RFAI_SALTY
ID RFAI_SALTY Reviewed; 337 AA.
AC P19816; O68267;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 4.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lipopolysaccharide 1,3-galactosyltransferase;
DE EC=2.4.1.44;
DE AltName: Full=Lipopolysaccharide 3-alpha-galactosyltransferase;
GN Name=rfaI; Synonyms=waaI; OrderedLocusNames=STM3718;
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 galactose(I) group on the glucose(I) group of LPS.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-galactose + [lipopolysaccharide] = UDP + 3-alpha-
CC D-galactosyl-[lipopolysaccharide].; EC=2.4.1.44;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37841.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X53847; CAA37841.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF026386; AAC16412.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22577.1; -; Genomic_DNA.
DR PIR; S12097; S12097.
DR RefSeq; NP_462618.1; NC_003197.2.
DR RefSeq; WP_000088479.1; NC_003197.2.
DR AlphaFoldDB; P19816; -.
DR SMR; P19816; -.
DR STRING; 99287.STM3718; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; P19816; -.
DR EnsemblBacteria; AAL22577; AAL22577; STM3718.
DR GeneID; 1255242; -.
DR KEGG; stm:STM3718; -.
DR PATRIC; fig|99287.12.peg.3932; -.
DR HOGENOM; CLU_050833_5_0_6; -.
DR OMA; TVFLHFC; -.
DR PhylomeDB; P19816; -.
DR BioCyc; MetaCyc:STM3718-MON; -.
DR BioCyc; SENT99287:STM3718-MON; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0008918; F:lipopolysaccharide 3-alpha-galactosyltransferase 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..337
FT /note="Lipopolysaccharide 1,3-galactosyltransferase"
FT /id="PRO_0000206065"
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 28..33
FT /note="FNIAYG -> LYSLW (in Ref. 1; CAA37841)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> R (in Ref. 1; CAA37841)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="E -> Q (in Ref. 2; AAC16412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 38905 MW; 6DB1FA1531AE25F7 CRC64;
MSRKYFEEEV IQQTLDYNYA QHSDADKFNI AYGIDKNFLF GCGVSIASVL LANPEKALAF
HVFTDFFDSE DQQRFEALAK QYATQIVVYL IDCERLKSLP STKNWTYATY FRFIIADYFS
DKTDRVLYLD ADIACKGSIQ ELIDLNFAEN EIAAVVAEGE LEWWTKRSVS LATPGLVSGY
FNAGFILINI PLWTAENISK KAIEMLKDPE VVQRITHLDQ DVLNIFLVNK ARFVDKKFNT
QFSLNYELKD SVINPVDAET VFVHYIGPTK PWHSWGAYPV SQYFLQAKSN SPWSHCALLN
PVTSHQLRYA AKHMFNQKHY TSGINYYIAY FKRKLLE
