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Ferrichrome outer membrane transporter/phage receptor (Ferric hydroxamate receptor) (Ferric hydroxamate uptake) (Ferrichrome-iron receptor)

 FHUA_ECOLI              Reviewed;         747 AA.
P06971; P71280; P75665;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
10-OCT-2018, entry version 189.
RecName: Full=Ferrichrome outer membrane transporter/phage receptor {ECO:0000305};
AltName: Full=Ferric hydroxamate receptor {ECO:0000305};
AltName: Full=Ferric hydroxamate uptake {ECO:0000305};
AltName: Full=Ferrichrome-iron receptor {ECO:0000303|PubMed:3079747};
Flags: Precursor;
Name=fhuA {ECO:0000303|PubMed:3079747};
Synonyms=tonA {ECO:0000303|PubMed:1089064};
OrderedLocusNames=b0150, JW0146;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-47.
STRAIN=K12;
PubMed=3079747; DOI=10.1128/jb.165.1.181-192.1986;
Coulton J.W., Mason P., Cameron D.R., Carmel G., Jean R., Rode H.N.;
"Protein fusions of beta-galactosidase to the ferrichrome-iron
receptor of Escherichia coli K-12.";
J. Bacteriol. 165:181-192(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
TO 609-610.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 482-647.
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-747.
PubMed=2823072; DOI=10.1007/BF00329835;
Burkhardt R., Braun V.;
"Nucleotide sequence of the fhuC and fhuD genes involved in iron (III)
hydroxamate transport: domains in FhuC homologous to ATP-binding
proteins.";
Mol. Gen. Genet. 209:49-55(1987).
[7]
FUNCTION.
PubMed=1089064;
Hantke K., Braun V.;
"Membrane receptor dependent iron transport in Escherichia coli.";
FEBS Lett. 49:301-305(1975).
[8]
FUNCTION.
PubMed=353030;
Hantke K., Braun V.;
"Functional interaction of the tonA/tonB receptor system in
Escherichia coli.";
J. Bacteriol. 135:190-197(1978).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=2066336;
Carmel G., Coulton J.W.;
"Internal deletions in the FhuA receptor of Escherichia coli K-12
define domains of ligand interactions.";
J. Bacteriol. 173:4394-4403(1991).
[10]
REVIEW.
PubMed=7515827; DOI=10.1016/0014-5793(94)00431-5;
Braun V., Killman H., Benz R.;
"Energy-coupled transport through the outer membrane of Escherichia
coli small deletions in the gating loop convert the FhuA transport
protein into a diffusion channel.";
FEBS Lett. 346:59-64(1994).
[11]
SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=K12;
PubMed=8916906; DOI=10.1021/bi9608673;
Boulanger P., le Maire M., Bonhivers M., Dubois S., Desmadril M.,
Letellier L.;
"Purification and structural and functional characterization of FhuA,
a transporter of the Escherichia coli outer membrane.";
Biochemistry 35:14216-14224(1996).
[12]
FUNCTION AS A ION CHANNEL, AND DOMAIN.
PubMed=8617231;
Bonhivers M., Ghazi A., Boulanger P., Letellier L.;
"FhuA, a transporter of the Escherichia coli outer membrane, is
converted into a channel upon binding of bacteriophage T5.";
EMBO J. 15:1850-1856(1996).
[13]
FUNCTION, ACTIVITY REGULATION, INTERACTION WITH TONB, AND DOMAIN.
PubMed=9353297;
Moeck G.S., Coulton J.W., Postle K.;
"Cell envelope signaling in Escherichia coli. Ligand binding to the
ferrichrome-iron receptor fhua promotes interaction with the energy-
transducing protein TonB.";
J. Biol. Chem. 272:28391-28397(1997).
[14]
FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH TONB.
PubMed=12427941; DOI=10.1099/00221287-148-11-3497;
Killmann H., Herrmann C., Torun A., Jung G., Braun V.;
"TonB of Escherichia coli activates FhuA through interaction with the
beta-barrel.";
Microbiology 148:3497-3509(2002).
[15]
INTERACTION WITH TONB, AND DOMAIN.
PubMed=18653801; DOI=10.1110/ps.036244.108;
James K.J., Hancock M.A., Moreau V., Molina F., Coulton J.W.;
"TonB induces conformational changes in surface-exposed loops of FhuA,
outer membrane receptor of Escherichia coli.";
Protein Sci. 17:1679-1688(2008).
[16]
INDUCTION BY HYDROXYUREA.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[17] {ECO:0000244|PDB:1FCP, ECO:0000244|PDB:2FCP}
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-747 IN COMPLEX WITH
FERRICHROME, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=9856937; DOI=10.1126/science.282.5397.2215;
Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W.;
"Siderophore-mediated iron transport: crystal structure of FhuA with
bound lipopolysaccharide.";
Science 282:2215-2220(1998).
[18] {ECO:0000244|PDB:1BY3, ECO:0000244|PDB:1BY5}
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 53-747 IN COMPLEX WITH
FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=9865695; DOI=10.1016/S0092-8674(00)81700-6;
Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L.,
Rosenbusch J.P., Moras D.;
"Transmembrane signaling across the ligand-gated FhuA receptor:
crystal structures of free and ferrichrome-bound states reveal
allosteric changes.";
Cell 95:771-778(1998).
[19] {ECO:0000244|PDB:1QJQ, ECO:0000244|PDB:1QKC}
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 34-747 IN COMPLEXES WITH
PHENYLFERRICROCIN AND ALBOMYCIN.
PubMed=10850805; DOI=10.1110/ps.9.5.956;
Ferguson A.D., Braun V., Fiedler H.-P., Coulton J.W., Diederichs K.,
Welte W.;
"Crystal structure of the antibiotic albomycin in complex with the
outer membrane transporter FhuA.";
Protein Sci. 9:956-963(2000).
-!- FUNCTION: Involved in the uptake of iron in complex with
ferrichrome, an hydroxamate-type siderophore. Binds and transports
ferrichrome-iron across the outer membrane (PubMed:1089064,
PubMed:2066336). In addition to its role in ferrichrome-iron
transport, transports the antibiotic albomycin, which is a
structural analog of ferrichrome, and acts as a receptor for
colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1
(PubMed:1089064, PubMed:353030, PubMed:2066336, PubMed:8617231).
The energy source, which is required for all FhuA functions except
infection by phage T5, is provided by the inner membrane TonB
system (PubMed:353030, PubMed:9353297, PubMed:12427941).
{ECO:0000269|PubMed:1089064, ECO:0000269|PubMed:12427941,
ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:353030,
ECO:0000269|PubMed:8617231, ECO:0000269|PubMed:9353297}.
-!- ACTIVITY REGULATION: Binding of ferrichrome or colicin M enhances
the interaction between FhuA and TonB (PubMed:9353297). TonB
activates FhuA through interaction with the beta-barrel
(PubMed:12427941). {ECO:0000269|PubMed:12427941,
ECO:0000269|PubMed:9353297}.
-!- SUBUNIT: Monomer (PubMed:8916906, PubMed:9856937, PubMed:9865695).
Interacts with TonB (PubMed:9353297, PubMed:12427941,
PubMed:18653801). {ECO:0000269|PubMed:12427941,
ECO:0000269|PubMed:18653801, ECO:0000269|PubMed:8916906,
ECO:0000269|PubMed:9353297, ECO:0000269|PubMed:9856937,
ECO:0000269|PubMed:9865695}.
-!- INTERACTION:
Q9X2V7:mcjA (xeno); NbExp=2; IntAct=EBI-1116714, EBI-16100378;
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:8916906,
ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}; Multi-
pass membrane protein {ECO:0000269|PubMed:9856937,
ECO:0000269|PubMed:9865695}.
-!- INDUCTION: Induced 1.6-fold by hydroxyurea.
{ECO:0000269|PubMed:20005847}.
-!- DOMAIN: Has two distinct conformations in the presence and absence
of ferrichrome. The globular N-terminal domain acts a plug that
closes the channel formed by the beta-barrel. Binding of
ferrichrome at the cell surface induces a conformational change in
FhuA, but does not open the channel. Structural changes are
propagated and amplified across the plug, and may facilitate
binding of FhuA to TonB (PubMed:9865695, PubMed:9353297). TonB
binding promotes conformational changes in outer surface-exposed
loops of FhuA (PubMed:18653801). Phage T5 is a TonB-independent
ligand, and its binding to FhuA results in the formation of high
conductance ion channels (PubMed:8617231, PubMed:9353297).
{ECO:0000269|PubMed:18653801, ECO:0000269|PubMed:8617231,
ECO:0000269|PubMed:9353297, ECO:0000269|PubMed:9865695}.
-!- SIMILARITY: Belongs to the TonB-dependent receptor family.
{ECO:0000305}.
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EMBL; M12486; AAB61768.1; -; Genomic_DNA.
EMBL; U00096; AAC73261.1; -; Genomic_DNA.
EMBL; AP009048; BAB96726.2; -; Genomic_DNA.
EMBL; U70214; AAB08580.1; -; Genomic_DNA.
EMBL; X05810; CAA29253.1; -; Genomic_DNA.
PIR; F64738; QRECFE.
RefSeq; NP_414692.1; NC_000913.3.
RefSeq; WP_000124438.1; NZ_LN832404.1.
PDB; 1BY3; X-ray; 2.74 A; A=34-747.
PDB; 1BY5; X-ray; 2.60 A; A=34-747.
PDB; 1FCP; X-ray; 2.70 A; A=52-747.
PDB; 1FI1; X-ray; 2.90 A; A=52-747.
PDB; 1QFF; X-ray; 2.70 A; A=34-747.
PDB; 1QFG; X-ray; 2.50 A; A=34-747.
PDB; 1QJQ; X-ray; 2.95 A; A=34-747.
PDB; 1QKC; X-ray; 3.10 A; A=34-747.
PDB; 2FCP; X-ray; 2.50 A; A=34-747.
PDB; 2GRX; X-ray; 3.30 A; A/B=34-747.
PDB; 4CU4; X-ray; 2.30 A; A=53-747.
PDBsum; 1BY3; -.
PDBsum; 1BY5; -.
PDBsum; 1FCP; -.
PDBsum; 1FI1; -.
PDBsum; 1QFF; -.
PDBsum; 1QFG; -.
PDBsum; 1QJQ; -.
PDBsum; 1QKC; -.
PDBsum; 2FCP; -.
PDBsum; 2GRX; -.
PDBsum; 4CU4; -.
ProteinModelPortal; P06971; -.
SMR; P06971; -.
BioGrid; 4259745; 139.
DIP; DIP-9602N; -.
IntAct; P06971; 7.
STRING; 316385.ECDH10B_0130; -.
DrugBank; DB02907; 2-Amino-Vinyl-Phosphate.
DrugBank; DB01814; 2-Tridecanoyloxy-Pentadecanoic Acid.
DrugBank; DB02700; 3-Deoxy-D-Glucosamine.
DrugBank; DB03548; 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid.
DrugBank; DB02767; 3-Hydroxy-Myristic Acid.
DrugBank; DB04039; 3-Oxo-Pentadecanoic Acid.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB02724; Delta-2-Albomycin A1.
DrugBank; DB04160; Diphosphate.
DrugBank; DB03574; Ferricrocin-Iron.
DrugBank; DB03111; Glucosamine 1-Phosphate.
DrugBank; DB02865; Glucosamine 4-Phosphate.
DrugBank; DB04526; L-Glycero-D-Manno-Heptopyranose.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB02415; N-Octyl-2-Hydroxyethyl Sulfoxide.
DrugBank; DB02626; Phenylferricrocin-Iron.
DrugBank; DB04220; Rifamycin Cgp 4832.
TCDB; 1.B.14.1.2; the outer membrane receptor (omr) family.
CarbonylDB; P06971; -.
EPD; P06971; -.
PaxDb; P06971; -.
PRIDE; P06971; -.
EnsemblBacteria; AAC73261; AAC73261; b0150.
EnsemblBacteria; BAB96726; BAB96726; BAB96726.
GeneID; 944856; -.
KEGG; ecj:JW0146; -.
KEGG; eco:b0150; -.
PATRIC; fig|1411691.4.peg.2130; -.
EchoBASE; EB0298; -.
EcoGene; EG10302; fhuA.
eggNOG; ENOG4105E0K; Bacteria.
eggNOG; COG1629; LUCA.
HOGENOM; HOG000260252; -.
InParanoid; P06971; -.
KO; K02014; -.
OMA; FSWRPDD; -.
PhylomeDB; P06971; -.
BioCyc; EcoCyc:EG10302-MONOMER; -.
BioCyc; MetaCyc:EG10302-MONOMER; -.
EvolutionaryTrace; P06971; -.
PRO; PR:P06971; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048037; F:cofactor binding; IPI:EcoliWiki.
GO; GO:0005506; F:iron ion binding; IPI:EcoliWiki.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
GO; GO:0015643; F:toxic substance binding; IMP:EcoliWiki.
GO; GO:0046790; F:virion binding; IMP:EcoliWiki.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0015891; P:siderophore transport; IEA:InterPro.
Gene3D; 2.170.130.10; -; 1.
Gene3D; 2.40.170.20; -; 1.
InterPro; IPR012910; Plug_dom.
InterPro; IPR037066; Plug_dom_sf.
InterPro; IPR000531; TonB-dep_rcpt_b-brl.
InterPro; IPR010916; TonB_box_CS.
InterPro; IPR036942; TonB_rcpt_b-brl_sf.
InterPro; IPR010917; TonB_rcpt_CS.
InterPro; IPR010105; TonB_sidphr_rcpt.
Pfam; PF07715; Plug; 1.
Pfam; PF00593; TonB_dep_Rec; 1.
TIGRFAMs; TIGR01783; TonB-siderophor; 1.
PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Ion transport; Iron;
Iron transport; Membrane; Receptor; Reference proteome; Signal;
TonB box; Transmembrane; Transmembrane beta strand; Transport.
SIGNAL 1 33 {ECO:0000269|PubMed:3079747}.
CHAIN 34 747 Ferrichrome outer membrane
transporter/phage receptor.
/FTId=PRO_0000034748.
TOPO_DOM 34 192 Periplasmic.
TRANSMEM 193 201 Beta stranded.
TOPO_DOM 202 206 Extracellular.
TRANSMEM 207 215 Beta stranded.
TOPO_DOM 216 222 Periplasmic.
TRANSMEM 223 231 Beta stranded.
TOPO_DOM 232 245 Extracellular.
TRANSMEM 246 255 Beta stranded.
TOPO_DOM 256 259 Periplasmic.
TRANSMEM 260 268 Beta stranded.
TOPO_DOM 269 312 Extracellular.
TRANSMEM 313 321 Beta stranded.
TOPO_DOM 322 326 Periplasmic.
TRANSMEM 327 335 Beta stranded.
TOPO_DOM 336 387 Extracellular.
TRANSMEM 388 396 Beta stranded.
TOPO_DOM 397 404 Periplasmic.
TRANSMEM 405 413 Beta stranded.
TOPO_DOM 414 464 Extracellular.
TRANSMEM 465 473 Beta stranded.
TOPO_DOM 474 477 Periplasmic.
TRANSMEM 478 486 Beta stranded.
TOPO_DOM 487 508 Extracellular.
TRANSMEM 509 517 Beta stranded.
TOPO_DOM 518 522 Periplasmic.
TRANSMEM 523 531 Beta stranded.
TOPO_DOM 532 551 Extracellular.
TRANSMEM 552 560 Beta stranded.
TOPO_DOM 561 565 Periplasmic.
TRANSMEM 566 574 Beta stranded.
TOPO_DOM 575 601 Extracellular.
TRANSMEM 602 610 Beta stranded.
TOPO_DOM 611 613 Periplasmic.
TRANSMEM 614 622 Beta stranded.
TOPO_DOM 623 645 Extracellular.
TRANSMEM 646 654 Beta stranded.
TOPO_DOM 655 661 Periplasmic.
TRANSMEM 662 670 Beta stranded.
TOPO_DOM 671 689 Extracellular.
TRANSMEM 690 698 Beta stranded.
TOPO_DOM 699 705 Periplasmic.
TRANSMEM 706 714 Beta stranded.
TOPO_DOM 715 737 Extracellular.
TRANSMEM 738 746 Beta stranded.
TOPO_DOM 747 747 Periplasmic.
REGION 148 149 Ferrichrome binding.
{ECO:0000305|PubMed:10850805,
ECO:0000305|PubMed:9856937,
ECO:0000305|PubMed:9865695}.
REGION 277 279 Ferrichrome binding.
{ECO:0000305|PubMed:10850805,
ECO:0000305|PubMed:9856937,
ECO:0000305|PubMed:9865695}.
REGION 346 348 Ferrichrome binding.
{ECO:0000305|PubMed:10850805,
ECO:0000305|PubMed:9856937,
ECO:0000305|PubMed:9865695}.
MOTIF 40 47 TonB box.
MOTIF 730 747 TonB C-terminal box.
BINDING 114 114 Ferrichrome.
{ECO:0000305|PubMed:10850805,
ECO:0000305|PubMed:9856937,
ECO:0000305|PubMed:9865695}.
BINDING 133 133 Ferrichrome.
{ECO:0000305|PubMed:10850805,
ECO:0000305|PubMed:9856937,
ECO:0000305|PubMed:9865695}.
BINDING 424 424 Ferrichrome.
{ECO:0000305|PubMed:9856937}.
BINDING 735 735 Ferrichrome.
{ECO:0000305|PubMed:9856937}.
DISULFID 351 362
DISULFID 725 731
CONFLICT 737 737 R -> P (in Ref. 6; CAA29253).
{ECO:0000305}.
STRAND 44 46 {ECO:0000244|PDB:2GRX}.
HELIX 55 60 {ECO:0000244|PDB:4CU4}.
HELIX 62 64 {ECO:0000244|PDB:4CU4}.
STRAND 65 67 {ECO:0000244|PDB:1BY5}.
TURN 68 70 {ECO:0000244|PDB:4CU4}.
HELIX 76 78 {ECO:0000244|PDB:4CU4}.
STRAND 83 87 {ECO:0000244|PDB:4CU4}.
HELIX 88 94 {ECO:0000244|PDB:4CU4}.
HELIX 99 102 {ECO:0000244|PDB:4CU4}.
TURN 103 105 {ECO:0000244|PDB:4CU4}.
STRAND 106 111 {ECO:0000244|PDB:4CU4}.
TURN 113 116 {ECO:0000244|PDB:4CU4}.
STRAND 124 127 {ECO:0000244|PDB:2GRX}.
HELIX 131 133 {ECO:0000244|PDB:4CU4}.
STRAND 137 139 {ECO:0000244|PDB:4CU4}.
HELIX 156 158 {ECO:0000244|PDB:4CU4}.
STRAND 159 167 {ECO:0000244|PDB:4CU4}.
HELIX 170 173 {ECO:0000244|PDB:4CU4}.
STRAND 178 186 {ECO:0000244|PDB:4CU4}.
STRAND 194 202 {ECO:0000244|PDB:4CU4}.
TURN 203 205 {ECO:0000244|PDB:4CU4}.
STRAND 206 235 {ECO:0000244|PDB:4CU4}.
STRAND 237 240 {ECO:0000244|PDB:2GRX}.
STRAND 242 257 {ECO:0000244|PDB:4CU4}.
STRAND 260 272 {ECO:0000244|PDB:4CU4}.
TURN 284 286 {ECO:0000244|PDB:4CU4}.
STRAND 307 322 {ECO:0000244|PDB:4CU4}.
STRAND 324 350 {ECO:0000244|PDB:4CU4}.
HELIX 354 356 {ECO:0000244|PDB:4CU4}.
HELIX 360 364 {ECO:0000244|PDB:4CU4}.
TURN 367 369 {ECO:0000244|PDB:4CU4}.
HELIX 370 372 {ECO:0000244|PDB:4CU4}.
STRAND 373 400 {ECO:0000244|PDB:4CU4}.
STRAND 403 434 {ECO:0000244|PDB:4CU4}.
TURN 436 438 {ECO:0000244|PDB:1QFG}.
STRAND 445 447 {ECO:0000244|PDB:2FCP}.
TURN 450 452 {ECO:0000244|PDB:4CU4}.
STRAND 453 475 {ECO:0000244|PDB:4CU4}.
STRAND 478 495 {ECO:0000244|PDB:4CU4}.
TURN 496 499 {ECO:0000244|PDB:4CU4}.
STRAND 500 517 {ECO:0000244|PDB:4CU4}.
STRAND 522 534 {ECO:0000244|PDB:4CU4}.
STRAND 543 545 {ECO:0000244|PDB:4CU4}.
STRAND 549 560 {ECO:0000244|PDB:4CU4}.
STRAND 565 584 {ECO:0000244|PDB:4CU4}.
STRAND 586 588 {ECO:0000244|PDB:1BY3}.
STRAND 590 610 {ECO:0000244|PDB:4CU4}.
STRAND 612 630 {ECO:0000244|PDB:4CU4}.
TURN 632 636 {ECO:0000244|PDB:4CU4}.
STRAND 644 655 {ECO:0000244|PDB:4CU4}.
STRAND 656 658 {ECO:0000244|PDB:1QJQ}.
TURN 659 662 {ECO:0000244|PDB:4CU4}.
STRAND 663 672 {ECO:0000244|PDB:4CU4}.
STRAND 675 678 {ECO:0000244|PDB:4CU4}.
STRAND 683 685 {ECO:0000244|PDB:4CU4}.
STRAND 688 698 {ECO:0000244|PDB:4CU4}.
HELIX 699 702 {ECO:0000244|PDB:4CU4}.
STRAND 708 715 {ECO:0000244|PDB:4CU4}.
STRAND 722 727 {ECO:0000244|PDB:4CU4}.
STRAND 730 733 {ECO:0000244|PDB:4CU4}.
STRAND 738 746 {ECO:0000244|PDB:4CU4}.
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


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