717-MON; -.
DR   SABIO-RK; P19817; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008918; F:lipopolysaccharide 3-alpha-galactosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008919; F:lipopolysaccharide glucosyltransferase I activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
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..336
FT                   /note="Lipopolysaccharide 1,2-glucosyltransferase"
FT                   /id="PRO_0000206067"
FT   BINDING         31..36
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         127..128
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         127
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         129
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         262..268
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H2URJ6"
SQ   SEQUENCE   336 AA;  38763 MW;  AAB23E412429E00B CRC64;
     MDSFPEIEIA EYKVFDESNN NDDNVLNISY GVDENYLDGV GVSIASVVLN NNIPLAFHII
     CDSYSPCFVK YIERLAVQHH IKISLYLIKV ESLEVLPQTK VWSRAMYFRL FAFDYLSKKV
     NTLLYLDADV VCKGSLQDLL QLDLTEKIAA VVKDVDSIQN KVNERLSAFN LQGGYFNSGV
     VFVNLKLWKE NALTKKAFLL LAGKEADSFK YPDQDVLNIL LQDKVIFLPR PYNTIYTIKS
     ELKDKSHKKY SNIINDNTIL IHYTGATKPW HAWANYPSVI YYKNARLNSP WKDFPAKDAR
     TIVEFKKRYK HLLVQGHYFK GLLAGSAYLY RKLFHK
 
 
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