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Site fhuA
- Name: fhuA
- Type: Gene
- Synonyms
b0150 MG1655 locus tag T1 T5rec tonA - Mnemonic: Ferric hydroxamate uptake
- Left End Point: 3.61
- Right End Point: 3.66
- Products:
outer membrane protein receptor for ferrichrome, colicin M, and phages T1, T5, and phi-80 - Direction: >
- Properties:
Property Comment transport gene iron-siderophore, ferrichrome: unusual specific transport across outer membrane due to size and low conc. - Priority: 0
- External Database Links:
Host Site Page Links NCBI/GenBank M12486 EcoGene.org EG10302 EcoliWiki fhuA - Comment:
- Selectable phenotype. Loss: albomycin, phages T1, T5, colicin M resistance. receptor protein for energy-coupled transport of Fe3+ via ferrichrome through outer membrane
- References:
- Luckey, M., J.R. Pollack, R. Wayne, B.N. Ames, J.B. Neilands 1972. Iron uptake in Salmonella typhimurium: utilization of exogenous siderochromes as iron carriers. J.Bacteriol. 111:731-738
- Luckey, M., J.B. Neilands 1976. Iron transport in Salmonella typhimurium LT-2: prevention, by ferrichrome, of adsorption of bacteriophages ES18 and ES18.h1 to a common cell envelope receptor. J.Bacteriol. 127:1036-1037
- Braun, V., K. Hantke, W. Stauder 1977. Identification of the sid outer membrane receptor protein in Salmonella typhimurium SL-1024. Mol.Gen.Genet. 155:227-229
- Kadner, R.J., K. Heller, J.W. Coulton, V. Braun 1980. Genetic control of hydroxamate-mediated iron uptake in Escherichia coli. J.Bacteriol. 143:256-264
- Fecker, L., V. Braun 1983. Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli. J.Bacteriol. 156:1301-1314
- Coulton, J.W., P. Mason, M.S. DuBow 1983. Molecular cloning of the ferrichrome-iron receptor of Escherichia coli K-12. J.Bacteriol. 156:1315-1321
- Braun, V., R. Gross, W. Koster, L. Zimmerman 1983. Plasmid and chromosomal mutants in the iron (III)-aerobactin transport system of Escherichia coli. Mol.Gen.Genet. 192:131-139
- Coulton, J.W., P. Mason, D.R. Cameron, G. Carmel, R. Jean, H.N. Rode 1986. Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12. J.Bacteriol. 165:181-192
- Killmann, H., V. Braun 1992. An aspartate deletion mutation defines a binding site of the multifunctional FhuA outer membrane receptor of Escherichia coli K-12. J.Bacteriol. 174:3479-3486
- Killmann, H., R. Benz, V. Braun 1993. Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. EMBO J. 12:3007-3016
- Killmann, H., V. Braun 1994. Energy-dependent receptor activities of Escherichia coli K-12: mutated TonB proteins alter FhuA receptor activities to phages T5, T1, phi80 and to colicin M. FEMS Microbiol.Lett. 119:71-76
- Braun, V., H. Killmann, R. Benz 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
- Neilands, J.B. 1995. Siderophores: structure and function of microbial iron transport compounds. J.Biol.Chem. 270:26723-26726
- Boulanger, P., M. le Maire, M. Bonhivers, S. Dubois, M. Desmadril, L. Letellier 1996. Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 35:14216-14224