Protein Domain : Ferric-uptake regulator IPR002481

Type	Family
Description	The Ferric uptake regulator (Fur) family includes metal ion uptake regulator proteins, which are responsible for controlling the intracellular concentration of iron in many bacteria. The Fur protein (a dimer having one Fe 2+coordinated per monomer) acts as an iron-responsive, DNA-binding repressor protein that binds to a 'Furbox' with the consensus sequence GATAATGATAATCATTATC in the promoter of iron-regulated genes. Under low-iron condition, the Fur protein is released from the promoter and transcription resumed []. Some members sense metal ions other than Fe 2+. For example, the zinc uptake regulator (Zur) responds to Zn 2+[ ], the manganese uptake regulator (Mur) responds to Mn2+, and the nickel uptake regulator (Nur) responds to Ni 2+[ , ]. Other members sense signals other than metal ions. For example, PerR, a metal-dependent sensor of hydrogen peroxide. PerR regulates DNA-binding activity through metal-based protein oxidation, and co-ordinates Mn2+or Fe 2+at its regulatory site [ ]. Furs can also control zinc homeostasis and is the subject of research on the pathogenesis of mycobacteria [, ]. Fur family proteins contain an N-terminal winged-helix DNA-binding domain followed by a dimerization domain; this entry spans both those domains [, , , , , , , , , , , , , , , , , , , , , , ].
Short Name	FUR