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ECOLI:FEPA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fepA (synonyms: fep, feuB)
Protein Name(s) Ferrienterobactin receptor

Enterobactin outer-membrane receptor

External Links
UniProt P05825
EMBL M13748
U82598
U00096
AP009048
J04216
PIR F64791
RefSeq NP_415116.1
YP_488872.1
PDB 1FEP
PDBsum 1FEP
ProteinModelPortal P05825
SMR P05825
DIP DIP-9592N
IntAct P05825
STRING 511145.b0584
TCDB 1.B.14.1.22
SWISS-2DPAGE P05825
PaxDb P05825
PRIDE P05825
EnsemblBacteria AAC73685
BAA35225
GeneID 12934080
945193
KEGG ecj:Y75_p0572
eco:b0584
PATRIC 32116338
EchoBASE EB0289
EcoGene EG10293
eggNOG COG4771
HOGENOM HOG000276827
InParanoid P05825
KO K16089
OMA YRQNYAV
OrthoDB EOG68H83J
PhylomeDB P05825
BioCyc EcoCyc:EG10293-MONOMER
ECOL316407:JW5086-MONOMER
MetaCyc:EG10293-MONOMER
EvolutionaryTrace P05825
PRO PR:P05825
Proteomes UP000000318
UP000000625
Genevestigator P05825
GO GO:0045203
GO:0042912
GO:0015620
GO:0005506
GO:0022834
GO:0004872
GO:0042914
GO:0015685
GO:0055072
GO:0055085
Gene3D 2.170.130.10
2.40.170.20
InterPro IPR012910
IPR000531
IPR010916
IPR010917
IPR010105
Pfam PF07715
PF00593
TIGRFAMs TIGR01783
PROSITE PS00430
PS01156

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

C

Table 1

complete

GO:0030313

cell envelope

PMID:23798405[2]

ECO:0000314

C

Figure 1A shows FepA localizing at the E. coli cell envelope via fluorescence microscopy.

complete
CACAO 11137

enables

GO:0019904

protein domain specific binding

PMID:15644214[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02929

F

Seeded From UniProt

complete

enables

GO:0042931

enterobactin transmembrane transporter activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001247782
UniProtKB:Q05098
UniProtKB:Q9I527

F

Seeded From UniProt

complete

involved_in

GO:0042930

enterobactin transport

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10293
PANTHER:PTN001247782
UniProtKB:Q05098
UniProtKB:Q9I527

P

Seeded From UniProt

complete

involved_in

GO:0033214

siderophore-dependent iron import into cell

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10293
PANTHER:PTN002824128

P

Seeded From UniProt

complete

part_of

GO:0031230

intrinsic component of cell outer membrane

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10293
PANTHER:PTN002824128
UniProtKB:P37409

C

Seeded From UniProt

complete

involved_in

GO:0015685

ferric-enterobactin import into cell

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10293
PANTHER:PTN001247782

P

Seeded From UniProt

complete

enables

GO:0015344

siderophore uptake transmembrane transporter activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002824128
UniProtKB:Q05098
UniProtKB:Q9I527

F

Seeded From UniProt

complete

part_of

GO:0045203

integral component of cell outer membrane

PMID:9886293[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0042914

colicin transport

PMID:9114029[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042914

colicin transport

PMID:2201687[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042914

colicin transport

PMID:139147[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042912

colicin transmembrane transporter activity

PMID:9114029[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042912

colicin transmembrane transporter activity

PMID:2201687[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042912

colicin transmembrane transporter activity

PMID:139147[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0033214

siderophore-dependent iron import into cell

PMID:2201687[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0022834

ligand-gated channel activity

PMID:1411544[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0015685

ferric-enterobactin import into cell

PMID:9114029[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0015685

ferric-enterobactin import into cell

PMID:2201687[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0015685

ferric-enterobactin import into cell

PMID:8471822[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0015620

ferric-enterobactin transmembrane transporter activity

PMID:9114029[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0015620

ferric-enterobactin transmembrane transporter activity

PMID:2201687[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0015620

ferric-enterobactin transmembrane transporter activity

PMID:8471822[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:6215063[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:22534293[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0044718

siderophore transmembrane transport

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0015344

P

Seeded From UniProt

complete

involved_in

GO:0055085

transmembrane transport

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0022834

P

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010105

F

Seeded From UniProt

complete

involved_in

GO:0015891

siderophore transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010105

P

Seeded From UniProt

complete

enables

GO:0038023

signaling receptor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010105

F

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0406

P

Seeded From UniProt

complete

involved_in

GO:0055072

iron ion homeostasis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0410

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0998
UniProtKB-SubCell:SL-0040

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
  2. ↑ Jordan, LD et al. (2013) Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane. Proc. Natl. Acad. Sci. U.S.A. 110 11553-8 PubMed GONUTS page
  3. ↑ Sean Peacock, R et al. (2005) The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. J. Mol. Biol. 345 1185-97 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. ↑ Buchanan, SK et al. (1999) Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 6 56-63 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 6.3 Newton, SM et al. (1997) Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA. Proc. Natl. Acad. Sci. U.S.A. 94 4560-5 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 7.3 7.4 Armstrong, SK et al. (1990) Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA. J. Biol. Chem. 265 14536-43 PubMed GONUTS page
  8. ↑ 8.0 8.1 Pugsley, AP & Reeves, P (1977) The role of colicin receptors in the uptake of ferrienterochelin by Escherichia coli K-12. Biochem. Biophys. Res. Commun. 74 903-11 PubMed GONUTS page
  9. ↑ Rutz, JM et al. (1992) Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 258 471-5 PubMed GONUTS page
  10. ↑ 10.0 10.1 Zhou, XH et al. (1993) Purification of outer membrane iron transport receptors from Escherichia coli by fast protein liquid chromatography: FepA and FecA. Biometals 6 25-35 PubMed GONUTS page
  11. ↑ Fiss, EH et al. (1982) Properties and proteolysis of ferric enterobactin outer membrane receptor in Escherichia coli K12. Biochemistry 21 4517-22 PubMed GONUTS page
  12. ↑ Han, MJ et al. (2012) Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains. J. Microbiol. Biotechnol. 22 470-8 PubMed GONUTS page
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