In silico characterization and functional prediction of MBO_200107: an uncharacterized protein of Mycobacterium tuberculosis variant caprae

Mycobacterium tuberculosis variant caprae is an acid-fast bacterium, a member of the Mycobacterium tuberculosis complex (MTC). In this ‘in silico’ study, we have characterized the MBO_200107 protein of M. tuberculosis variant caprae stored in the National Center for Biotechnology Information (NCBI) database as an uncharacterized protein. We have determined the physicochemical properties, functions, secondary and tertiary structure, active and binding site, and subcellular localization of the protein, applying several bioinformatics tools. The protein was made of a 354 amino acid long chain and had a molecular weight of 39089.37 Da. Moreover, the protein was found alkaline and having an isoelectric point (pI) of 9.62. The secondary and tertiary structure implied that the protein was well stable. Besides, there was no binding site has been found in this protein. In terms of functional characteristics, the protein had two functional domains, the Gammaglutamylcyclotransferase (GGCT) and the YjqB, though no protein motif has been found. The literature search revealed that the upregulation of GGCT is implicated in several cancers, including lung, breast, prostate, ovarian, cervical, urinary bladder, and colon cancers. We hypothesized that the protein could contribute to cancer research as it has GGCT like domain and recommend further analysis.