FEPA_ECOLI
ID FEPA_ECOLI Reviewed; 746 AA.
AC P05825; P75722; P76821; P77093;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Ferrienterobactin receptor;
DE AltName: Full=Enterobactin outer-membrane receptor;
DE Flags: Precursor;
GN Name=fepA; Synonyms=fep, feuB; OrderedLocusNames=b0584, JW5086;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015941; DOI=10.1016/s0021-9258(18)67457-5;
RA Lundrigan M.D., Kadner R.J.;
RT "Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in
RT Escherichia coli. Homology among outer membrane receptors that interact
RT with TonB.";
RL J. Biol. Chem. 261:10797-10801(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=2974033; DOI=10.1016/s0021-9258(18)37361-7;
RA Pettis G.S., Brickman T.J., McIntosh M.A.;
RT "Transcriptional mapping and nucleotide sequence of the Escherichia coli
RT fepA-fes enterobactin region. Identification of a unique iron-regulated
RT bidirectional promoter.";
RL J. Biol. Chem. 263:18857-18863(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-746.
RX PubMed=2526281; DOI=10.1111/j.1365-2958.1989.tb00224.x;
RA Armstrong S.K., Pettis G.S., Forrester L.J., McIntosh M.A.;
RT "The Escherichia coli enterobactin biosynthesis gene, entD: nucleotide
RT sequence and membrane localization of its protein product.";
RL Mol. Microbiol. 3:757-766(1989).
RN [8]
RP MOLECULAR ANALYSIS.
RX PubMed=2201687; DOI=10.1016/s0021-9258(18)77336-5;
RA Armstrong S.K., Francis C.L., McIntosh M.A.;
RT "Molecular analysis of the Escherichia coli ferric enterobactin receptor
RT FepA.";
RL J. Biol. Chem. 265:14536-14543(1990).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9886293; DOI=10.1038/4931;
RA Buchanan S.K., Smith B.S., Venkatramani L., Xia D., Esser L., Palnitkar M.,
RA Chakraborty R., van der Helm D., Deisenhofer J.;
RT "Crystal structure of the outer membrane active transporter FepA from
RT Escherichia coli.";
RL Nat. Struct. Biol. 6:56-63(1999).
CC -!- FUNCTION: This protein is involved in the initial step of iron uptake
CC by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore
CC that allows E.coli to extract iron from the environment. FepA also acts
CC as a receptor for colicins B and D.
CC -!- INTERACTION:
CC P05825; P02929: tonB; NbExp=2; IntAct=EBI-6400027, EBI-6399993;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced 1.9-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40783.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M13748; AAA65994.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40783.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73685.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35225.1; -; Genomic_DNA.
DR EMBL; J04216; AAA23756.1; -; Genomic_DNA.
DR PIR; F64791; QRECFC.
DR RefSeq; NP_415116.1; NC_000913.3.
DR RefSeq; WP_001034943.1; NZ_LN832404.1.
DR PDB; 1FEP; X-ray; 2.40 A; A=23-746.
DR PDBsum; 1FEP; -.
DR AlphaFoldDB; P05825; -.
DR PCDDB; P05825; -.
DR SMR; P05825; -.
DR BioGRID; 4263074; 241.
DR ComplexPortal; CPX-3578; Ferric-enterobactin outer membrane transporter complex.
DR DIP; DIP-9592N; -.
DR IntAct; P05825; 1.
DR STRING; 511145.b0584; -.
DR TCDB; 1.B.14.1.22; the outer membrane receptor (omr) family.
DR SWISS-2DPAGE; P05825; -.
DR jPOST; P05825; -.
DR PaxDb; P05825; -.
DR PRIDE; P05825; -.
DR EnsemblBacteria; AAC73685; AAC73685; b0584.
DR EnsemblBacteria; BAA35225; BAA35225; BAA35225.
DR GeneID; 945193; -.
DR KEGG; ecj:JW5086; -.
DR KEGG; eco:b0584; -.
DR PATRIC; fig|1411691.4.peg.1688; -.
DR EchoBASE; EB0289; -.
DR eggNOG; COG4771; Bacteria.
DR HOGENOM; CLU_008287_18_2_6; -.
DR InParanoid; P05825; -.
DR OMA; NESGRTW; -.
DR PhylomeDB; P05825; -.
DR BioCyc; EcoCyc:EG10293-MON; -.
DR BioCyc; MetaCyc:EG10293-MON; -.
DR EvolutionaryTrace; P05825; -.
DR PRO; PR:P05825; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030313; C:cell envelope; IDA:CACAO.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0042912; F:colicin transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042931; F:enterobactin transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015620; F:ferric-enterobactin transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0022834; F:ligand-gated channel activity; IMP:EcoCyc.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0042914; P:colicin transport; IDA:EcoCyc.
DR GO; GO:0042930; P:enterobactin transport; IBA:GO_Central.
DR GO; GO:0015685; P:ferric-enterobactin import into cell; IDA:EcoCyc.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GO_Central.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:EcoCyc.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR039426; BtuB-like.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR InterPro; IPR010105; TonB_sidphr_rcpt.
DR PANTHER; PTHR30069; PTHR30069; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01783; TonB-siderophor; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Iron; Iron transport;
KW Membrane; Receptor; Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT CHAIN 23..746
FT /note="Ferrienterobactin receptor"
FT /id="PRO_0000034747"
FT REGION 76..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..41
FT /note="TonB box"
FT MOTIF 729..746
FT /note="TonB C-terminal box"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 152
FT /note="A -> R (in Ref. 1; AAA65994)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Missing (in Ref. 1; AAA65994)"
FT /evidence="ECO:0000305"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1FEP"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 176..188
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 206..220
FT /evidence="ECO:0007829|PDB:1FEP"
FT TURN 225..231
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 249..264
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 267..281
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 304..318
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 324..338
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 360..397
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 426..441
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 443..457
FT /evidence="ECO:0007829|PDB:1FEP"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 461..473
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 478..489
FT /evidence="ECO:0007829|PDB:1FEP"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 527..540
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 543..560
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 573..597
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 600..614
FT /evidence="ECO:0007829|PDB:1FEP"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 626..638
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 641..650
FT /evidence="ECO:0007829|PDB:1FEP"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 676..686
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 688..699
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 719..723
FT /evidence="ECO:0007829|PDB:1FEP"
FT STRAND 737..746
FT /evidence="ECO:0007829|PDB:1FEP"
SQ SEQUENCE 746 AA; 82107 MW; 09348AAB1C29710A CRC64;
MNKKIHSLAL LVNLGIYGVA QAQEPTDTPV SHDDTIVVTA AEQNLQAPGV STITADEIRK
NPVARDVSKI IRTMPGVNLT GNSTSGQRGN NRQIDIRGMG PENTLILIDG KPVSSRNSVR
QGWRGERDTR GDTSWVPPEM IERIEVLRGP AAARYGNGAA GGVVNIITKK GSGEWHGSWD
AYFNAPEHKE EGATKRTNFS LTGPLGDEFS FRLYGNLDKT QADAWDINQG HQSARAGTYA
TTLPAGREGV INKDINGVVR WDFAPLQSLE LEAGYSRQGN LYAGDTQNTN SDSYTRSKYG
DETNRLYRQN YALTWNGGWD NGVTTSNWVQ YEHTRNSRIP EGLAGGTEGK FNEKATQDFV
DIDLDDVMLH SEVNLPIDFL VNQTLTLGTE WNQQRMKDLS SNTQALTGTN TGGAIDGVST
TDRSPYSKAE IFSLFAENNM ELTDSTIVTP GLRFDHHSIV GNNWSPALNI SQGLGDDFTL
KMGIARAYKA PSLYQTNPNY ILYSKGQGCY ASAGGCYLQG NDDLKAETSI NKEIGLEFKR
DGWLAGVTWF RNDYRNKIEA GYVAVGQNAV GTDLYQWDNV PKAVVEGLEG SLNVPVSETV
MWTNNITYML KSENKTTGDR LSIIPEYTLN STLSWQARED LSMQTTFTWY GKQQPKKYNY
KGQPAVGPET KEISPYSIVG LSATWDVTKN VSLTGGVDNL FDKRLWRAGN AQTTGDLAGA
NYIAGAGAYT YNEPGRTWYM SVNTHF
