Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.

Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.

Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Membrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Ferrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...]

Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. 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. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.