The concerned protein protease HtpX homolog is associated with endodontic infections. This protein is a putative membrane-bound zinc metalloprotease that participates in the proteolytic quality control of membrane proteins. Any structural or functional disturbance may lead to infections. A computational proteomic study was performed that included retrieval of the concerned protein sequence from UniProt, sequence homology search by UniProt BLAST, physicochemical characterization by ProtParam, multiple sequence alignment by CLUSTALW, molecular phylogenetics by MEGA11, virulence and protein disorder prediction by VirulentPred and PONDR respectively, pathway analysis through Pathway Commons, protein-protein interaction analysis through STRING and per-site evolutionary rate estimation by ConSurf. The number of amino acids of the selected proteins ranged from 279 to 336. These proteins were slightly acidic to basic in nature, thermally stable and hydrophobic so that they would reside in and interact with biological membranes. Polynucleobacter necessarius was the ancestor of all the selected organisms, and the related organisms were more or less clustered together. Thus, they might share common pathogenic strategies. The selected proteins were non-virulent. Overall percentage of disordered region ranged from 18.53 to 43.69, which provides functional flexibility as they can assemble linkers and macromolecular complexes to attach with host cell receptors. def, Pnec_1775, fmt, Pnec_1774, Pnec_1773, Pec_1772, ftsH, Pnec_1779, Pnec_1611 and grpE were the functional partners of htpX. Nineteen residues were conserved & exposed. Thirty-eight residues were conserved & buried. This study revealed the mechanism of action of the concerned protein, evolutionary relatedness among organisms, pathways involved and extent of conserved residues. The results from this investigation could be used in the development of effective therapeutic strategies.