Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably bound at the interface of two monomers. Homodimer. Up-regulated under conditions of iron depletion or oxidative stress, via IscR. Is also induced by heat shock or the presence of misfolded proteins. Consits of two domains, an N-terminal domain that resembles the so-called Fe/S A-type scaffold, and a C-terminal domain that shares sequence identity with Nfu-type scaffold proteins. Both domains are important for NfuA to fulfill its function in vivo. The N-terminal domain does not possess the three conserved cysteine residues thought to act as Fe/S cluster ligands in A-type scaffold proteins, but may keep the ability to interact with apoproteins. Cells express the stationary phase-specific competition-defective (SPCD) phenotype and are unable to catabolize dsDNA. Belongs to the NfuA family. Was originally thought to be involved in gluconate metabolism and was referred to as GntY.