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FhuA is a multifunctional outer membrane protein in *Escherichia coli* responsible for the uptake of ferrichrome, an iron-chelating siderophore. It also acts as a receptor for certain bacteriophages (T1, T5, phi80) and antibiotics (albomycin, rifamycin), facilitating their entry into the cell. FhuA's structure comprises a 22-stranded β-barrel and an N-terminal cork domain that undergoes conformational changes during substrate transport and phage infection. Its function is essential for bacterial survival in iron-limited environments, making it a potential target for novel antibacterial strategies and phage therapy.
TonB-dependent energy transduction facilitates ferrichrome-iron complex transport across the outer membrane. Functions as a receptor for phage adsorption and DNA injection.
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