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Using anion-exchange high-pressure liquid chromatography (HPLC), we purified legiobactin from culture supernatants of a virulent strain of<jats:italic>L. pneumophila<\/jats:italic>. In the process, we detected the ferrated form of legiobactin as well as other CAS-reactive substances. Purified legiobactin had a yellow-gold color and absorbed primarily from 220 nm and below. In accordance, nuclear magnetic resonance spectroscopy revealed that legiobactin lacks aromatic carbons, and among the 13 aliphatics present, there were 3 carbonyls. When examined by HPLC, supernatants from<jats:italic>L. pneumophila<\/jats:italic>mutants inactivated for<jats:italic>lbtA<\/jats:italic>and<jats:italic>lbtB<\/jats:italic>completely lacked legiobactin, indicating that the LbtA and LbtB proteins are absolutely required for siderophore activity. Independently derived<jats:italic>lbtA<\/jats:italic>mutants, but not a complemented derivative, displayed a reduced ability to infect the lungs of A\/J mice after intratracheal inoculation, indicating that legiobactin is required for optimal intrapulmonary survival by<jats:italic>L. pneumophila<\/jats:italic>. This defect, however, was not evident when the<jats:italic>lbtA<\/jats:italic>mutant and its parental strain were coinoculated into the lung, indicating that legiobactin secreted by the wild type can promote growth of the mutant in<jats:italic>trans<\/jats:italic>. Legiobactin mutants grew normally in murine lung macrophages and alveolar epithelial cells, suggesting that legiobactin promotes something other than intracellular infection of resident lung cells. 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