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LPTF_ECOLI
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   03-AUG-2022, entry version 119.
DE   RecName: Full=Lipopolysaccharide export system permease protein LptF;
GN   Name=lptF; Synonyms=yjgP; OrderedLocusNames=b4261, JW4218;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   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}.
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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_STEB01000013.1.
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   PDBsum; 6MHU; -.
DR   PDBsum; 6MHZ; -.
DR   PDBsum; 6MI7; -.
DR   PDBsum; 6MI8; -.
DR   AlphaFoldDB; P0AF98; -.
DR   SMR; P0AF98; -.
DR   BioGRID; 4262727; 260.
DR   ComplexPortal; CPX-3861; lptBFG LPS ABC transporter complex.
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; P0AF98; -.
DR   PRIDE; P0AF98; -.
DR   DNASU; 948795; -.
DR   EnsemblBacteria; AAC77218; AAC77218; b4261.
DR   EnsemblBacteria; BAE78258; BAE78258; BAE78258.
DR   GeneID; 66671820; -.
DR   GeneID; 948795; -.
DR   KEGG; ecj:JW4218; -.
DR   KEGG; eco:b4261; -.
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; ELQWRIA; -.
DR   PhylomeDB; P0AF98; -.
DR   BioCyc; EcoCyc:G7888-MON; -.
DR   BioCyc; MetaCyc:G7888-MON; -.
DR   PRO; PR:P0AF98; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR   GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
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; IC: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   PANTHER; PTHR33529; PTHR33529; 1.
DR   Pfam; PF03739; LptF_LptG; 1.
DR   TIGRFAMs; TIGR04407; LptF_YjgP; 1.
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
 
 
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