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FEPD_ECOLI
ID   FEPD_ECOLI              Reviewed;         334 AA.
AC   P23876; P77097; Q2MBL1;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Ferric enterobactin transport system permease protein FepD {ECO:0000305};
GN   Name=fepD; OrderedLocusNames=b0590, JW0582;
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 [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1787794; DOI=10.1111/j.1365-2958.1991.tb00787.x;
RA   Chenault S.S., Earhart C.F.;
RT   "Organization of genes encoding membrane proteins of the Escherichia coli
RT   ferrienterobactin permease.";
RL   Mol. Microbiol. 5:1405-1413(1991).
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   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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   TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [8]
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:1479347).
CC       Responsible for the translocation of the substrate across the membrane
CC       (Probable). {ECO:0000269|PubMed:1479347, ECO:0000269|PubMed:1838574,
CC       ECO:0000305}.
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:1479347,
CC       ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Controlled in part by the amount of available iron
CC       (PubMed:1838574). Induced by hydroxyurea (PubMed:20005847).
CC       {ECO:0000269|PubMed:1838574, ECO:0000269|PubMed:20005847}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. FecCD subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40789.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X57471; CAA40707.1; -; Genomic_DNA.
DR   EMBL; X59402; CAA42043.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40789.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73691.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76345.1; -; Genomic_DNA.
DR   PIR; S16296; S16296.
DR   RefSeq; NP_415122.1; NC_000913.3.
DR   RefSeq; WP_000016947.1; NZ_SSZK01000032.1.
DR   AlphaFoldDB; P23876; -.
DR   SMR; P23876; -.
DR   BioGRID; 4261558; 236.
DR   ComplexPortal; CPX-4404; Ferric-enterobactin ABC transporter complex.
DR   STRING; 511145.b0590; -.
DR   TCDB; 3.A.1.14.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P23876; -.
DR   PRIDE; P23876; -.
DR   EnsemblBacteria; AAC73691; AAC73691; b0590.
DR   EnsemblBacteria; BAE76345; BAE76345; BAE76345.
DR   GeneID; 945214; -.
DR   KEGG; ecj:JW0582; -.
DR   KEGG; eco:b0590; -.
DR   PATRIC; fig|1411691.4.peg.1679; -.
DR   EchoBASE; EB0292; -.
DR   eggNOG; COG0609; Bacteria.
DR   HOGENOM; CLU_013016_1_0_6; -.
DR   InParanoid; P23876; -.
DR   OMA; VFIWIVR; -.
DR   PhylomeDB; P23876; -.
DR   BioCyc; EcoCyc:FEPD-MON; -.
DR   BioCyc; MetaCyc:FEPD-MON; -.
DR   PRO; PR:P23876; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0015620; F:ferric-enterobactin transmembrane transporter activity; IMP:EcoCyc.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015685; P:ferric-enterobactin import into cell; IMP:EcoCyc.
DR   GO; GO:0033212; P:iron import into cell; IC:ComplexPortal.
DR   GO; GO:0033214; P:siderophore-dependent iron import into cell; IBA:GO_Central.
DR   Gene3D; 1.10.3470.10; -; 1.
DR   InterPro; IPR037294; ABC_BtuC-like.
DR   InterPro; IPR000522; ABC_transptr_permease_BtuC.
DR   PANTHER; PTHR30472; PTHR30472; 1.
DR   Pfam; PF01032; FecCD; 1.
DR   SUPFAM; SSF81345; SSF81345; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Ion transport; Iron; Iron transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..334
FT                   /note="Ferric enterobactin transport system permease
FT                   protein FepD"
FT                   /id="PRO_0000060022"
FT   TOPO_DOM        1..9
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..92
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..151
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..241
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..305
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996"
FT   CONFLICT        233..234
FT                   /note="RV -> AL (in Ref. 2; CAA42043)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  33871 MW;  BB5C5E939A96951B CRC64;
     MSGSVAVTRA IAVPGLLLLL IIATALSLLI GAKSLPASVV LEAFSGTCQS ADCTIVLDAR
     LPRTLAGLLA GGALGLAGAL MQTLTRNPLA DPGLLGVNAG ASFAIVLGAA LFGYSSAQEQ
     LAMAFAGALV ASLIVAFTGS QGGGQLSPVR LTLAGVALAA VLEGLTSGIA LLNPDVYDQL
     RFWQAGSLDI RNLHTLKVVL IPVLIAGATA LLLSRALNSL SLGSDTATAL GSRVARTQLI
     GLLAITVLCG SATAIVGPIA FIGLMMPHMA RWLVGADHRW SLPVTLLATP ALLLFADIIG
     RVIVPGELRV SVVSAFIGAP VLIFLVRRKT RGGA
 
 
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