ID   RFBP_SALTY              Reviewed;         476 AA.
AC   P26406;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Undecaprenyl-phosphate galactose phosphotransferase;
DE            EC=2.7.8.6;
DE   AltName: Full=Galactosyl-P-P-undecaprenol synthase;
GN   Name=rfbP; OrderedLocusNames=STM2082;
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).
CC   -!- FUNCTION: Is responsible for transferring galactose-1-phosphate to the
CC       lipid precursor undecaprenol phosphate in the first steps of O-
CC       polysaccharide biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-
CC         galactose = alpha-D-galactosyl-di-trans,octa-cis-undecaprenyl
CC         diphosphate + UMP; Xref=Rhea:RHEA:11652, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:66914, ChEBI:CHEBI:138733; EC=2.7.8.6;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; X56793; CAA40130.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20986.1; -; Genomic_DNA.
DR   PIR; S15314; S15314.
DR   RefSeq; NP_461027.1; NC_003197.2.
DR   RefSeq; WP_000368707.1; NC_003197.2.
DR   AlphaFoldDB; P26406; -.
DR   SMR; P26406; -.
DR   STRING; 99287.STM2082; -.
DR   PaxDb; P26406; -.
DR   DNASU; 1253603; -.
DR   EnsemblBacteria; AAL20986; AAL20986; STM2082.
DR   GeneID; 1253603; -.
DR   KEGG; stm:STM2082; -.
DR   PATRIC; fig|99287.12.peg.2204; -.
DR   HOGENOM; CLU_024920_3_5_6; -.
DR   OMA; MFSHEMM; -.
DR   PhylomeDB; P26406; -.
DR   BioCyc; MetaCyc:STM2082-MON; -.
DR   BioCyc; SENT99287:STM2082-MON; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
DR   GO; GO:0047360; F:undecaprenyl-phosphate galactose phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003362; Bact_transf.
DR   InterPro; IPR017475; EPS_sugar_tfrase.
DR   InterPro; IPR017472; Undecaprenyl-P_galact_Ptfrase.
DR   Pfam; PF02397; Bac_transf; 1.
DR   TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
DR   TIGRFAMs; TIGR03022; WbaP_sugtrans; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..476
FT                   /note="Undecaprenyl-phosphate galactose phosphotransferase"
FT                   /id="PRO_0000166468"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="Y -> I (in Ref. 1; CAA40130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  56198 MW;  E8F205F8353F7C12 CRC64;
     MDNIDNKYNP QLCKIFLAIS DLIFFNLALW FSLGCVYFIF DQVQRFIPQD QLDTRVITHF
     ILSVVCVGWF WIRLRHYTYR KPFWYELKEI FRTIVIFAIF DLALIAFTKW QFSRYVWVFC
     WTFALILVPF FRALTKHLLN KLGIWKKKTI ILGSGQNARG AYSALQSEEM MGFDVIAFFD
     TDASDAEINM LPVIKDTEII WDLNRTGDVH YILAYEYTEL EKTHFWLREL SKHHCRSVTV
     VPSFRGLPLY NTDMSFIFSH EVMLLRIQNN LAKRSSRFLK RTFDIVCSIM ILIIASPLMI
     YLWYKVTRDG GPAIYGHQRV GRHGKLFPCY KFRSMVMNSQ EVLKELLAND PIARAEWEKD
     FKLKNDPRIT AVGRFIRKTS LDELPQLFNV LKGDMSLVGP RPIVSDELER YCDDVDYYLM
     AKPGMTGLWQ VSGRNDVDYD TRVYFDSWYV KNWTLWNDIA ILFKTAKVVL RRDGAY