FHUA_ECOLI
ID FHUA_ECOLI Reviewed; 747 AA.
AC P06971; P71280; P75665;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ferrichrome outer membrane transporter/phage receptor {ECO:0000305};
DE AltName: Full=Ferric hydroxamate receptor {ECO:0000305};
DE AltName: Full=Ferric hydroxamate uptake {ECO:0000305};
DE AltName: Full=Ferrichrome-iron receptor {ECO:0000303|PubMed:3079747};
DE Flags: Precursor;
GN Name=fhuA {ECO:0000303|PubMed:3079747};
GN Synonyms=tonA {ECO:0000303|PubMed:1089064};
GN OrderedLocusNames=b0150, JW0146;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-47.
RC STRAIN=K12;
RX PubMed=3079747; DOI=10.1128/jb.165.1.181-192.1986;
RA Coulton J.W., Mason P., Cameron D.R., Carmel G., Jean R., Rode H.N.;
RT "Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of
RT Escherichia coli K-12.";
RL J. Bacteriol. 165:181-192(1986).
RN [2]
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 [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], AND SEQUENCE REVISION TO
RP 609-610.
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 [LARGE SCALE GENOMIC DNA] OF 482-647.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-747.
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 [7]
RP FUNCTION.
RX PubMed=1089064; DOI=10.1016/0014-5793(75)80771-x;
RA Hantke K., Braun V.;
RT "Membrane receptor dependent iron transport in Escherichia coli.";
RL FEBS Lett. 49:301-305(1975).
RN [8]
RP FUNCTION.
RX PubMed=353030; DOI=10.1128/jb.135.1.190-197.1978;
RA Hantke K., Braun V.;
RT "Functional interaction of the tonA/tonB receptor system in Escherichia
RT coli.";
RL J. Bacteriol. 135:190-197(1978).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2066336; DOI=10.1128/jb.173.14.4394-4403.1991;
RA Carmel G., Coulton J.W.;
RT "Internal deletions in the FhuA receptor of Escherichia coli K-12 define
RT domains of ligand interactions.";
RL J. Bacteriol. 173:4394-4403(1991).
RN [10]
RP REVIEW.
RX PubMed=7515827; DOI=10.1016/0014-5793(94)00431-5;
RA Braun V., Killman H., Benz R.;
RT "Energy-coupled transport through the outer membrane of Escherichia coli
RT small deletions in the gating loop convert the FhuA transport protein into
RT a diffusion channel.";
RL FEBS Lett. 346:59-64(1994).
RN [11]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=8916906; DOI=10.1021/bi9608673;
RA Boulanger P., le Maire M., Bonhivers M., Dubois S., Desmadril M.,
RA Letellier L.;
RT "Purification and structural and functional characterization of FhuA, a
RT transporter of the Escherichia coli outer membrane.";
RL Biochemistry 35:14216-14224(1996).
RN [12]
RP FUNCTION AS A ION CHANNEL, AND DOMAIN.
RX PubMed=8617231; DOI=10.1002/j.1460-2075.1996.tb00535.x;
RA Bonhivers M., Ghazi A., Boulanger P., Letellier L.;
RT "FhuA, a transporter of the Escherichia coli outer membrane, is converted
RT into a channel upon binding of bacteriophage T5.";
RL EMBO J. 15:1850-1856(1996).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH TONB, AND DOMAIN.
RX PubMed=9353297; DOI=10.1074/jbc.272.45.28391;
RA Moeck G.S., Coulton J.W., Postle K.;
RT "Cell envelope signaling in Escherichia coli. Ligand binding to the
RT ferrichrome-iron receptor fhua promotes interaction with the energy-
RT transducing protein TonB.";
RL J. Biol. Chem. 272:28391-28397(1997).
RN [14]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH TONB.
RX PubMed=12427941; DOI=10.1099/00221287-148-11-3497;
RA Killmann H., Herrmann C., Torun A., Jung G., Braun V.;
RT "TonB of Escherichia coli activates FhuA through interaction with the beta-
RT barrel.";
RL Microbiology 148:3497-3509(2002).
RN [15]
RP INTERACTION WITH TONB, AND DOMAIN.
RX PubMed=18653801; DOI=10.1110/ps.036244.108;
RA James K.J., Hancock M.A., Moreau V., Molina F., Coulton J.W.;
RT "TonB induces conformational changes in surface-exposed loops of FhuA,
RT outer membrane receptor of Escherichia coli.";
RL Protein Sci. 17:1679-1688(2008).
RN [16]
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 [17] {ECO:0007744|PDB:1FCP, ECO:0007744|PDB:2FCP}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-747 IN COMPLEX WITH
RP FERRICHROME, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9856937; DOI=10.1126/science.282.5397.2215;
RA Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W.;
RT "Siderophore-mediated iron transport: crystal structure of FhuA with bound
RT lipopolysaccharide.";
RL Science 282:2215-2220(1998).
RN [18] {ECO:0007744|PDB:1BY3, ECO:0007744|PDB:1BY5}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 53-747 IN COMPLEX WITH
RP FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9865695; DOI=10.1016/s0092-8674(00)81700-6;
RA Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L.,
RA Rosenbusch J.P., Moras D.;
RT "Transmembrane signaling across the ligand-gated FhuA receptor: crystal
RT structures of free and ferrichrome-bound states reveal allosteric
RT changes.";
RL Cell 95:771-778(1998).
RN [19] {ECO:0007744|PDB:1QJQ, ECO:0007744|PDB:1QKC}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 34-747 IN COMPLEXES WITH
RP PHENYLFERRICROCIN AND ALBOMYCIN.
RX PubMed=10850805; DOI=10.1110/ps.9.5.956;
RA Ferguson A.D., Braun V., Fiedler H.-P., Coulton J.W., Diederichs K.,
RA Welte W.;
RT "Crystal structure of the antibiotic albomycin in complex with the outer
RT membrane transporter FhuA.";
RL Protein Sci. 9:956-963(2000).
CC -!- FUNCTION: Involved in the uptake of iron in complex with ferrichrome, a
CC hydroxamate-type siderophore. Binds and transports ferrichrome-iron
CC across the outer membrane (PubMed:1089064, PubMed:2066336). In addition
CC to its role in ferrichrome-iron transport, transports the antibiotic
CC albomycin, which is a structural analog of ferrichrome, and acts as a
CC receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80
CC and UC-1 (PubMed:1089064, PubMed:353030, PubMed:2066336,
CC PubMed:8617231). The energy source, which is required for all FhuA
CC functions except infection by phage T5, is provided by the inner
CC membrane TonB system (PubMed:353030, PubMed:9353297, PubMed:12427941).
CC {ECO:0000269|PubMed:1089064, ECO:0000269|PubMed:12427941,
CC ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:353030,
CC ECO:0000269|PubMed:8617231, ECO:0000269|PubMed:9353297}.
CC -!- ACTIVITY REGULATION: Binding of ferrichrome or colicin M enhances the
CC interaction between FhuA and TonB (PubMed:9353297). TonB activates FhuA
CC through interaction with the beta-barrel (PubMed:12427941).
CC {ECO:0000269|PubMed:12427941, ECO:0000269|PubMed:9353297}.
CC -!- SUBUNIT: Monomer (PubMed:8916906, PubMed:9856937, PubMed:9865695).
CC Interacts with TonB (PubMed:9353297, PubMed:12427941, PubMed:18653801).
CC {ECO:0000269|PubMed:12427941, ECO:0000269|PubMed:18653801,
CC ECO:0000269|PubMed:8916906, ECO:0000269|PubMed:9353297,
CC ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}.
CC -!- INTERACTION:
CC P06971; P02929: tonB; NbExp=4; IntAct=EBI-1116714, EBI-6399993;
CC P06971; Q9X2V7: mcjA; Xeno; NbExp=2; IntAct=EBI-1116714, EBI-16100378;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2066336,
CC ECO:0000269|PubMed:8916906, ECO:0000269|PubMed:9856937,
CC ECO:0000269|PubMed:9865695}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}.
CC -!- INDUCTION: Induced 1.6-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: Has two distinct conformations in the presence and absence of
CC ferrichrome. The globular N-terminal domain acts a plug that closes the
CC channel formed by the beta-barrel. Binding of ferrichrome at the cell
CC surface induces a conformational change in FhuA, but does not open the
CC channel. Structural changes are propagated and amplified across the
CC plug, and may facilitate binding of FhuA to TonB (PubMed:9865695,
CC PubMed:9353297). TonB binding promotes conformational changes in outer
CC surface-exposed loops of FhuA (PubMed:18653801). Phage T5 is a TonB-
CC independent ligand, and its binding to FhuA results in the formation of
CC high conductance ion channels (PubMed:8617231, PubMed:9353297).
CC {ECO:0000269|PubMed:18653801, ECO:0000269|PubMed:8617231,
CC ECO:0000269|PubMed:9353297, ECO:0000269|PubMed:9865695}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
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DR EMBL; M12486; AAB61768.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73261.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96726.2; -; Genomic_DNA.
DR EMBL; U70214; AAB08580.1; -; Genomic_DNA.
DR EMBL; X05810; CAA29253.1; -; Genomic_DNA.
DR PIR; F64738; QRECFE.
DR RefSeq; NP_414692.1; NC_000913.3.
DR RefSeq; WP_000124438.1; NZ_SSZK01000004.1.
DR PDB; 1BY3; X-ray; 2.74 A; A=34-747.
DR PDB; 1BY5; X-ray; 2.60 A; A=34-747.
DR PDB; 1FCP; X-ray; 2.70 A; A=52-747.
DR PDB; 1FI1; X-ray; 2.90 A; A=52-747.
DR PDB; 1QFF; X-ray; 2.70 A; A=34-747.
DR PDB; 1QFG; X-ray; 2.50 A; A=34-747.
DR PDB; 1QJQ; X-ray; 2.95 A; A=34-747.
DR PDB; 1QKC; X-ray; 3.10 A; A=34-747.
DR PDB; 2FCP; X-ray; 2.50 A; A=34-747.
DR PDB; 2GRX; X-ray; 3.30 A; A/B=34-747.
DR PDB; 4CU4; X-ray; 2.30 A; A=53-747.
DR PDBsum; 1BY3; -.
DR PDBsum; 1BY5; -.
DR PDBsum; 1FCP; -.
DR PDBsum; 1FI1; -.
DR PDBsum; 1QFF; -.
DR PDBsum; 1QFG; -.
DR PDBsum; 1QJQ; -.
DR PDBsum; 1QKC; -.
DR PDBsum; 2FCP; -.
DR PDBsum; 2GRX; -.
DR PDBsum; 4CU4; -.
DR AlphaFoldDB; P06971; -.
DR PCDDB; P06971; -.
DR SMR; P06971; -.
DR BioGRID; 4259745; 139.
DR ComplexPortal; CPX-2843; Ferrichrome outer membrane transporter complex.
DR DIP; DIP-9602N; -.
DR IntAct; P06971; 7.
DR STRING; 511145.b0150; -.
DR DrugBank; DB02767; (R)-3-hydroxytetradecanoic acid.
DR DrugBank; DB02907; 2-Amino-Vinyl-Phosphate.
DR DrugBank; DB01814; 2-Tridecanoyloxy-Pentadecanoic Acid.
DR DrugBank; DB03548; 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid.
DR DrugBank; DB02700; 3-Deoxy-D-Glucosamine.
DR DrugBank; DB04039; 3-Oxo-Pentadecanoic Acid.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02613; Capric dimethyl amine oxide.
DR DrugBank; DB04220; CGP 4832.
DR DrugBank; DB02724; Delta-2-Albomycin A1.
DR DrugBank; DB03574; Ferricrocin-iron.
DR DrugBank; DB03111; Glucosamine 1-Phosphate.
DR DrugBank; DB02865; Glucosamine 4-Phosphate.
DR DrugBank; DB04526; L-Glycero-D-Manno-Heptopyranose.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB02415; N-Octyl-2-Hydroxyethyl Sulfoxide.
DR DrugBank; DB02626; Phenylferricrocin-iron.
DR TCDB; 1.B.14.1.2; the outer membrane receptor (omr) family.
DR CarbonylDB; P06971; -.
DR PaxDb; P06971; -.
DR PRIDE; P06971; -.
DR EnsemblBacteria; AAC73261; AAC73261; b0150.
DR EnsemblBacteria; BAB96726; BAB96726; BAB96726.
DR GeneID; 66671561; -.
DR GeneID; 944856; -.
DR KEGG; ecj:JW0146; -.
DR KEGG; eco:b0150; -.
DR PATRIC; fig|1411691.4.peg.2130; -.
DR EchoBASE; EB0298; -.
DR eggNOG; COG4774; Bacteria.
DR HOGENOM; CLU_008287_9_0_6; -.
DR InParanoid; P06971; -.
DR OMA; FSWRPDD; -.
DR PhylomeDB; P06971; -.
DR BioCyc; EcoCyc:EG10302-MON; -.
DR BioCyc; MetaCyc:EG10302-MON; -.
DR BRENDA; 7.2.2.16; 2026.
DR EvolutionaryTrace; P06971; -.
DR PRO; PR:P06971; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0005506; F:iron ion binding; IPI:EcoliWiki.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; IMP:EcoliWiki.
DR GO; GO:0046790; F:virion binding; IMP:EcoliWiki.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR039423; TonB-dep_rcpt.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR InterPro; IPR010105; TonB_sidphr_rcpt.
DR PANTHER; PTHR32552; PTHR32552; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01783; TonB-siderophor; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Disulfide bond; Ion transport; Iron; Iron transport; Membrane; Receptor;
KW Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:3079747"
FT CHAIN 34..747
FT /note="Ferrichrome outer membrane transporter/phage
FT receptor"
FT /id="PRO_0000034748"
FT TOPO_DOM 34..192
FT /note="Periplasmic"
FT TRANSMEM 193..201
FT /note="Beta stranded"
FT TOPO_DOM 202..206
FT /note="Extracellular"
FT TRANSMEM 207..215
FT /note="Beta stranded"
FT TOPO_DOM 216..222
FT /note="Periplasmic"
FT TRANSMEM 223..231
FT /note="Beta stranded"
FT TOPO_DOM 232..245
FT /note="Extracellular"
FT TRANSMEM 246..255
FT /note="Beta stranded"
FT TOPO_DOM 256..259
FT /note="Periplasmic"
FT TRANSMEM 260..268
FT /note="Beta stranded"
FT TOPO_DOM 269..312
FT /note="Extracellular"
FT TRANSMEM 313..321
FT /note="Beta stranded"
FT TOPO_DOM 322..326
FT /note="Periplasmic"
FT TRANSMEM 327..335
FT /note="Beta stranded"
FT TOPO_DOM 336..387
FT /note="Extracellular"
FT TRANSMEM 388..396
FT /note="Beta stranded"
FT TOPO_DOM 397..404
FT /note="Periplasmic"
FT TRANSMEM 405..413
FT /note="Beta stranded"
FT TOPO_DOM 414..464
FT /note="Extracellular"
FT TRANSMEM 465..473
FT /note="Beta stranded"
FT TOPO_DOM 474..477
FT /note="Periplasmic"
FT TRANSMEM 478..486
FT /note="Beta stranded"
FT TOPO_DOM 487..508
FT /note="Extracellular"
FT TRANSMEM 509..517
FT /note="Beta stranded"
FT TOPO_DOM 518..522
FT /note="Periplasmic"
FT TRANSMEM 523..531
FT /note="Beta stranded"
FT TOPO_DOM 532..551
FT /note="Extracellular"
FT TRANSMEM 552..560
FT /note="Beta stranded"
FT TOPO_DOM 561..565
FT /note="Periplasmic"
FT TRANSMEM 566..574
FT /note="Beta stranded"
FT TOPO_DOM 575..601
FT /note="Extracellular"
FT TRANSMEM 602..610
FT /note="Beta stranded"
FT TOPO_DOM 611..613
FT /note="Periplasmic"
FT TRANSMEM 614..622
FT /note="Beta stranded"
FT TOPO_DOM 623..645
FT /note="Extracellular"
FT TRANSMEM 646..654
FT /note="Beta stranded"
FT TOPO_DOM 655..661
FT /note="Periplasmic"
FT TRANSMEM 662..670
FT /note="Beta stranded"
FT TOPO_DOM 671..689
FT /note="Extracellular"
FT TRANSMEM 690..698
FT /note="Beta stranded"
FT TOPO_DOM 699..705
FT /note="Periplasmic"
FT TRANSMEM 706..714
FT /note="Beta stranded"
FT TOPO_DOM 715..737
FT /note="Extracellular"
FT TRANSMEM 738..746
FT /note="Beta stranded"
FT TOPO_DOM 747
FT /note="Periplasmic"
FT MOTIF 40..47
FT /note="TonB box"
FT MOTIF 730..747
FT /note="TonB C-terminal box"
FT BINDING 114
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:10850805,
FT ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695"
FT BINDING 133
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:10850805,
FT ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695"
FT BINDING 148..149
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:10850805,
FT ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695"
FT BINDING 277..279
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:10850805,
FT ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695"
FT BINDING 346..348
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:10850805,
FT ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695"
FT BINDING 424
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:9856937"
FT BINDING 735
FT /ligand="ferrichrome"
FT /ligand_id="ChEBI:CHEBI:5019"
FT /evidence="ECO:0000305|PubMed:9856937"
FT DISULFID 351..362
FT DISULFID 725..731
FT CONFLICT 737
FT /note="R -> P (in Ref. 6; CAA29253)"
FT /evidence="ECO:0000305"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2GRX"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1BY5"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2GRX"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 206..235
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2GRX"
FT STRAND 242..257
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 260..272
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 307..322
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 324..350
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 373..400
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 403..434
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1QFG"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:2FCP"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 453..475
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 478..495
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 500..517
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 522..534
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 549..560
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 565..584
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1BY3"
FT STRAND 590..610
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 612..630
FT /evidence="ECO:0007829|PDB:4CU4"
FT TURN 632..636
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 644..655
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:1QJQ"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 663..672
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 688..698
FT /evidence="ECO:0007829|PDB:4CU4"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 708..715
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 722..727
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 730..733
FT /evidence="ECO:0007829|PDB:4CU4"
FT STRAND 738..746
FT /evidence="ECO:0007829|PDB:4CU4"
SQ SEQUENCE 747 AA; 82182 MW; 1C2B251D1990E444 CRC64;
MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP QESAWGPAAT
IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK EALSYTPGVS VGTRGASNTY
DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG
LLNMVSKRPT TEPLKEVQFK AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG
SEEQRYAIAP AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN
EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV CSDPANAYSK
QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT GDIDHTLLTG VDFMRMRNDI
NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV
TLGGRYDWAD QESLNRVAGT TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG
KDGNIFAPSK GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA
RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW ADYTFFDGPL
SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA RVGMAGSNVA LHVNNLFDRE
YVASCFNTYG CFWGAERQVV ATATFRF
