Matches in DBpedia 2016-04 for { ?s ?p "FepA is an integral bacterial outer membrane porin protein, which is involved in the active transport of iron from the extracellular space, into the periplasm of Gram-negative bacteria.A Gram-negative bacterium secretes iron-binding proteins called siderophores, which bind strongly to ferric ions. The FepA receptor is present at the outer membrane and binds to ferric siderophores, and actively transport it into the cell. FepA has also been shown to transport vitamin B12, and colicins B and D as well. This protein belongs to family of ligand-gated protein channels.Because no energy is directly available to the outer membrane, FepA has been studied to determine the mechanism by which energy is brought to the outer membrane to drive the transport. It was found that the energy to drive the active transport originates from the proton motive force (electrochemical gradient) generated in the inner membrane complex TonB–ExbB–ExbD, and this force is relayed physically to FepA through the TonB subunit."@en }
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- FepA abstract "FepA is an integral bacterial outer membrane porin protein, which is involved in the active transport of iron from the extracellular space, into the periplasm of Gram-negative bacteria.A Gram-negative bacterium secretes iron-binding proteins called siderophores, which bind strongly to ferric ions. The FepA receptor is present at the outer membrane and binds to ferric siderophores, and actively transport it into the cell. FepA has also been shown to transport vitamin B12, and colicins B and D as well. This protein belongs to family of ligand-gated protein channels.Because no energy is directly available to the outer membrane, FepA has been studied to determine the mechanism by which energy is brought to the outer membrane to drive the transport. It was found that the energy to drive the active transport originates from the proton motive force (electrochemical gradient) generated in the inner membrane complex TonB–ExbB–ExbD, and this force is relayed physically to FepA through the TonB subunit.".
- Q5443729 abstract "FepA is an integral bacterial outer membrane porin protein, which is involved in the active transport of iron from the extracellular space, into the periplasm of Gram-negative bacteria.A Gram-negative bacterium secretes iron-binding proteins called siderophores, which bind strongly to ferric ions. The FepA receptor is present at the outer membrane and binds to ferric siderophores, and actively transport it into the cell. FepA has also been shown to transport vitamin B12, and colicins B and D as well. This protein belongs to family of ligand-gated protein channels.Because no energy is directly available to the outer membrane, FepA has been studied to determine the mechanism by which energy is brought to the outer membrane to drive the transport. It was found that the energy to drive the active transport originates from the proton motive force (electrochemical gradient) generated in the inner membrane complex TonB–ExbB–ExbD, and this force is relayed physically to FepA through the TonB subunit.".