ID LPTF_ECOLI Reviewed; 366 AA. AC P0AF98; P39340; Q2M648; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 28-JAN-2026, entry version 133. DE RecName: Full=Lipopolysaccharide export system permease protein LptF; GN Name=lptF; Synonyms=yjgP; OrderedLocusNames=b4261, JW4218; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [2] 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 [3] 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 [4] 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). RN [5] RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=18375759; DOI=10.1073/pnas.0801196105; RA Ruiz N., Gronenberg L.S., Kahne D., Silhavy T.J.; RT "Identification of two inner-membrane proteins required for the transport RT of lipopolysaccharide to the outer membrane of Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5537-5542(2008). RN [6] RP SUBUNIT, AND INTERACTION WITH LPTB AND LPTG. RX PubMed=19500581; DOI=10.1016/j.febslet.2009.05.051; RA Narita S., Tokuda H.; RT "Biochemical characterization of an ABC transporter LptBFGC complex RT required for the outer membrane sorting of lipopolysaccharides."; RL FEBS Lett. 583:2160-2164(2009). 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:0000269|PubMed:18375759}. 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). CC {ECO:0000269|PubMed:19500581}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the LptF/LptG 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; U14003; AAA97158.1; -; Genomic_DNA. DR EMBL; U00096; AAC77218.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78258.1; -; Genomic_DNA. DR PIR; S56487; S56487. DR RefSeq; NP_418682.1; NC_000913.3. DR RefSeq; WP_000584114.1; NZ_CP009789.1. DR PDB; 6MHU; EM; 4.00 A; F=1-366. DR PDB; 6MHZ; EM; 4.10 A; F=1-366. DR PDB; 6MI7; EM; 4.20 A; F=1-366. DR PDB; 6MI8; EM; 4.30 A; F=1-366. DR AlphaFoldDB; P0AF98; -. DR EMDB; EMD-9118; -. DR EMDB; EMD-9124; -. DR EMDB; EMD-9125; -. DR EMDB; EMD-9126; -. DR SMR; P0AF98; -. DR BioGRID; 4262727; 260. DR ComplexPortal; CPX-3861; lptBFG LPS ABC transporter complex. DR FunCoup; P0AF98; 299. DR IntAct; P0AF98; 1. DR MINT; P0AF98; -. DR STRING; 511145.b4261; -. DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family. DR jPOST; P0AF98; -. DR PaxDb; 511145-b4261; -. DR DNASU; 948795; -. DR EnsemblBacteria; AAC77218; AAC77218; b4261. DR GeneID; 75169782; -. DR GeneID; 75203518; -. DR GeneID; 948795; -. DR KEGG; ecj:JW4218; -. DR KEGG; eco:b4261; -. DR KEGG; ecoc:C3026_22985; -. DR PATRIC; fig|511145.12.peg.4392; -. DR EchoBASE; EB2424; -. DR eggNOG; COG0795; Bacteria. DR HOGENOM; CLU_028799_0_2_6; -. DR InParanoid; P0AF98; -. DR OMA; NYISSMI; -. DR OrthoDB; 9778062at2; -. DR PhylomeDB; P0AF98; -. DR BioCyc; EcoCyc:G7888-MONOMER; -. DR BioCyc; MetaCyc:G7888-MONOMER; -. DR PRO; PR:P0AF98; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; IDA:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:1990351; C:transporter complex; IDA:EcoCyc. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:ComplexPortal. DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:ComplexPortal. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030922; LptF. DR InterPro; IPR005495; LptG/LptF_permease. DR NCBIfam; TIGR04407; LptF_YjgP; 1. DR PANTHER; PTHR33529:SF7; LIPOPOLYSACCHARIDE EXPORT SYSTEM PERMEASE PROTEIN LPTF; 1. DR PANTHER; PTHR33529; SLR0882 PROTEIN-RELATED; 1. DR Pfam; PF03739; LptF_LptG; 1. DR PDBsum; 6MHU; -. DR PDBsum; 6MHZ; -. DR PDBsum; 6MI7; -. DR PDBsum; 6MI8; -. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..366 FT /note="Lipopolysaccharide export system permease protein FT LptF" FT /id="PRO_0000169771" 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 //