Two fep genes are required for ferrienterochelin uptake in Escherichia coli K-12.

Escherichia coli mutants defective in the assimilation of iron from ferrienterochelin were isolated and characterized. One mutant was able to bind ferrienterochelin to its outer membrane but could not transport it into the cell. Complementation tests with lambda hybrid phage were employed to distinguish the defective gene, which we term fepB, from fepA, the structural gene for the outer membrane ferrienterochelin receptor protein. These same physiological and genetic tests were employed to tentatively classify several previously described fep mutants as carrying either fepA or fepB. The data demonstrate the existence of fepB and provide an explanation for previous difficulties in identifying fepB mutants.