FETA_ECOLI
ID FETA_ECOLI Reviewed; 225 AA.
AC P77279; Q2MBT7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable iron export ATP-binding protein FetA;
DE EC=7.2.2.-;
GN Name=fetA; Synonyms=ybbL; OrderedLocusNames=b0490, JW0479;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24038693; DOI=10.1128/aem.02322-13;
RA Nicolaou S.A., Fast A.G., Nakamaru-Ogiso E., Papoutsakis E.T.;
RT "Overexpression of fetA (ybbL) and fetB (ybbM), encoding an iron exporter,
RT enhances resistance to oxidative stress in Escherichia coli.";
RL Appl. Environ. Microbiol. 79:7210-7219(2013).
CC -!- FUNCTION: Part of the ABC transporter complex FetAB, which is probably
CC involved in iron export and enhances resistance to H(2)O(2)-mediated
CC oxidative stress. Probably responsible for energy coupling to the
CC transport system. {ECO:0000269|PubMed:24038693}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FetA) and
CC two transmembrane proteins (FetB). {ECO:0000250}.
CC -!- INTERACTION:
CC P77279; P0A6F5: groEL; NbExp=3; IntAct=EBI-560090, EBI-543750;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits increased sensitivity to H(2)O(2)
CC stress. {ECO:0000269|PubMed:24038693}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U82664; AAB40244.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73592.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76269.1; -; Genomic_DNA.
DR PIR; A64780; A64780.
DR RefSeq; NP_415023.1; NC_000913.3.
DR RefSeq; WP_001157540.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P77279; -.
DR SMR; P77279; -.
DR BioGRID; 4259847; 151.
DR BioGRID; 851329; 2.
DR DIP; DIP-11320N; -.
DR IntAct; P77279; 6.
DR STRING; 511145.b0490; -.
DR TCDB; 3.A.1.139.2; the atp-binding cassette (abc) superfamily.
DR jPOST; P77279; -.
DR PaxDb; P77279; -.
DR PRIDE; P77279; -.
DR EnsemblBacteria; AAC73592; AAC73592; b0490.
DR EnsemblBacteria; BAE76269; BAE76269; BAE76269.
DR GeneID; 946990; -.
DR KEGG; ecj:JW0479; -.
DR KEGG; eco:b0490; -.
DR PATRIC; fig|511145.12.peg.511; -.
DR EchoBASE; EB3047; -.
DR eggNOG; COG4619; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P77279; -.
DR OMA; SSKIEHM; -.
DR PhylomeDB; P77279; -.
DR BioCyc; EcoCyc:YBBL-MON; -.
DR PRO; PR:P77279; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:EcoCyc.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
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 InterPro; IPR005670; Phosp_transpt1.
DR PANTHER; PTHR43423; PTHR43423; 1.
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..225
FT /note="Probable iron export ATP-binding protein FetA"
FT /id="PRO_0000093155"
FT DOMAIN 8..225
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"
SQ SEQUENCE 225 AA; 25382 MW; 0E2E07A5E0B7793D CRC64;
MQENSPLLQL QNVGYLAGDA KILNNINFSL RAGEFKLITG PSGCGKSTLL KIVASLISPT
SGTLLFEGED VSTLKPEIYR QQVSYCAQTP TLFGDTVYDN LIFPWQIRNR QPDPAIFLDF
LERFALPDSI LTKNIAELSG GEKQRISLIR NLQFMPKVLL LDEITSALDE SNKHNVNEMI
HRYVREQNIA VLWVTHDKDE INHADKVITL QPHAGEMQEA RYELA
