TB is caused by an infection of MTB, the foremost cause of mortality attributable to a single infectious agent, resulting in numerous fatalities globally. The pathogen often resides in the human body in a dormant state. Because of how common tuberculosis is, scientists need to find new ways to treat it and make anti-tuberculosis vaccines that can handle multidrug resistance and latent TB infections. This study aims to examine the MTB protein sequence, gaining knowledge about its physicochemical properties, structure-based functional analyses, domain anticipation for specific functional predictions, 2D and 3D structures, and the PPI network. The physicochemical parameters indicated that the protein contains a greater number of negatively charged residues compared to positively charged residues in its sequence. The instability index and aliphatic index indicate that this protein is stable and has suitable thermostability. Documentation also confirms the hydrophobic nature of this protein. The protein has a sensor histidine kinase domain that helps phosphorylate a histidine residue and move its phosphate group to HssR. Consequently, this protein can function as an enzyme, engaging in interactions with ATP and protein L-histidine to produce ADP and protein N-phospho-L-histidine. Gene ontology analyses have revealed the protein interactions in cellular, molecular, and biological processes. The PPI network established an interaction network between the selected protein and 10 other proteins. The secondary structural assessment documented that the alpha helix was the most dominant structural element, followed by random coils and extended strands. Moreover, three different programs, namely AlphaFold, I-TASSER, and SWISS-MODEL, modeled the 3D structure of the protein. After studying different structures, the structural assessment study showed that the one predicted by the SWISS-MODEL program was the best one, taking into account the values for the most desired and extra-allowed areas in the plot statistics results.