FEPB_ECOLI
ID FEPB_ECOLI Reviewed; 318 AA.
AC P0AEL6; P14609; Q2MBK9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ferric enterobactin-binding periplasmic protein FepB {ECO:0000305};
DE Flags: Precursor;
GN Name=fepB {ECO:0000303|PubMed:2529253}; OrderedLocusNames=b0592, JW0584;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=2529253; DOI=10.1128/jb.171.10.5443-5451.1989;
RA Elkins M.F., Earhart C.F.;
RT "Nucleotide sequence and regulation of the Escherichia coli gene for
RT ferrienterobactin transport protein FepB.";
RL J. Bacteriol. 171:5443-5451(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, AND INDUCTION.
RX PubMed=2139473; DOI=10.1016/0022-2836(90)90229-f;
RA Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Regulation of divergent transcription from the iron-responsive fepB-entC
RT promoter-operator regions in Escherichia coli.";
RL J. Mol. Biol. 212:669-682(1990).
RN [6]
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 [7]
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 [8]
RP FUNCTION, AND FERRIENTEROBACTIN-BINDING.
RC STRAIN=K12;
RX PubMed=7551033; DOI=10.1099/13500872-141-7-1647;
RA Stephens D.L., Choe M.D., Earhart C.F.;
RT "Escherichia coli periplasmic protein FepB binds ferrienterobactin.";
RL Microbiology 141:1647-1654(1995).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10986237; DOI=10.1128/jb.182.19.5359-5364.2000;
RA Sprencel C., Cao Z., Qi Z., Scott D.C., Montague M.A., Ivanoff N., Xu J.,
RA Raymond K.M., Newton S.M., Klebba P.E.;
RT "Binding of ferric enterobactin by the Escherichia coli periplasmic protein
RT FepB.";
RL J. Bacteriol. 182:5359-5364(2000).
RN [10]
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).
RN [11] {ECO:0007744|PDB:3TLK}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ENTEROBACTIN.
RA Li N., Gu L.;
RT "Crystal structure of holo FepB.";
RL Submitted (AUG-2011) to the PDB data bank.
RN [12] {ECO:0007744|PDB:2M6K, ECO:0007744|PDB:2M6L}
RP STRUCTURE BY NMR OF 27-318 OF APO- AND HOLO-PROTEIN, AND FUNCTION.
RX PubMed=25173704; DOI=10.1074/jbc.m114.564021;
RA Chu B.C., Otten R., Krewulak K.D., Mulder F.A., Vogel H.J.;
RT "The solution structure, binding properties, and dynamics of the bacterial
RT siderophore-binding protein FepB.";
RL J. Biol. Chem. 289:29219-29234(2014).
CC -!- FUNCTION: Part of the ABC transporter complex FepBDGC involved in
CC ferric enterobactin uptake (PubMed:3011753). Binds ferric enterobactin
CC (PubMed:7551033, PubMed:10986237, PubMed:25173704). Can also bind
CC ferric enantioenterobactin, the left-handed stereoisomer of the natural
CC E.coli siderophore, and the apo-siderophore, enterobactin, but does not
CC bind ferric agrobactin (PubMed:10986237). {ECO:0000269|PubMed:10986237,
CC ECO:0000269|PubMed:25173704, ECO:0000269|PubMed:3011753,
CC ECO:0000269|PubMed:7551033}.
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: Periplasm {ECO:0000269|PubMed:10986237,
CC ECO:0000269|PubMed:3011753, ECO:0000305|PubMed:2529253}.
CC -!- INDUCTION: Expression is regulated by iron, via the regulatory protein
CC Fur (PubMed:2529253, PubMed:2139473). Induced by hydroxyurea
CC (PubMed:20005847). {ECO:0000269|PubMed:20005847,
CC ECO:0000269|PubMed:2139473, ECO:0000269|PubMed:2529253}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; M29730; AAA83853.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40791.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73693.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76347.1; -; Genomic_DNA.
DR EMBL; X53274; CAA37370.1; -; Genomic_DNA.
DR PIR; JV0045; JV0045.
DR RefSeq; NP_415124.1; NC_000913.3.
DR RefSeq; WP_001234311.1; NZ_SSZK01000032.1.
DR PDB; 2M6K; NMR; -; A=27-318.
DR PDB; 2M6L; NMR; -; A=27-318.
DR PDB; 3TLK; X-ray; 1.85 A; A/B/C=1-318.
DR PDBsum; 2M6K; -.
DR PDBsum; 2M6L; -.
DR PDBsum; 3TLK; -.
DR AlphaFoldDB; P0AEL6; -.
DR BMRB; P0AEL6; -.
DR SMR; P0AEL6; -.
DR BioGRID; 4260980; 354.
DR ComplexPortal; CPX-4404; Ferric-enterobactin ABC transporter complex.
DR DIP; DIP-9593N; -.
DR IntAct; P0AEL6; 14.
DR STRING; 511145.b0592; -.
DR jPOST; P0AEL6; -.
DR PaxDb; P0AEL6; -.
DR PRIDE; P0AEL6; -.
DR EnsemblBacteria; AAC73693; AAC73693; b0592.
DR EnsemblBacteria; BAE76347; BAE76347; BAE76347.
DR GeneID; 947538; -.
DR KEGG; ecj:JW0584; -.
DR KEGG; eco:b0592; -.
DR PATRIC; fig|1411691.4.peg.1677; -.
DR EchoBASE; EB0290; -.
DR eggNOG; COG4592; Bacteria.
DR HOGENOM; CLU_038034_4_0_6; -.
DR InParanoid; P0AEL6; -.
DR OMA; DESFMFI; -.
DR PhylomeDB; P0AEL6; -.
DR BioCyc; EcoCyc:FEPB-MON; -.
DR BioCyc; MetaCyc:FEPB-MON; -.
DR PRO; PR:P0AEL6; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0015685; P:ferric-enterobactin import into cell; IMP:EcoCyc.
DR GO; GO:0033212; P:iron import into cell; IC:ComplexPortal.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Iron; Iron transport; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..318
FT /note="Ferric enterobactin-binding periplasmic protein
FT FepB"
FT /id="PRO_0000031821"
FT DOMAIN 48..318
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3TLK"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2M6K"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 166..186
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:3TLK"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2M6K"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2M6K"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3TLK"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3TLK"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:3TLK"
SQ SEQUENCE 318 AA; 34283 MW; 807676D03A508079 CRC64;
MRLAPLYRNA LLLTGLLLSG IAAVQAADWP RQITDSRGTH TLESQPQRIV STSVTLTGSL
LAIDAPVIAS GATTPNNRVA DDQGFLRQWS KVAKERKLQR LYIGEPSAEA VAAQMPDLIL
ISATGGDSAL ALYDQLSTIA PTLIINYDDK SWQSLLTQLG EITGHEKQAA ERIAQFDKQL
AAAKEQIKLP PQPVTAIVYT AAAHSANLWT PESAQGQMLE QLGFTLAKLP AGLNASQSQG
KRHDIIQLGG ENLAAGLNGE SLFLFAGDQK DADAIYANPL LAHLPAVQNK QVYALGTETF
RLDYYSAMQV LDRLKALF
