ID   LPTF_ECO57              Reviewed;         366 AA.
AC   P0AFA0; P39340;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Lipopolysaccharide export system permease protein LptF;
GN   Name=lptF; OrderedLocusNames=Z5873, ECs5238;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in the
CC       translocation of lipopolysaccharide (LPS) from the inner membrane to
CC       the outer membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. The LptBFG transporter is composed of two ATP-binding proteins
CC       (LptB) and two transmembrane proteins (LptF and LptG) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LptF/LptG family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG59460.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38661.1; -; Genomic_DNA.
DR   PIR; F91283; F91283.
DR   PIR; H86124; H86124.
DR   RefSeq; NP_313265.1; NC_002695.1.
DR   RefSeq; WP_000584114.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFA0; -.
DR   SMR; P0AFA0; -.
DR   STRING; 155864.EDL933_5611; -.
DR   EnsemblBacteria; AAG59460; AAG59460; Z5873.
DR   EnsemblBacteria; BAB38661; BAB38661; ECs_5238.
DR   GeneID; 66671820; -.
DR   GeneID; 913803; -.
DR   KEGG; ece:Z5873; -.
DR   KEGG; ecs:ECs_5238; -.
DR   PATRIC; fig|386585.9.peg.5476; -.
DR   eggNOG; COG0795; Bacteria.
DR   HOGENOM; CLU_028799_0_2_6; -.
DR   OMA; ELQWRIA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030922; LptF.
DR   InterPro; IPR005495; LptG/LptF_permease.
DR   PANTHER; PTHR33529; PTHR33529; 1.
DR   Pfam; PF03739; LptF_LptG; 1.
DR   TIGRFAMs; TIGR04407; LptF_YjgP; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..366
FT                   /note="Lipopolysaccharide export system permease protein
FT                   LptF"
FT                   /id="PRO_0000169772"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..53
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..269
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..327
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  40358 MW;  69A564AA22CBFFEA CRC64;
     MIIIRYLVRE TLKSQLAILF ILLLIFFCQK LVRILGAAVD GDIPANLVLS LLGLGVPEMA
     QLILPLSLFL GLLMTLGKLY TESEITVMHA CGLSKAVLVK AAMILAVFTA IVAAVNVMWA
     GPWSSRHQDE VLAEAKANPG MAALAQGQFQ QATNGSSVLF IESVDGSDFK DVFLAQIRPK
     GNARPSVVVA DSGHLTQLRD GSQVVTLNQG TRFEGTALLR DFRITDFQDY QAIIGHQAVA
     LDPNDTDQMD MRTLWNTDTD RARAELNWRI TLVFTVFMMA LMVVPLSVVN PRQGRVLSML
     PAMLLYLLFF LIQTSLKSNG GKGKLDPTLW MWTVNLIYLA LAIVLNLWDT VPVRRLRASF
     SRKGAV