Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. Cloning and sequencing of the iron(II) transport genes revealed an open reading frame (feoA) possibly coding for a small protein with 75 amino acids and a membrane protein with 773 amino acids (feoB). The upstream region offeoAB contained a binding site for the regulatory protein Fur, which acts with iron(ll) as a corepressor in all known iron transport systems ofE. coli. In addition, a Fnr binding site was identified in the promoter region. The FeoB protein had an apparent molecular mass of 70 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was localized in the cytoplasmic membrane.The sequence revealed regions of homology to ATPases, which indicates that ferrous iron uptake may be ATP driven. FeoA or FeoB mutants could be complemented by clones with the feoA orfeoB gene, respectively.Since iron(III) is practically insoluble at neutral pH, many aerobic microorganisms secrete siderophores, iron(III) chelating compounds, for their iron supply. Six different siderophore-iron(III) transport systems in Escherichia coli have been sequenced and analyzed, and many more in other gram-negative bacteria have been characterized (4). These transport systems share a common structure. A ferric siderophore-specific receptor in the outer membrane delivers its substrate in an energy-dependent mechanism to the periplasm. The energy is provided by the TonB-ExbB-ExbD complex (4). Even heme (33) and transferrin iron (6) are taken up in a TonB-dependent manner. With