Ubiquitin is a 76-amino acid, well-folded and highly stable protein that is highly conserved across all eukaryotes. It is a post-translational modifier of other proteins through itsattachment via an isopeptide bond to a substrate lysine sidechain. Multiple ubiquitin units can be stacked to form a polyubiquitin chain, with chain topologies and cellular outcomes varying based on which of ubiquitin’s lysine residues they are attached to. The most common and well-studied outcome of polyubiquitin attachment is degradation by the proteasome, a massive barrel-shaped protease complex responsible for general protein quality control as well as cell cycle progression. Proteasomes have been discovered in archaea and bacteria, and are controlled by the small archaeal modifier protein (SAMP) and the disordered prokaryotic ubiquitin-like protein (Pup), respectively. Recently, a second bacterial proteasome operon was discovered with a new putative signaling protein, ubiquitin bacterial (UBact). Here, the first investigation of the UBact proteasomal operon is presented. Using nuclear magnetic resonance (NMR) spectroscopy and a variety of biophysical techniques, UBact is demonstrated to be disordered in solution and interact with its putative proteasomal receptor. This sets the groundwork for further studies of the UBact system. Additionally, NMR is used to explore the activity and directionality of various deubiquitinase enzymes responsible for breaking down polyubiquitin chains, and for exploring small molecule binding to ubiquitin chains themselves. This likewise provides a groundwork for further studies of the ubiquitin system, whose dysregulation is responsible for many diseases and is an area of intense therapeutic development.