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Protein

Long-chain fatty acid transport protein

Gene

fadL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel.

GO - Molecular functioni

  • ligand-gated channel activity Source: EcoCyc
  • long-chain fatty acid transporting porin activity Source: EcoCyc

GO - Biological processi

  • long-chain fatty acid transport Source: GOC
  • monocarboxylic acid transport Source: GOC
  • transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG10280-MONOMER.
ECOL316407:JW2341-MONOMER.
MetaCyc:EG10280-MONOMER.

Protein family/group databases

TCDBi1.B.9.1.1. the fadl outer membrane protein (fadl) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain fatty acid transport protein
Alternative name(s):
Outer membrane FadL protein
Outer membrane flp protein
Gene namesi
Name:fadL
Synonyms:ttr
Ordered Locus Names:b2344, JW2341
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10280. fadL.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 446421Long-chain fatty acid transport proteinPRO_0000025202Add
BLAST

Proteomic databases

EPDiP10384.
PaxDbiP10384.
PRIDEiP10384.

Expressioni

Inductioni

By long-chain fatty acids. Expression of fadL is under the control of the FadR repressor.

Interactioni

Subunit structurei

Has been isolated from outer membrane preparation as a homodimer.

Protein-protein interaction databases

BioGridi4260536. 111 interactions.
STRINGi511145.b2344.

Structurei

Secondary structure

1
446
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395Combined sources
Turni40 – 423Combined sources
Turni45 – 473Combined sources
Helixi52 – 565Combined sources
Helixi59 – 646Combined sources
Beta strandi69 – 8416Combined sources
Beta strandi90 – 923Combined sources
Beta strandi95 – 973Combined sources
Beta strandi102 – 11211Combined sources
Beta strandi114 – 12411Combined sources
Beta strandi127 – 1326Combined sources
Turni138 – 1425Combined sources
Beta strandi144 – 16017Combined sources
Beta strandi162 – 18322Combined sources
Helixi187 – 19711Combined sources
Helixi199 – 2024Combined sources
Helixi204 – 21411Combined sources
Beta strandi221 – 24323Combined sources
Beta strandi246 – 2538Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi263 – 2653Combined sources
Turni272 – 2765Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi298 – 30912Combined sources
Beta strandi312 – 32514Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi337 – 3426Combined sources
Beta strandi347 – 35913Combined sources
Beta strandi361 – 37414Combined sources
Helixi379 – 3813Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi391 – 41727Combined sources
Beta strandi420 – 4245Combined sources
Beta strandi427 – 44620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T16X-ray2.60A/B26-446[»]
1T1LX-ray2.80A/B26-446[»]
2R4LX-ray3.30A/B/C26-446[»]
2R4NX-ray3.20A/B26-446[»]
2R4OX-ray3.60A/B26-446[»]
2R4PX-ray2.90A/B26-446[»]
2R88X-ray2.60A/B26-446[»]
2R89X-ray3.40A/B31-446[»]
2R8AX-ray3.00A/B36-446[»]
3DWNX-ray2.50A/B26-446[»]
3PF1X-ray2.70A/B26-446[»]
3PGRX-ray2.60A26-446[»]
3PGSX-ray1.90A/B26-446[»]
3PGUX-ray1.70A26-446[»]
ProteinModelPortaliP10384.
SMRiP10384. Positions 26-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10384.

Family & Domainsi

Sequence similaritiesi

Belongs to the OmpP1/FadL family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105CKF. Bacteria.
COG2067. LUCA.
HOGENOMiHOG000277333.
InParanoidiP10384.
KOiK06076.
OMAiNRYGFTY.
OrthoDBiEOG6Z0Q6D.
PhylomeDBiP10384.

Family and domain databases

InterProiIPR005017. OMPP1/FadL/TodX.
[Graphical view]
PfamiPF03349. Toluene_X. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKTLFTKS ALAVAVALIS TQAWSAGFQL NEFSSSGLGR AYSGEGAIAD
60 70 80 90 100
DAGNVSRNPA LITMFDRPTF SAGAVYIDPD VNISGTSPSG RSLKADNIAP
110 120 130 140 150
TAWVPNMHFV APINDQFGWG ASITSNYGLA TEFNDTYAGG SVGGTTDLET
160 170 180 190 200
MNLNLSGAYR LNNAWSFGLG FNAVYARAKI ERFAGDLGQL VAGQIMQSPA
210 220 230 240 250
GQTQQGQALA ATANGIDSNT KIAHLNGNQW GFGWNAGILY ELDKNNRYAL
260 270 280 290 300
TYRSEVKIDF KGNYSSDLNR AFNNYGLPIP TATGGATQSG YLTLNLPEMW
310 320 330 340 350
EVSGYNRVDP QWAIHYSLAY TSWSQFQQLK ATSTSGDTLF QKHEGFKDAY
360 370 380 390 400
RIALGTTYYY DDNWTFRTGI AFDDSPVPAQ NRSISIPDQD RFWLSAGTTY
410 420 430 440
AFNKDASVDV GVSYMHGQSV KINEGPYQFE SEGKAWLFGT NFNYAF
Length:446
Mass (Da):48,542
Last modified:December 12, 2006 - v5
Checksum:i9B50C55D82CDB085
GO

Sequence cautioni

The sequence AAA64433.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA16205.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA68630.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1783ARA → RRP (PubMed:2840553).Curated
Sequence conflicti176 – 1761A → V in AAA64433 (PubMed:1987139).Curated
Sequence conflicti286 – 2861A → R (PubMed:1987139).Curated
Sequence conflicti286 – 2861A → R (PubMed:2840553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60607 Genomic DNA. Translation: AAA64433.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75404.2.
AP009048 Genomic DNA. Translation: BAA16205.1. Different initiation.
Y00552 Genomic DNA. Translation: CAA68630.1. Different initiation.
PIRiF65007.
RefSeqiNP_416846.2. NC_000913.3.
WP_001295701.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75404; AAC75404; b2344.
BAA16205; BAA16205; BAA16205.
GeneIDi946820.
KEGGiecj:JW2341.
eco:b2344.
PATRICi32120061. VBIEscCol129921_2440.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60607 Genomic DNA. Translation: AAA64433.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75404.2.
AP009048 Genomic DNA. Translation: BAA16205.1. Different initiation.
Y00552 Genomic DNA. Translation: CAA68630.1. Different initiation.
PIRiF65007.
RefSeqiNP_416846.2. NC_000913.3.
WP_001295701.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T16X-ray2.60A/B26-446[»]
1T1LX-ray2.80A/B26-446[»]
2R4LX-ray3.30A/B/C26-446[»]
2R4NX-ray3.20A/B26-446[»]
2R4OX-ray3.60A/B26-446[»]
2R4PX-ray2.90A/B26-446[»]
2R88X-ray2.60A/B26-446[»]
2R89X-ray3.40A/B31-446[»]
2R8AX-ray3.00A/B36-446[»]
3DWNX-ray2.50A/B26-446[»]
3PF1X-ray2.70A/B26-446[»]
3PGRX-ray2.60A26-446[»]
3PGSX-ray1.90A/B26-446[»]
3PGUX-ray1.70A26-446[»]
ProteinModelPortaliP10384.
SMRiP10384. Positions 26-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260536. 111 interactions.
STRINGi511145.b2344.

Protein family/group databases

TCDBi1.B.9.1.1. the fadl outer membrane protein (fadl) family.

Proteomic databases

EPDiP10384.
PaxDbiP10384.
PRIDEiP10384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75404; AAC75404; b2344.
BAA16205; BAA16205; BAA16205.
GeneIDi946820.
KEGGiecj:JW2341.
eco:b2344.
PATRICi32120061. VBIEscCol129921_2440.

Organism-specific databases

EchoBASEiEB0276.
EcoGeneiEG10280. fadL.

Phylogenomic databases

eggNOGiENOG4105CKF. Bacteria.
COG2067. LUCA.
HOGENOMiHOG000277333.
InParanoidiP10384.
KOiK06076.
OMAiNRYGFTY.
OrthoDBiEOG6Z0Q6D.
PhylomeDBiP10384.

Enzyme and pathway databases

BioCyciEcoCyc:EG10280-MONOMER.
ECOL316407:JW2341-MONOMER.
MetaCyc:EG10280-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP10384.
PROiP10384.

Family and domain databases

InterProiIPR005017. OMPP1/FadL/TodX.
[Graphical view]
PfamiPF03349. Toluene_X. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary sequence of the Escherichia coli fadL gene encoding an outer membrane protein required for long-chain fatty acid transport."
    Black P.N.
    J. Bacteriol. 173:435-442(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-36.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequencing and expression of the fadL gene involved in long-chain fatty acid transport in Escherichia coli."
    Said B., Ghosn C.R., Vu L., Nunn W.
    Mol. Microbiol. 2:363-370(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-446.
    Strain: K12.
  6. Cited for: DIMERIZATION, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  7. "Crystal structure of the long-chain fatty acid transporter FadL."
    van den Berg B., Black P.N., Clemons W.M. Jr., Rapoport T.A.
    Science 304:1506-1509(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 26-446.

Entry informationi

Entry nameiFADL_ECOLI
AccessioniPrimary (citable) accession number: P10384
Secondary accession number(s): P77697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 12, 2006
Last modified: March 16, 2016
This is version 147 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.