FHUD_ECOLI
ID FHUD_ECOLI Reviewed; 296 AA.
AC P07822; P77711;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Iron(3+)-hydroxamate-binding protein FhuD {ECO:0000305};
DE AltName: Full=Ferric hydroxamate uptake protein D {ECO:0000305};
DE AltName: Full=Ferrichrome-binding periplasmic protein {ECO:0000305};
DE AltName: Full=Iron(III)-hydroxamate-binding protein FhuD {ECO:0000305};
DE Flags: Precursor;
GN Name=fhuD; OrderedLocusNames=b0152, JW0148;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3301821; DOI=10.1128/jb.169.8.3844-3849.1987;
RA Coulton J.W., Mason P., Allatt D.D.;
RT "fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia
RT coli K-12.";
RL J. Bacteriol. 169:3844-3849(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2823072; DOI=10.1007/bf00329835;
RA Burkhardt R., Braun V.;
RT "Nucleotide sequence of the fhuC and fhuD genes involved in iron (III)
RT hydroxamate transport: domains in FhuC homologous to ATP-binding
RT proteins.";
RL Mol. Gen. Genet. 209:49-55(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 154.
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 [7]
RP PROTEIN SEQUENCE OF 32-39.
RX PubMed=7651325; DOI=10.1007/bf02456611;
RA Rohrback M.R., Paul S., Koster W.;
RT "In vivo reconstitution of an active siderophore transport system by a
RT binding protein derivative lacking a signal sequence.";
RL Mol. Gen. Genet. 248:33-42(1995).
RN [8]
RP FUNCTION.
RX PubMed=2254301; DOI=10.1016/s0021-9258(18)45749-3;
RA Koester W., Braun V.;
RT "Iron (III) hydroxamate transport into Escherichia coli. Substrate binding
RT to the periplasmic FhuD protein.";
RL J. Biol. Chem. 265:21407-21410(1990).
RN [9]
RP FUNCTION, INTERACTION WITH FHUB, AND MUTAGENESIS OF TRP-68.
RX PubMed=8522527; DOI=10.1128/jb.177.24.7186-7193.1995;
RA Rohrbach M.R., Braun V., Koester W.;
RT "Ferrichrome transport in Escherichia coli K-12: altered substrate
RT specificity of mutated periplasmic FhuD and interaction of FhuD with the
RT integral membrane protein FhuB.";
RL J. Bacteriol. 177:7186-7193(1995).
RN [10]
RP INTERACTION WITH FHUB.
RX PubMed=9426146; DOI=10.1046/j.1365-2958.1997.6592008.x;
RA Mademidis A., Killmann H., Kraas W., Flechsler I., Jung G., Braun V.;
RT "ATP-dependent ferric hydroxamate transport system in Escherichia coli:
RT periplasmic FhuD interacts with a periplasmic and with a
RT transmembrane/cytoplasmic region of the integral membrane protein FhuB, as
RT revealed by competitive peptide mapping.";
RL Mol. Microbiol. 26:1109-1123(1997).
RN [11]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM, AND SUBCELLULAR LOCATION.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-296 IN COMPLEX WITH
RP GALLICHROME, AND FUNCTION.
RX PubMed=10742172; DOI=10.1038/74048;
RA Clarke T.E., Ku S.-Y., Dougan D.R., Vogel H.J., Tari L.W.;
RT "The structure of the ferric siderophore binding protein FhuD complexed
RT with gallichrome.";
RL Nat. Struct. Biol. 7:287-291(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-296 IN COMPLEX WITH COPROGEN;
RP DESFERRIOXAMINE AND ALBOMYCIN, AND FUNCTION.
RX PubMed=11805094; DOI=10.1074/jbc.m109385200;
RA Clarke T.E., Braun V., Winkelmann G., Tari L.W., Vogel H.J.;
RT "X-ray crystallographic structures of the Escherichia coli periplasmic
RT protein FhuD bound to hydroxamate-type siderophores and the antibiotic
RT albomycin.";
RL J. Biol. Chem. 277:13966-13972(2002).
CC -!- FUNCTION: Part of the ABC transporter complex FhuCDB involved in
CC iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and
CC transfers it to the membrane-bound permease. Required for the transport
CC of all iron(3+)-hydroxamate siderophores such as ferrichrome,
CC gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen,
CC rhodotorulic acid and the antibiotic albomycin.
CC {ECO:0000269|PubMed:10742172, ECO:0000269|PubMed:11805094,
CC ECO:0000269|PubMed:2254301, ECO:0000269|PubMed:8522527}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FhuC),
CC two transmembrane proteins (FhuB) and a solute-binding protein (FhuD)
CC (Probable). FhuD interacts with FhuB (PubMed:8522527, PubMed:9426146).
CC {ECO:0000269|PubMed:8522527, ECO:0000269|PubMed:9426146, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17218314}.
CC -!- INDUCTION: Induced 1.3-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has been experimentally proven. Can also be exported by the
CC Sec system. {ECO:0000269|PubMed:17218314}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; X05810; CAA29255.1; -; Genomic_DNA.
DR EMBL; M12486; AAB61770.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08582.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73263.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96728.2; -; Genomic_DNA.
DR PIR; H64738; QRECFD.
DR RefSeq; NP_414694.1; NC_000913.3.
DR RefSeq; WP_001310529.1; NZ_SSZK01000004.1.
DR PDB; 1EFD; X-ray; 1.90 A; N=31-296.
DR PDB; 1ESZ; X-ray; 2.00 A; A=31-296.
DR PDB; 1K2V; X-ray; 1.97 A; N=31-296.
DR PDB; 1K7S; X-ray; 2.60 A; N=33-296.
DR PDB; 7LB8; EM; 3.40 A; D=1-296.
DR PDBsum; 1EFD; -.
DR PDBsum; 1ESZ; -.
DR PDBsum; 1K2V; -.
DR PDBsum; 1K7S; -.
DR PDBsum; 7LB8; -.
DR AlphaFoldDB; P07822; -.
DR SMR; P07822; -.
DR BioGRID; 4263041; 342.
DR ComplexPortal; CPX-4286; Ferric-hydroxamate ABC transporter complex.
DR IntAct; P07822; 2.
DR STRING; 511145.b0152; -.
DR DrugBank; DB01747; Coprogen.
DR DrugBank; DB02724; Delta-2-Albomycin A1.
DR DrugBank; DB13949; Ferric cation.
DR DrugBank; DB03436; Gallichrome.
DR DrugBank; DB14520; Tetraferric tricitrate decahydrate.
DR TCDB; 3.A.1.14.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; P07822; -.
DR PRIDE; P07822; -.
DR EnsemblBacteria; AAC73263; AAC73263; b0152.
DR EnsemblBacteria; BAB96728; BAB96728; BAB96728.
DR GeneID; 947510; -.
DR KEGG; ecj:JW0148; -.
DR KEGG; eco:b0152; -.
DR PATRIC; fig|1411691.4.peg.2128; -.
DR EchoBASE; EB0301; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_10_0_6; -.
DR InParanoid; P07822; -.
DR OMA; GIWMFGG; -.
DR PhylomeDB; P07822; -.
DR BioCyc; EcoCyc:FHUD-MON; -.
DR BioCyc; MetaCyc:FHUD-MON; -.
DR EvolutionaryTrace; P07822; -.
DR PRO; PR:P07822; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0098711; P:iron ion import across plasma membrane; 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; Direct protein sequencing; Ion transport; Iron;
KW Iron transport; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..30
FT /note="Tat-type signal"
FT CHAIN 31..296
FT /note="Iron(3+)-hydroxamate-binding protein FhuD"
FT /id="PRO_0000031824"
FT DOMAIN 37..296
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT MUTAGEN 68
FT /note="W->L: Decreases binding of coprogen. Does not bind
FT aerobactin and ferrichrome. Increases resistance to
FT albomycin."
FT /evidence="ECO:0000269|PubMed:8522527"
FT CONFLICT 48
FT /note="L -> V (in Ref. 1; CAA29255)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="H -> D (in Ref. 1; AAB61770)"
FT /evidence="ECO:0000305"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1K2V"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1EFD"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1EFD"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:1EFD"
SQ SEQUENCE 296 AA; 32998 MW; 4687A34771397D9F CRC64;
MSGLPLISRR RLLTAMALSP LLWQMNTAHA AAIDPNRIVA LEWLPVELLL ALGIVPYGVA
DTINYRLWVS EPPLPDSVID VGLRTEPNLE LLTEMKPSFM VWSAGYGPSP EMLARIAPGR
GFNFSDGKQP LAMARKSLTE MADLLNLQSA AETHLAQYED FIRSMKPRFV KRGARPLLLT
TLIDPRHMLV FGPNSLFQEI LDEYGIPNAW QGETNFWGST AVSIDRLAAY KDVDVLCFDH
DNSKDMDALM ATPLWQAMPF VRAGRFQRVP AVWFYGATLS AMHFVRVLDN AIGGKA
