In Silico Characterization of Hypothetical Protein AZJ53₁0480 in Streptococcus pneumoniae

Background. Streptococcus pneumoniae is a major human pathogen responsible for serious infections such as pneumonia. Despite extensive research, many proteins in S. pneumoniae, including hypothetical proteins, remain uncharacterized, limiting the understanding of the bacterium's pathogenic mechanisms. Methods. This study utilizes in silico tools to characterize the hypothetical protein AZJ53₁0480 from S. pneumoniae. Sequence alignment and phylogenetic analysis were conducted using BLASTp and ClustalW, while PSIPRED and I-TASSER predicted the protein’s secondary and tertiary structures. Molecular docking studies were performed with AutoDock Vina to assess potential interactions with the antiviral drug sofosbuvir Results. The in silico analysis revealed that the hypothetical protein AZJ53₁0480 shares structural and functional similarities with viral capsid proteins of the hepatitis C virus. The protein was found to have a mixed localization, suggesting potential multifunctionality within the bacterial cell. Molecular docking studies indicated a strong binding affinity between AZJ53₁0480 and sofosbuvir, suggesting that this protein could be a potential target for therapeutic intervention. Conclusion. This study highlights structural properties and functional roles of hypothetical protein AZJ53₁0480 in S. pneumoniae of. The findings suggest that AZJ53₁0480 may play a role in the pathogenicity of this bacterium and could serve as a novel target for therapeutic development. Further experimental studies are needed to validate these findings and explore the protein's potential as a drug target. Highlights In silico analysis reveals structural similarities between the hypothetical protein AZJ53₁0480 and viral capsid proteins. Docking studies suggest AZJ53₁0480 as a potential target for antiviral drugs like sofosbuvir. The study provides new insights into the possible pathogenic role of hypothetical proteins in Streptococcus pneumoniae.