First report of an insilico study of Luciferase in Mycobacterium sp. EPa45

Mycobacterium are a genus of Actinobacteria known to be responsible for several deadly diseases in both humans and animals, including tuberculosis. Luciferase is the primary protein in Mycobacteria that plays a role in bioluminescence. It also plays a role in some bacteria of being a source of energy transference, such as in the case of lumazine proteins. Although studies have been conducted in different luciferase in bacteria, there has been hardly any structural studies on luciferase expressed in Mycobacterium sp. EPa45. Therefore, in this paper we have studied luciferase expressed in Mycobacterium sp. EPa45 by insilico analysis of its structure from its protein sequence. We report the observed differences within luciferase reported from other strains of mycobacterium and pathogenic and non-pathogenic forms of bacteria in terms of their (i) physiochemical characteristics, (ii) protein structure, (iii) multiple sequence alignment and (iv) phylogenetic relationships. We report for the first time the relation of this specific strain of Luciferase in mycobacterium and bacterium at large. HighlightsO_LIMycobacterium sp. EPa45 shows similar characteristics to pathogenic mycobacterium C_LIO_LIAnalysis of Luciferase sequence and protein qualities provides insight to pathogenicity C_LIO_LIThe deadly nature of infectious mycobacterium, especially with luciferase sequences similar to Mycobacterium sp. EPa45, is analyzed C_LI