FADL_ECOLI
ID FADL_ECOLI Reviewed; 446 AA.
AC P10384; P77697;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 5.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Long-chain fatty acid transport protein;
DE AltName: Full=Outer membrane FadL protein;
DE AltName: Full=Outer membrane flp protein;
DE Flags: Precursor;
GN Name=fadL; Synonyms=ttr; OrderedLocusNames=b2344, JW2341;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-36.
RX PubMed=1987139; DOI=10.1128/jb.173.2.435-442.1991;
RA Black P.N.;
RT "Primary sequence of the Escherichia coli fadL gene encoding an outer
RT membrane protein required for long-chain fatty acid transport.";
RL J. Bacteriol. 173:435-442(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-446.
RC STRAIN=K12;
RX PubMed=2840553; DOI=10.1111/j.1365-2958.1988.tb00040.x;
RA Said B., Ghosn C.R., Vu L., Nunn W.;
RT "Nucleotide sequencing and expression of the fadL gene involved in long-
RT chain fatty acid transport in Escherichia coli.";
RL Mol. Microbiol. 2:363-370(1988).
RN [6]
RP DIMERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 26-446.
RX PubMed=15178802; DOI=10.1126/science.1097524;
RA van den Berg B., Black P.N., Clemons W.M. Jr., Rapoport T.A.;
RT "Crystal structure of the long-chain fatty acid transporter FadL.";
RL Science 304:1506-1509(2004).
CC -!- FUNCTION: Involved in translocation of long-chain fatty acids across
CC the outer membrane. It is a receptor for the bacteriophage T2. FadL may
CC form a specific channel.
CC -!- SUBUNIT: Has been isolated from outer membrane preparation as a
CC homodimer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: By long-chain fatty acids. Expression of fadL is under the
CC control of the FadR repressor.
CC -!- SIMILARITY: Belongs to the OmpP1/FadL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64433.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA16205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA68630.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60607; AAA64433.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75404.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16205.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y00552; CAA68630.1; ALT_INIT; Genomic_DNA.
DR PIR; F65007; F65007.
DR RefSeq; NP_416846.2; NC_000913.3.
DR RefSeq; WP_001295701.1; NZ_LN832404.1.
DR PDB; 1T16; X-ray; 2.60 A; A/B=26-446.
DR PDB; 1T1L; X-ray; 2.80 A; A/B=26-446.
DR PDB; 2R4L; X-ray; 3.30 A; A/B/C=26-446.
DR PDB; 2R4N; X-ray; 3.20 A; A/B=26-446.
DR PDB; 2R4O; X-ray; 3.60 A; A/B=26-446.
DR PDB; 2R4P; X-ray; 2.90 A; A/B=26-446.
DR PDB; 2R88; X-ray; 2.60 A; A/B=26-446.
DR PDB; 2R89; X-ray; 3.40 A; A/B=31-446.
DR PDB; 2R8A; X-ray; 3.00 A; A/B=36-446.
DR PDB; 3DWN; X-ray; 2.50 A; A/B=26-446.
DR PDB; 3PF1; X-ray; 2.70 A; A/B=26-446.
DR PDB; 3PGR; X-ray; 2.60 A; A=26-446.
DR PDB; 3PGS; X-ray; 1.90 A; A/B=26-446.
DR PDB; 3PGU; X-ray; 1.70 A; A=26-446.
DR PDBsum; 1T16; -.
DR PDBsum; 1T1L; -.
DR PDBsum; 2R4L; -.
DR PDBsum; 2R4N; -.
DR PDBsum; 2R4O; -.
DR PDBsum; 2R4P; -.
DR PDBsum; 2R88; -.
DR PDBsum; 2R89; -.
DR PDBsum; 2R8A; -.
DR PDBsum; 3DWN; -.
DR PDBsum; 3PF1; -.
DR PDBsum; 3PGR; -.
DR PDBsum; 3PGS; -.
DR PDBsum; 3PGU; -.
DR AlphaFoldDB; P10384; -.
DR SMR; P10384; -.
DR BioGRID; 4260536; 118.
DR STRING; 511145.b2344; -.
DR ChEMBL; CHEMBL3309022; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.B.9.1.1; the fadl outer membrane protein (fadl) family.
DR jPOST; P10384; -.
DR PaxDb; P10384; -.
DR PRIDE; P10384; -.
DR EnsemblBacteria; AAC75404; AAC75404; b2344.
DR EnsemblBacteria; BAA16205; BAA16205; BAA16205.
DR GeneID; 946820; -.
DR KEGG; ecj:JW2341; -.
DR KEGG; eco:b2344; -.
DR PATRIC; fig|1411691.4.peg.4388; -.
DR EchoBASE; EB0276; -.
DR eggNOG; COG2067; Bacteria.
DR HOGENOM; CLU_035981_0_0_6; -.
DR InParanoid; P10384; -.
DR OMA; NRYGFTY; -.
DR PhylomeDB; P10384; -.
DR BioCyc; EcoCyc:EG10280-MON; -.
DR BioCyc; MetaCyc:EG10280-MON; -.
DR EvolutionaryTrace; P10384; -.
DR PRO; PR:P10384; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022834; F:ligand-gated channel activity; IDA:EcoCyc.
DR GO; GO:0015483; F:long-chain fatty acid transporting porin activity; IDA:EcoCyc.
DR InterPro; IPR005017; OMPP1/FadL/TodX.
DR PANTHER; PTHR35093; PTHR35093; 1.
DR Pfam; PF03349; Toluene_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Lipid transport; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1987139"
FT CHAIN 26..446
FT /note="Long-chain fatty acid transport protein"
FT /id="PRO_0000025202"
FT CONFLICT 176..178
FT /note="ARA -> RRP (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> V (in Ref. 1; AAA64433)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> R (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:3PGU"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3PGS"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 69..84
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1T1L"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2R4P"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3PGU"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 144..160
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 162..183
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 221..243
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1T1L"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 312..325
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 347..359
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 361..374
FT /evidence="ECO:0007829|PDB:3PGU"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3PGS"
FT STRAND 391..417
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:3PGU"
FT STRAND 427..446
FT /evidence="ECO:0007829|PDB:3PGU"
SQ SEQUENCE 446 AA; 48542 MW; 9B50C55D82CDB085 CRC64;
MSQKTLFTKS ALAVAVALIS TQAWSAGFQL NEFSSSGLGR AYSGEGAIAD DAGNVSRNPA
LITMFDRPTF SAGAVYIDPD VNISGTSPSG RSLKADNIAP TAWVPNMHFV APINDQFGWG
ASITSNYGLA TEFNDTYAGG SVGGTTDLET MNLNLSGAYR LNNAWSFGLG FNAVYARAKI
ERFAGDLGQL VAGQIMQSPA GQTQQGQALA ATANGIDSNT KIAHLNGNQW GFGWNAGILY
ELDKNNRYAL TYRSEVKIDF KGNYSSDLNR AFNNYGLPIP TATGGATQSG YLTLNLPEMW
EVSGYNRVDP QWAIHYSLAY TSWSQFQQLK ATSTSGDTLF QKHEGFKDAY RIALGTTYYY
DDNWTFRTGI AFDDSPVPAQ NRSISIPDQD RFWLSAGTTY AFNKDASVDV GVSYMHGQSV
KINEGPYQFE SEGKAWLFGT NFNYAF
