FEPG_ECOLI
ID FEPG_ECOLI Reviewed; 330 AA.
AC P23877; P77587; Q2MBL2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ferric enterobactin transport system permease protein FepG {ECO:0000305};
GN Name=fepG; OrderedLocusNames=b0589, JW0581;
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, 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 [6]
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 [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: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 1.4-fold 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}.
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DR EMBL; X57471; CAA40708.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40788.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73690.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76344.1; -; Genomic_DNA.
DR PIR; C64792; C64792.
DR RefSeq; NP_415121.1; NC_000913.3.
DR RefSeq; WP_000640988.1; NZ_SSZK01000032.1.
DR AlphaFoldDB; P23877; -.
DR SMR; P23877; -.
DR BioGRID; 4261377; 423.
DR ComplexPortal; CPX-4404; Ferric-enterobactin ABC transporter complex.
DR DIP; DIP-9597N; -.
DR IntAct; P23877; 1.
DR STRING; 511145.b0589; -.
DR TCDB; 3.A.1.14.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P23877; -.
DR PRIDE; P23877; -.
DR EnsemblBacteria; AAC73690; AAC73690; b0589.
DR EnsemblBacteria; BAE76344; BAE76344; BAE76344.
DR GeneID; 945209; -.
DR KEGG; ecj:JW0581; -.
DR KEGG; eco:b0589; -.
DR PATRIC; fig|1411691.4.peg.1680; -.
DR EchoBASE; EB0294; -.
DR eggNOG; COG4779; Bacteria.
DR HOGENOM; CLU_013016_1_1_6; -.
DR InParanoid; P23877; -.
DR OMA; AWKRGVH; -.
DR PhylomeDB; P23877; -.
DR BioCyc; EcoCyc:FEPG-MON; -.
DR BioCyc; MetaCyc:FEPG-MON; -.
DR PRO; PR:P23877; -.
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..330
FT /note="Ferric enterobactin transport system permease
FT protein FepG"
FT /id="PRO_0000060023"
FT TOPO_DOM 1..7
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..92
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..146
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..235
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..303
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 230..231
FT /note="SV -> RL (in Ref. 1; CAA40708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 34910 MW; A67FA9513733D3CB CRC64;
MIYVSRRLLI TCLLLVSACV VAGIWGLRSG AVTLETSQVF AALMGDAPRS MTMVVTEWRL
PRVLMALLIG AALGVSGAIF QSLMRNPLGS PDVMGFNTGA WSGVLVAMVL FGQDLTAIAL
SAMVGGIVTS LLVWLLAWRN GIDTFRLIII GIGVRAMLVA FNTWLLLKAS LETALTAGLW
NAGSLNGLTW AKTSPSAPII ILMLIAAALL VRRMRLLEMG DDTACALGVS VERSRLLMML
VAVVLTAAAT ALAGPISFIA LVAPHIARRI SGTARWGLTQ AALCGALLLL AADLCAQQLF
MPYQLPVGVV TVSLGGIYLI VLLIQESRKK
