Structural and Functional Elucidation of IF-3 Protein of Chloroflexus aurantiacus Involved in Protein Biosynthesis: An In-Silico Approach

Chloroflexus aurantiacus is a thermophilic bacterium that produces a multitude of proteinswithin its genome. Bioinformatics strategies can facilitate comprehending this organism throughfunctional and structural interpretation assessments.This study aimed to allocate the structure andfunction through an in-silico approach required for bacterial protein biosynthesis. This in-silicoviewpoint provides copious properties, including the physicochemical properties, subcellular location,three-dimensional structure, protein-protein interactions, and functional elucidation of the protein(WP_012256288.1). The STRING program is utilized for the explication of protein-proteininteractions. The in-silico investigation documented the protein's hydrophilic nature withpredominantly alpha (α) helices in its secondary structure.The tertiary-structure model of the proteinhas been shown to exhibit reasonably high consistency based on various quality assessmentmethods.The functional interpretation suggested that the protein can act as a translation initiationfactor, a protein required for translation and protein biosynthesis. Protein-protein interactions alsodemonstrated high credence that the protein interconnected with 30S ribosomal subunit involved inprotein synthesis. This study is bioinformatically examined that the protein (WP_012256288.1) isaffiliated in protein biosynthesis as a translation initiation factor IF-3 of C. aurantiacus.