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Vibrio cholerae uses the catechol siderophore vibriobactin for iron transport under iron-limiting conditions. We have identified genes for vibriobactin transport and mapped them within the vibriobactin biosynthetic gene cluster. Within this genetic region we have identified four genes,viuP ,viuD ,viuG andviuC , whose protein products have homology to the periplasmic binding protein, the two integral cytoplasmic membrane proteins, and the ATPase component, respectively, of other iron transport systems. The amino-terminal region of ViuP has homology to a lipoprotein signal sequence, and ViuP could be labeled with [3 H]palmitic acid. This suggests that ViuP is a membrane lipoprotein. The ViuPDGC system transports both vibriobactin and enterobactin inEscherichia coli . In the same assay, theE. coli enterobactin transport system, FepBDGC, allowed the utilization of enterobactin but not vibriobactin. Although the entireviuPDGC system could complement mutations infepB ,fepD ,fepG , orfepC , onlyviuC was able to independently complement the correspondingfep mutation. This indicates that these proteins usually function as a complex.V. cholerae strains carrying a mutation inviuP or inviuG were constructed by marker exchange. These mutations reduced, but did not completely eliminate, vibriobactin utilization. This suggests thatV. cholerae contains genes in addition toviuPDGC that function in the transport of catechol siderophores.

A Multifunctional ATP-Binding Cassette Transporter System from Vibrio cholerae Transports Vibriobactin and Enterobactin