FEPC_ECOLI
ID FEPC_ECOLI Reviewed; 271 AA.
AC P23878; P75724; P77096; Q2MBL3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ferric enterobactin transport ATP-binding protein FepC {ECO:0000305};
DE EC=7.2.2.17 {ECO:0000305|PubMed:1838574};
GN Name=fepC; OrderedLocusNames=b0588, JW0580;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1838574; DOI=10.1111/j.1365-2958.1991.tb00788.x;
RA Shea C.M., McIntosh M.A.;
RT "Nucleotide sequence and genetic organization of the ferric enterobactin
RT transport system: homology to other periplasmic binding protein-dependent
RT systems in Escherichia coli.";
RL Mol. Microbiol. 5:1415-1428(1991).
RN [2]
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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=3011753; DOI=10.1128/jb.166.3.930-936.1986;
RA Pierce J.R., Earhart C.F.;
RT "Escherichia coli K-12 envelope proteins specifically required for
RT ferrienterobactin uptake.";
RL J. Bacteriol. 166:930-936(1986).
RN [6]
RP SUBUNIT.
RX PubMed=1479347; DOI=10.1099/00221287-138-10-2167;
RA Chenault S.S., Earhart C.F.;
RT "Identification of hydrophobic proteins FepD and FepG of the Escherichia
RT coli ferrienterobactin permease.";
RL J. Gen. Microbiol. 138:2167-2171(1992).
RN [7]
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).
CC -!- FUNCTION: Part of the ABC transporter complex FepBDGC involved in
CC ferric enterobactin uptake (PubMed:1838574, PubMed:3011753).
CC Responsible for energy coupling to the transport system (Probable).
CC {ECO:0000269|PubMed:1838574, ECO:0000269|PubMed:3011753, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Fe(III)-enterobactin(out) + H2O = ADP + Fe(III)-
CC enterobactin(in) + H(+) + phosphate; Xref=Rhea:RHEA:58492,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.17; Evidence={ECO:0000305|PubMed:1838574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58493;
CC Evidence={ECO:0000305|PubMed:1838574};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FepC),
CC two transmembrane proteins (FepD and FepG) and a solute-binding protein
CC (FepB). {ECO:0000305|PubMed:1479347}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:3011753};
CC Peripheral membrane protein {ECO:0000269|PubMed:3011753}.
CC -!- INDUCTION: Controlled in part by the amount of available iron
CC (PubMed:1838574). Induced 1.5-fold by hydroxyurea (PubMed:20005847).
CC {ECO:0000269|PubMed:1838574, ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40787.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57471; CAA40709.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40787.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73689.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76343.1; -; Genomic_DNA.
DR PIR; B64792; B64792.
DR RefSeq; NP_415120.1; NC_000913.3.
DR RefSeq; WP_000140647.1; NZ_STEB01000047.1.
DR AlphaFoldDB; P23878; -.
DR SMR; P23878; -.
DR BioGRID; 4259899; 380.
DR BioGRID; 849587; 2.
DR ComplexPortal; CPX-4404; Ferric-enterobactin ABC transporter complex.
DR IntAct; P23878; 14.
DR STRING; 511145.b0588; -.
DR TCDB; 3.A.1.14.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P23878; -.
DR PRIDE; P23878; -.
DR EnsemblBacteria; AAC73689; AAC73689; b0588.
DR EnsemblBacteria; BAE76343; BAE76343; BAE76343.
DR GeneID; 66671137; -.
DR GeneID; 945201; -.
DR KEGG; ecj:JW0580; -.
DR KEGG; eco:b0588; -.
DR PATRIC; fig|1411691.4.peg.1681; -.
DR EchoBASE; EB0291; -.
DR eggNOG; COG1120; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR InParanoid; P23878; -.
DR OMA; FHIDAEI; -.
DR PhylomeDB; P23878; -.
DR BioCyc; EcoCyc:FEPC-MON; -.
DR BioCyc; MetaCyc:FEPC-MON; -.
DR PRO; PR:P23878; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015620; F:ferric-enterobactin transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015685; P:ferric-enterobactin import into cell; IMP:EcoCyc.
DR GO; GO:0033212; P:iron import into cell; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Iron;
KW Iron transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..271
FT /note="Ferric enterobactin transport ATP-binding protein
FT FepC"
FT /id="PRO_0000092325"
FT DOMAIN 8..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 227
FT /note="A -> R (in Ref. 1; CAA40709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29784 MW; B734924A31F06CE1 CRC64;
MTESVARLRG EQLTLGYGKY TVAENLTVEI PDGHFTAIIG PNGCGKSTLL RTLSRLMTPA
HGHVWLDGEH IQHYASKEVA RRIGLLAQNA TTPGDITVQE LVARGRYPHQ PLFTRWRKED
EEAVTKAMQA TGITHLADQS VDTLSGGQRQ RAWIAMVLAQ ETAIMLLDEP TTWLDISHQI
DLLELLSELN REKGYTLAAV LHDLNQACRY ASHLIALREG KIVAQGAPKE IVTAELIERI
YGLRCMIIDD PVAGTPLVVP LGRTAPSTAN S
