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Database: UniProt
Entry: P15031
LinkDB: P15031
Original site: P15031 
ID   FECE_ECOLI              Reviewed;         255 AA.
AC   P15031; Q2M628;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Fe(3+) dicitrate transport ATP-binding protein FecE {ECO:0000305};
DE            EC=7.2.2.18 {ECO:0000305|PubMed:1526456, ECO:0000305|PubMed:2651410};
DE   AltName: Full=Iron(III) dicitrate transport ATP-binding protein FecE;
GN   Name=fecE {ECO:0000303|PubMed:2651410}; OrderedLocusNames=b4287, JW4247;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=K12;
RX   PubMed=2651410; DOI=10.1128/jb.171.5.2626-2633.1989;
RA   Staudenmaier H., van Hove B., Yaraghi Z., Braun V.;
RT   "Nucleotide sequences of the fecBCDE genes and locations of the proteins
RT   suggest a periplasmic-binding-protein-dependent transport mechanism for
RT   iron(III) dicitrate in Escherichia coli.";
RL   J. Bacteriol. 171:2626-2633(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
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 ATP-BINDING.
RX   PubMed=1526456; DOI=10.1016/0378-1097(92)90434-p;
RA   Schultz-Hauser G., Van Hove B., Braun V.;
RT   "8-Azido-ATP labelling of the FecE protein of the Escherichia coli iron
RT   citrate transport system.";
RL   FEMS Microbiol. Lett. 74:231-234(1992).
RN   [6]
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 FecBCDE involved in
CC       citrate-dependent Fe(3+) uptake (PubMed:2651410). Binds ATP
CC       (PubMed:1526456). Probably responsible for energy coupling to the
CC       transport system (PubMed:1526456). {ECO:0000269|PubMed:1526456,
CC       ECO:0000269|PubMed:2651410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + iron(III) dicitrate(out) = ADP + H(+) + iron(III)
CC         dicitrate(in) + phosphate; Xref=Rhea:RHEA:58912, ChEBI:CHEBI:4991,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.18;
CC         Evidence={ECO:0000305|PubMed:1526456, ECO:0000305|PubMed:2651410};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FecE),
CC       two transmembrane proteins (FecC and FecD) and a solute-binding protein
CC       (FecB). {ECO:0000269|PubMed:2651410}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2651410};
CC       Peripheral membrane protein {ECO:0000305|PubMed:2651410}.
CC   -!- INDUCTION: Induced 1.6-fold by hydroxyurea.
CC       {ECO:0000269|PubMed:20005847}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; M26397; AAA23765.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97183.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77243.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78278.1; -; Genomic_DNA.
DR   PIR; JS0115; QRECM3.
DR   RefSeq; NP_418707.1; NC_000913.3.
DR   RefSeq; WP_000175457.1; NZ_STEB01000013.1.
DR   AlphaFoldDB; P15031; -.
DR   SMR; P15031; -.
DR   BioGRID; 4262739; 249.
DR   ComplexPortal; CPX-4403; Ferric-citrate ABC transporter complex.
DR   IntAct; P15031; 2.
DR   STRING; 511145.b4287; -.
DR   TCDB; 3.A.1.14.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; 511145-b4287; -.
DR   EnsemblBacteria; AAC77243; AAC77243; b4287.
DR   GeneID; 948819; -.
DR   KEGG; ecj:JW4247; -.
DR   KEGG; eco:b4287; -.
DR   PATRIC; fig|1411691.4.peg.2413; -.
DR   EchoBASE; EB0286; -.
DR   eggNOG; COG1120; Bacteria.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   InParanoid; P15031; -.
DR   OMA; DKIWLMD; -.
DR   OrthoDB; 5292475at2; -.
DR   PhylomeDB; P15031; -.
DR   BioCyc; EcoCyc:FECE-MONOMER; -.
DR   BioCyc; MetaCyc:FECE-MONOMER; -.
DR   PHI-base; PHI:11754; -.
DR   PHI-base; PHI:8010; -.
DR   PRO; PR:P15031; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; NAS:ComplexPortal.
DR   GO; GO:0033212; P:iron import into cell; NAS:ComplexPortal.
DR   GO; GO:0055085; P:transmembrane transport; IEA:GOC.
DR   CDD; cd03214; ABC_Iron-Siderophores_B12_Hemin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR42771:SF12; FE(3+) DICITRATE TRANSPORT ATP-BINDING PROTEIN FECE-RELATED; 1.
DR   PANTHER; PTHR42771; IRON(3+)-HYDROXAMATE IMPORT ATP-BINDING PROTEIN FHUC; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..255
FT                   /note="Fe(3+) dicitrate transport ATP-binding protein FecE"
FT                   /id="PRO_0000092324"
FT   DOMAIN          3..238
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   255 AA;  28191 MW;  89785C2A91D51FF3 CRC64;
     MTLRTENLTV SYGTDKVLND VSLSLPTGKI TALIGPNGCG KSTLLNCFSR LLMPQSGTVF
     LGDNPINMLS SRQLARRLSL LPQHHLTPEG ITVQELVSYG RNPWLSLWGR LSAEDNARVN
     VAMNQTRINH LAVRRLTELS GGQRQRAFLA MVLAQNTPVV LLDEPTTYLD INHQVDLMRL
     MGELRTQGKT VVAVLHDLNQ ASRYCDQLVV MANGHVMAQG TPEEVMTPGL LRTVFSVEAE
     IHPEPVSGRP MCLMR
//
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