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The nucleotide sugar transporter family, FAD-binding proteins (FAD-BPs), is a superfamily of low-affinity ATP/ADP translocases. In this study, we characterized the FAD66 family of proteins in the phytopathogenic bacterium Pseudomonas syringae pv. tomato. Genome analysis indicated that 12 FAD66 genes are present in P. syringae, which is in contrast to the three members in Escherichia coli. The conserved FAD66 motifs were identified in all the P. syringae FAD66 family members. Phylogenetic analysis revealed that the P. syringae FAD66 family consists of three distinct subfamilies, and FadH subfamily members possess a distinct function as heat-shock protein Hsp16 in E. coli. Phenotypic analysis indicated that the FAD66 family is required for swarming motility, virulence, and plant invasion. Direct evidence of the pathogenicity of the putative ADP/ATP translocase was provided by comparing the invasion of wild-type and adenine-deficient mutants through tobacco stems. The adenine concentration in the plant vacuoles was also determined by high-performance liquid chromatography. Our data suggest that P. syringae uses the adenine translocator to transport the adenine into plant vacuoles.Q:
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