The current study was directed to create the first 3D structure and propose probable functions of the Yersinia pestis hypothetical protein AVO28_00330. It was submitted as the new record to the protein model database. The identified protein revealed its essential role in the regulation of the lipopolysaccharide metabolic process of the bacterium cell using globin-like folding pattern. Predicted active binding sites of the homology modeled protein would be helpful for further investigation of therapeutic drug designing against the protein using the molecular docking approach. The physicochemical, structural and functional annotation would provide a better understanding of the protein's activity. This sort of methodology would be helpful in the structural and functional elucidation of other uncharacterized proteins. Finally, in vitro experimentation should be conducted to validate the predicted results that are shown here and to annotate the protein's role in biotechnology.