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The protein Clp fromXanthomonas axonopodis pv. citri regulates pathogenesis and is a member of the CRP (cyclic AMP receptor protein) superfamily. We show that unlike the DNA-binding activity of other members of this family, the DNA-binding activity of Clp is allosterically inhibited by its effector and that cyclic di-GMP serves as that effector at physiological concentrations.

Cyclic di-GMP Allosterically Inhibits the CRP-Like Protein (Clp) of Xanthomonas axonopodis pv. citri