UniProt functional annotation for P06971



	UniProt functional annotation for P06971

UniProt code: P06971.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Involved in the uptake of iron in complex with ferrichrome, a 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}.

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}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Involved in the uptake of iron in complex with ferrichrome, a 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}.
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}.