Iron(3+)-hydroxamate-binding protein FhuD
Details
- Name
- Iron(3+)-hydroxamate-binding protein FhuD
- Synonyms
- Ferric hydroxamate uptake protein D
- Ferrichrome-binding periplasmic protein
- Iron(III)-hydroxamate-binding protein FhuD
- Gene Name
- fhuD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010966|Iron(3+)-hydroxamate-binding protein FhuD MSGLPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVA DTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGR GFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLT TLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDH DNSKDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGKA
- Number of residues
- 296
- Molecular Weight
- 32997.965
- Theoretical pI
- 6.37
- GO Classification
- Processesion transport / iron ion homeostasisComponentsperiplasmic space
- General Function
- Not Available
- Specific Function
- Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin.
- Pfam Domain Function
- Peripla_BP_2 (PF01497)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0010967|Iron(3+)-hydroxamate-binding protein FhuD (fhuD) ATGAGCGGCTTACCTCTTATTTCGCGCCGTCGACTGTTAACGGCGATGGCGCTTTCTCCG TTGTTATGGCAGATGAATACCGCCCACGCGGCGGCTATTGATCCCAATCGTATTGTGGCG CTGGAGTGGTTGCCGGTGGAATTACTGCTGGCGCTCGGCATCGTGCCTTACGGCGTGGCG GATACCATCAACTATCGCCTGTGGGTCAGCGAACCACCATTGCCGGACTCAGTGATCGAC GTCGGTTTGCGCACAGAACCTAACCTTGAACTGCTGACCGAAATGAAACCATCGTTTATG GTCTGGTCGGCAGGATATGGCCCTTCACCAGAAATGCTGGCTCGTATTGCGCCGGGTCGC GGATTTAACTTCAGTGACGGCAAACAGCCGTTGGCGATGGCGCGTAAATCGCTGACGGAA ATGGCAGATTTACTTAACCTGCAAAGCGCAGCGGAAACGCATTTAGCGCAATATGAAGAC TTTATCCGCAGCATGAAACCCCGCTTTGTGAAGCGTGGTGCGCGTCCGTTATTGCTGACG ACGCTTATCGATCCGCGCCATATGCTGGTCTTCGGTCCAAACAGCTTGTTCCAGGAAATT CTTGATGAGTACGGCATCCCAAATGCCTGGCAAGGGGAAACCAACTTCTGGGGCAGTACC GCCGTCAGTATCGATCGTCTGGCGGCGTATAAAGACGTTGATGTGCTCTGTTTTGATCAC GACAACAGCAAAGACATGGATGCGCTAATGGCAACGCCGCTGTGGCAGGCCATGCCGTTT GTCCGCGCCGGACGCTTTCAGCGCGTACCTGCAGTCTGGTTTTATGGTGCGACGCTCTCG GCAATGCACTTTGTGCGCGTTCTGGATAACGCCATCGGAGGTAAAGCGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P07822 UniProtKB Entry Name FHUD_ECOLI GenBank Protein ID 41440 GenBank Gene ID X05810 - General References
- Coulton JW, Mason P, Allatt DD: fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12. J Bacteriol. 1987 Aug;169(8):3844-9. [Article]
- 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. 1987 Aug;209(1):49-55. [Article]
- 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. 1994 May 11;22(9):1637-9. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Rohrback MR, Paul S, Koster W: In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence. Mol Gen Genet. 1995 Jul 22;248(1):33-42. [Article]
- Tullman-Ercek D, DeLisa MP, Kawarasaki Y, Iranpour P, Ribnicky B, Palmer T, Georgiou G: Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides. J Biol Chem. 2007 Mar 16;282(11):8309-16. Epub 2007 Jan 11. [Article]
- Davies BW, Kohanski MA, Simmons LA, Winkler JA, Collins JJ, Walker GC: Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli. Mol Cell. 2009 Dec 11;36(5):845-60. doi: 10.1016/j.molcel.2009.11.024. [Article]
- Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW: The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Biol. 2000 Apr;7(4):287-91. [Article]
- Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ: X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J Biol Chem. 2002 Apr 19;277(16):13966-72. Epub 2002 Jan 22. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01747 Coprogen experimental unknown Details DB02724 Delta-2-Albomycin A1 experimental unknown Details DB03436 Gallichrome experimental unknown antagonist Details DB13949 Ferric cation approved unknown binder Details DB14520 Tetraferric tricitrate decahydrate approved unknown binder Details