Cell cycle dependent proteolysis is an extremely important process for cell viability and homeostasis. A great example of this is the ClpXP protease in Caulobacter crescentus which is responsible for maintaining quality control and timely degradation of substrates to drive cell cycle progression. ClpXP utilizes three different adaptor proteins to achieve selective degradation. This thesis will focus on the last two adaptors in this hierarchy, RcdA and PopA. Aiming to uncover the binding interface between RcdA and PopA along with understanding the full mechanism of how their interaction facilitates CtrA degradation. In the presence of cyclic di- GMP when RcdA binds to PopA it allows for delivery of CtrA, a master regulator in Caulobacter crescentus for degradation via the ClpXP protease. This thesis will also give insight into the role that cyclic di-GMP is playing in delivering CtrA for degradation. The remainder of this thesis will present the data that was collected investigating these projects.