Nature has produced a large range of motor protein complexes that transform chemical energy into mechanical work. The remarkable efficiency of these motors makes life under far from equilibrium conditions possible. Despite their critical importance many aspects of their mechanisms are yet to be fully determined. These including the relative contributions of Brownian ratchet and power-stroke mechanisms, and how information is transduced across the motor. Natural motors are highly evolved and optimised machines, making reductionist studies of their mechanisms difficult. An alternate route is to design motors from scratch, where the mechanism of action can be rationally designed, modified and dissected. In the first step towards this overall goal, we have designed a three-legged artificial clocked protein walker, dubbed Tumbleweed. Tumbleweed is designed to walk on a DNA track using feet derived from ligand-dependent bacterial transcriptional repressor proteins. Alternating the flux of ligands will allow for the control of foot binding, enabling Tumbleweed to walk along a track. We have purified the designed components and assembled them into a single functional unit using native protein ligation techniques. Mass photometry experiments show that Tumbleweed is a well behaved monomer when free in solution, and binds DNA tracks with a 1:1 stoichiometry. Surface plasmon resonance experiments indicate that Tumbleweed can bind DNA in a biphasic manner, with both short- and long-lived states. These experiments are being used to inform walking experiments by SPR and single molecule fluorescence. Our studies of Tumbleweed will provide the basis for designing, producing and characterising more complex artificial autonomous protein motors, which in turn will help illuminate the fundamental mechanisms of natural protein motors.