Ferrous iron transport protein B (FeoB)

Ferrous iron transport protein B (FeoB) is an integral membrane protein found in many prokaryotes (bacteria and archaea) and is a principal component of the Feo system, which enables high-affinity uptake of ferrous iron (\( Fe^{2+} \)) under reducing and anaerobic conditions[1][2][3][4][5]. FeoB typically consists of 700–800 amino acids, with an N-terminal cytosolic G-protein (GTPase) domain that regulates transport activity, and a C-terminal membrane domain forming the translocation pore[1][4][5]. The Feo system commonly includes at least two genes, feoA and feoB, sometimes feoC, but FeoB is essential for mediating ferrous iron import[2][3][4][5]. FeoB is vital for maintaining cellular iron homeostasis and is crucial for the virulence and survival of pathogenic bacteria in host environments, particularly where iron is limiting[2][3][4][5]. This protein does not exist in animals or plants, making it a potential target for antimicrobial drug discovery, but there are currently no direct small-molecule inhibitors in therapeutic use[4][5].

Other names

FeoBFerrous iron transporter BIron transport protein FeoBFerrous iron uptake protein B

N/A for small-molecule drugs (the target is principally inhibited or studied genetically; no approved drugs directly inhibit FeoB) Potential mechanisms: inhibition of iron uptake, occupation of transporter, GTPase inhibition (experimental)