Yersinia pestis is an infamous gram-negative, coccobacillus enterobacterium responsible for three devastating plague pandemics worldwide. The recent outbreak of this zoonotic disease demands in silico study of the hypothetical proteins for efficient drug and vaccine discovery. As hypothetical proteins constitute a substantial portion of the proteome, it’s essential to annotate them structurally and functionally. The current study characterized physicochemical properties, predicted homology-based 3D structure and annotated functions of the hypothetical protein AVO28_00330 of Y. pestis using a range of bioinformatic tools and softwares. Swiss Model and Phyre2 server were utilized to predict the tertiary model which was minimized energetically using YASARA server. The quality assessment servers found the model as a good one. For future molecular docking analysis, active binding sites were predicted using CASTp. Protein-protein interaction analysis was performed in STRING server. For functional prediction InterPro, Pfam, Motif and other tools were used. The hypothetical protein revealed tricopeptide repeat domain and rubredoxin metal-binding domain which regulates lipopolysaccharide metabolic process in the outer cell membrane which contributes to virulence property of the protein. Therefore, this in silico analysis will improve the current understanding of the protein and aid in the future analysis regarding therapeutic drug and vaccine investigation.
Important Insight of Hypothetical Proteins from E. faecium Strain 13-022, the Drug Targeted Virulent Big-1 Adhesins: An in-silico Approach
