Ferrichrome-iron receptor (P06971)

Identification
Name:Ferrichrome-iron receptor
Synonyms:
  • Ferric hydroxamate receptor
  • Ferric hydroxamate uptake
Gene Name:fhuA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in receptor activity
Specific Function:This receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin
Cellular Location:Cell outer membrane; Multi-pass membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Transports:
Transport References:
  • Orth, J. D., Conrad, T. M., Na, J., Lerman, J. A., Nam, H., Feist, A. M., Palsson, B. O. (2011). "A comprehensive genome-scale reconstruction of Escherichia coli metabolism--2011." Mol Syst Biol 7:535. Pubmed: 21988831
Metabolites:
ECMDB IDNameView
ECMDB21218FerrichromeMetaboCard
ECMDB21217Ferrichrome minus Fe(III)MetaboCard
ECMDB21333FerroxamineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Component
cell part
membrane
Function
binding
cation binding
cation transmembrane transporter activity
di-, tri-valent inorganic cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
ion binding
ion transmembrane transporter activity
iron ion binding
iron ion transmembrane transporter activity
metal ion binding
molecular transducer activity
receptor activity
siderophore-iron transmembrane transporter activity
signal transducer activity
substrate-specific transmembrane transporter activity
transition metal ion binding
transmembrane transporter activity
transporter activity
Process
establishment of localization
siderophore transport
transport
Gene Properties
Blattner:b0150
Gene OrientationClockwise
Centisome Percentage:3.61
Left Sequence End167484
Right Sequence End169727
Gene Sequence:
>2244 bp
ATGGCGCGTTCCAAAACTGCTCAGCCAAAACACTCACTGCGTAAAATCGCAGTTGTAGTA
GCCACAGCGGTTAGCGGCATGTCTGTTTATGCACAGGCAGCGGTTGAACCGAAAGAAGAC
ACTATCACCGTTACCGCTGCACCTGCGCCGCAAGAAAGCGCATGGGGGCCTGCTGCAACT
ATTGCGGCGCGACAGTCTGCTACCGGCACTAAAACCGATACGCCGATTCAAAAAGTGCCA
CAGTCTATTTCTGTTGTGACCGCCGAAGAGATGGCGCTGCATCAGCCGAAGTCGGTAAAA
GAAGCGCTTAGCTACACGCCGGGTGTCTCTGTTGGTACGCGTGGCGCATCCAACACCTAT
GACCACCTGATCATTCGCGGCTTTGCGGCAGAAGGCCAAAGCCAGAATAACTATCTGAAT
GGCCTGAAGTTGCAGGGCAACTTCTATAACGATGCGGTCATTGACCCGTATATGCTGGAA
CGCGCTGAAATTATGCGTGGCCCGGTTTCCGTGCTTTACGGTAAAAGCAGTCCTGGCGGC
CTGTTGAATATGGTCAGCAAGCGTCCGACCACCGAACCGCTGAAAGAAGTTCAGTTTAAA
GCCGGTACTGACAGCCTGTTCCAGACTGGTTTTGACTTTAGCGATTCGTTGGATGATGAC
GGTGTTTACTCTTATCGCCTGACCGGTCTTGCGCGTTCTGCCAATGCCCAGCAGAAAGGG
TCAGAAGAGCAGCGTTATGCTATTGCACCGGCGTTCACCTGGCGTCCGGATGATAAAACC
AATTTTACCTTCCTTTCTTACTTCCAGAACGAGCCGGAAACCGGTTATTACGGCTGGTTG
CCGAAAGAGGGAACCGTTGAGCCGCTGCCGAACGGTAAGCGTCTGCCGACAGACTTTAAT
GAAGGGGCGAAGAACAACACCTATTCTCGTAATGAGAAGATGGTCGGCTACAGCTTCGAT
CACGAATTTAACGACACCTTTACTGTGCGTCAGAACCTGCGCTTTGCTGAAAACAAAACC
TCGCAAAACAGCGTTTATGGTTACGGCGTCTGCTCCGATCCGGCGAATGCTTACAGCAAA
CAGTGTGCGGCATTAGCGCCAGCGGATAAAGGCCATTATCTGGCACGTAAATACGTCGTT
GATGATGAGAAGCTGCAAAACTTCTCCGTTGATACCCAGTTGCAGAGCAAGTTTGCCACT
GGCGATATCGACCACACCCTGCTGACCGGTGTCGACTTTATGCGTATGCGTAATGACATC
AACGCCTGGTTTGGTTACGACGACTCTGTGCCACTGCTCAATCTGTACAATCCGGTGAAT
ACCGATTTCGACTTCAATGCCAAAGATCCGGCAAACTCCGGCCCTTACCGCATTCTGAAT
AAACAGAAACAAACGGGCGTTTATGTTCAGGATCAGGCGCAGTGGGATAAAGTGCTGGTC
ACCCTAGGCGGTCGTTATGACTGGGCAGATCAAGAATCTCTTAACCGCGTTGCCGGGACG
ACCGATAAACGTGATGACAAACAGTTTACCTGGCGTGGTGGTGTTAACTACCTGTTTGAT
AATGGTGTAACACCTTACTTCAGCTATAGCGAATCGTTTGAACCTTCTTCGCAAGTTGGG
AAGGATGGTAATATTTTCGCACCGTCTAAAGGTAAGCAGTATGAAGTCGGCGTGAAATAT
GTACCGGAAGATCGTCCGATTGTAGTTACTGGTGCCGTGTATAATCTCACTAAAACCAAC
AACCTGATGGCGGACCCTGAGGGTTCCTTCTTCTCGGTTGAAGGTGGCGAGATCCGCGCA
CGTGGCGTAGAAATCGAAGCGAAAGCGGCGCTGTCGGCGAGTGTTAACGTAGTCGGTTCT
TATACTTACACCGATGCGGAATACACCACCGATACTACCTATAAAGGCAATACGCCTGCA
CAGGTGCCAAAACACATGGCTTCGTTGTGGGCTGACTACACCTTCTTTGACGGTCCGCTT
TCAGGTCTGACGCTGGGCACCGGTGGTCGTTATACTGGCTCCAGTTATGGTGATCCGGCT
AACTCCTTTAAAGTGGGAAGTTATACGGTCGTGGATGCGTTAGTACGTTATGATCTGGCG
CGAGTCGGCATGGCTGGCTCCAACGTGGCGCTGCATGTTAACAACCTGTTCGATCGTGAA
TACGTCGCCAGCTGCTTTAACACTTATGGCTGCTTCTGGGGCGCAGAACGTCAGGTCGTT
GCAACCGCAACCTTCCGTTTCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:747
Protein Molecular Weight:82182
Protein Theoretical pI:5
PDB File:1BY3
Signaling Regions:
  • 1-33
Transmembrane Regions:
  • 193-201
  • 207-215
  • 223-231
  • 246-255
  • 260-268
  • 313-321
  • 327-335
  • 388-396
  • 405-413
  • 465-473
  • 478-486
  • 509-517
  • 523-531
  • 552-560
  • 566-574
  • 602-610
  • 614-622
  • 646-654
  • 662-670
  • 690-698
  • 706-714
  • 738-746
Protein Sequence:
>Ferrichrome-iron receptor
MARSKTAQPKHSLRKIAVVVATAVSGMSVYAQAAVEPKEDTITVTAAPAPQESAWGPAAT
IAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTY
DHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGG
LLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKG
SEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFN
EGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSK
QCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDI
NAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLV
TLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVG
KDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRA
RGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPL
SGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDRE
YVASCFNTYGCFWGAERQVVATATFRF
References
External Links:
ResourceLink
Uniprot ID:P06971
Uniprot Name:FHUA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674356
PDB ID:1BY3
Ecogene ID:EG10302
Ecocyc:EG10302
ColiBase:b0150
Kegg Gene:b0150
EchoBASE ID:EB0298
CCDB:FHUA_ECOLI
BacMap:16128143
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bonhivers, M., Ghazi, A., Boulanger, P., Letellier, L. (1996). "FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5." EMBO J 15:1850-1856. Pubmed: 8617231
  • Braun, V., Killmann, H., Benz, R. (1994). "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. Pubmed: 7515827
  • Burkhardt, R., Braun, V. (1987). "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. Pubmed: 2823072
  • Coulton, J. W., Mason, P., Cameron, D. R., Carmel, G., Jean, R., Rode, H. N. (1986). "Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12." J Bacteriol 165:181-192. Pubmed: 3079747
  • Ferguson, A. D., Braun, V., Fiedler, H. P., Coulton, J. W., Diederichs, K., Welte, W. (2000). "Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA." Protein Sci 9:956-963. Pubmed: 10850805
  • Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., Welte, W. (1998). "Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide." Science 282:2215-2220. Pubmed: 9856937
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "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. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., Moras, D. (1998). "Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes." Cell 95:771-778. Pubmed: 9865695