RFBX_ECOLI
ID RFBX_ECOLI Reviewed; 415 AA.
AC P37746; P76376;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative O-antigen transporter;
GN Name=rfbX; Synonyms=wzx; OrderedLocusNames=b2037, JW2022;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7517390; DOI=10.1128/jb.176.13.4133-4143.1994;
RA Yao Z., Valvano M.A.;
RT "Genetic analysis of the O-specific lipopolysaccharide biosynthesis region
RT (rfb) of Escherichia coli K-12 W3110: identification of genes that confer
RT group 6 specificity to Shigella flexneri serotypes Y and 4a.";
RL J. Bacteriol. 176:4133-4143(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / WG1;
RX PubMed=7517391; DOI=10.1128/jb.176.13.4144-4156.1994;
RA Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M.,
RA Redmond J.W., Lindquist L., Reeves P.R.;
RT "Structure of the O antigen of Escherichia coli K-12 and the sequence of
RT its rfb gene cluster.";
RL J. Bacteriol. 176:4144-4156(1994).
RN [3]
RP SEQUENCE REVISION TO 236.
RA Stevenson G.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: May be involved in the translocation process of the nascent
CC O-polysaccharide molecules and/or its ligation to lipid A core units.
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 polysaccharide synthase family.
CC {ECO:0000305}.
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DR EMBL; U03041; AAC31631.1; -; Genomic_DNA.
DR EMBL; U09876; AAB88402.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75098.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15879.1; -; Genomic_DNA.
DR PIR; D64969; D64969.
DR RefSeq; NP_416541.1; NC_000913.3.
DR RefSeq; WP_001393538.1; NZ_LN832404.1.
DR AlphaFoldDB; P37746; -.
DR SMR; P37746; -.
DR BioGRID; 4259620; 173.
DR STRING; 511145.b2037; -.
DR TCDB; 2.A.66.2.1; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; P37746; -.
DR PRIDE; P37746; -.
DR EnsemblBacteria; AAC75098; AAC75098; b2037.
DR EnsemblBacteria; BAA15879; BAA15879; BAA15879.
DR GeneID; 946557; -.
DR KEGG; ecj:JW2022; -.
DR KEGG; eco:b2037; -.
DR PATRIC; fig|1411691.4.peg.214; -.
DR EchoBASE; EB1923; -.
DR eggNOG; COG2244; Bacteria.
DR HOGENOM; CLU_022017_0_2_6; -.
DR InParanoid; P37746; -.
DR OMA; RTQYLIP; -.
DR PhylomeDB; P37746; -.
DR BioCyc; EcoCyc:RFBX-MON; -.
DR BioCyc; MetaCyc:RFBX-MON; -.
DR UniPathway; UPA00281; -.
DR PRO; PR:P37746; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR InterPro; IPR002797; Polysacc_synth.
DR Pfam; PF01943; Polysacc_synt; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..415
FT /note="Putative O-antigen transporter"
FT /id="PRO_0000166449"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..117
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..220
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..328
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..385
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 236
FT /note="I -> V (in Ref. 1; AAC31631)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="Q -> R (in Ref. 1; AAC31631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45383 MW; BE902BE9241CBA5F CRC64;
MNTNKLSLRR NVIYLAVVQG SNYLLPLLTF PYLVRTLGPE NFGIFGFCQA TMLYMIMFVE
YGFNLTATQS IAKAADSKDK VTSIFWAVIF SKIVLIVITL IFLTSMTLLV PEYNKHAVII
WSFVPALVGN LIYPIWLFQG KEKMKWLTLS SILSRLAIIP LTFIFVNTKS DIAIAGFIQS
SANLVAGIIA LAIVVHEGWI GKVTLSLHNV RRSLADGFHV FISTSAISLY STGIVIILGF
ISGPTSVGNF NAANTIRNAL QGLLNPITQA IYPRISSTLV LNRVKGVILI KKSLTCLSLI
GGAFSLILLL GASILVKISI GPGYDNAVIV LMIISPLPFL ISLSNVYGIQ VMLTHNYKKE
FSKILIAAGL LSLLLIFPLT TLFKEIGAAI TLLATECLVT SLMLMFVRNN KLLVC
