The ferric iron repressed outer-membrane protein) gene was cloned from by screening a library of Tn insertion mutants for iron-repressed fusions to The gene encoded an 80 kDa outer-membrane protein with a high level of amino acid sequence identity to several bacterial proteins belonging to the family of Ton B-dependent outer-membrane receptors. BfrA was especially homologous to Cir of , IrgA of and to three previously characterized ferric enterobactin receptors. DNA hybridization results indicated that was not present in other species. Expression of the gene was induced by low iron availability from a promoter overlapped by a sequence resembling a consensus Fur-binding sequence, and expression was derepressed in a mutant. Utilization of the siderophore alcaligin and the exogenous siderophore enterobactin was unaffected in mutants. Upon attempting to find the specificity of BfrA, 2,3-dihydroxybenzoylserine (DHBS) was shown to be utilized in a ferric enterobactin receptor gene)-dependent manner by and In addition, the hydroxamate siderophores ferrichrome and desferrioxamine B, and the iron source haemin were shown to be utilized independently of and in and


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