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