RFBV_SALTY
ID RFBV_SALTY Reviewed; 333 AA.
AC P26401;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Abequosyltransferase RfbV;
DE EC=2.4.1.60;
DE AltName: Full=O antigen biosynthesis abequosyltransferase RfbV;
GN Name=rfbV; Synonyms=ORF 14.1; OrderedLocusNames=STM2087;
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=1710759; DOI=10.1111/j.1365-2958.1991.tb00741.x;
RA Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
RT "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella
RT serovar typhimurium (strain LT2).";
RL Mol. Microbiol. 5:695-713(1991).
RN [2]
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).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=4297268; DOI=10.1016/s0021-9258(18)93419-8;
RA Osborn M.J., Weiner I.M.;
RT "Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of
RT incorporation of abequose into the O-antigen of Salmonella typhimurium.";
RL J. Biol. Chem. 243:2631-2639(1968).
RN [4]
RP FUNCTION.
RX PubMed=7541787; DOI=10.1128/jb.177.14.4084-4088.1995;
RA Liu D., Lindqvist L., Reeves P.R.;
RT "Transferases of O-antigen biosynthesis in Salmonella enterica:
RT dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of
RT group C2.";
RL J. Bacteriol. 177:4084-4088(1995).
CC -!- FUNCTION: Catalyzes the transfer of CDP-abequose on D-mannosyl-L-
CC rhamnosyl-D-galactose-1-diphospholipid to yield D-abequosyl-D-mannosyl-
CC rhamnosyl-D-galactose-1-diphospholipid. {ECO:0000269|PubMed:7541787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-
CC trans,octa-cis-undecaprenyl diphosphate + CDP-alpha-D-abequose =
CC alpha-D-Abe-(1->3)-alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-
CC di-trans,octa-cis-undecaprenyl diphosphate + CDP + H(+);
CC Xref=Rhea:RHEA:34183, ChEBI:CHEBI:15378, ChEBI:CHEBI:58069,
CC ChEBI:CHEBI:70784, ChEBI:CHEBI:157670, ChEBI:CHEBI:157673;
CC EC=2.4.1.60; Evidence={ECO:0000269|PubMed:4297268};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56793; CAA40125.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20991.1; -; Genomic_DNA.
DR PIR; S15309; S15309.
DR RefSeq; NP_461032.1; NC_003197.2.
DR RefSeq; WP_000908622.1; NC_003197.2.
DR AlphaFoldDB; P26401; -.
DR SMR; P26401; -.
DR STRING; 99287.STM2087; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; P26401; -.
DR DNASU; 1253608; -.
DR EnsemblBacteria; AAL20991; AAL20991; STM2087.
DR GeneID; 1253608; -.
DR KEGG; stm:STM2087; -.
DR PATRIC; fig|99287.12.peg.2209; -.
DR HOGENOM; CLU_067064_0_0_6; -.
DR OMA; NSILCHE; -.
DR PhylomeDB; P26401; -.
DR BioCyc; MetaCyc:STM2087-MON; -.
DR BioCyc; SENT99287:STM2087-MON; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0047600; F:abequosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
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 Glycosyltransferase; Lipopolysaccharide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..333
FT /note="Abequosyltransferase RfbV"
FT /id="PRO_0000059218"
FT CONFLICT 14
FT /note="E -> Q (in Ref. 1; CAA40125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38579 MW; 7A4DADA54D304689 CRC64;
MLISFCIPTY NRKEYLEELL NSINNQEKFN LDIEICISDN ASTDGTEEMI DVWRNNYNFP
IIYRRNSVNL GPDRNFLASV SLANGDYCWI FGSDDALAKD SLAILQTYLD SQADIYLCDR
KETGCDLVEI RNPHRSWLRT DDELYVFNNN LDREIYLSRC LSIGGVFSYL SSLIVKKERW
DAIDFDASYI GTSYPHVFIM MSVFNTPGCL LHYISKPLVI CRGDNDSFEK KGKARRILID
FIAYLKLAND FYSKNISLKR AFENVLLKER PWLYTTLAMA CYGNSDEKRD LSEFYAKLGC
NKNMINTVLR FGKLAYAVKN ITVLKNFTKR IIK
