Structural and Functional Characterization of a Putative Type VI Secretion System Protein in Cronobacter sakazakii as a Potential Therapeutic Target: A Computational Study

Despite many unknown functions of hypothetical proteins in bacterial genomes, bioinformatic techniques have successfully annotated their roles in various pathogens. Objectives: 7G strain (accession no. WP_004386962.1, 277 residues) using computational tools. Methods: Multiple bioinformatic tools were used to identify the homologous protein and to construct and validate its 3D structure. A 3D model was generated using SWISS-MODEL and validated using tools, developing a reliable 3D structure. The STRING and CASTp servers provided information on protein-protein interactions and active sites, identifying functional partners. Results: The putative protein was soluble, stable, and localized in the cytoplasmic membranes, indicating its biological activity. Functional annotation identified TagJ (HsiE1) within the protein, a member of the ImpE superfamily involved in the transport of toxins and a part of the bacterial type VI secretion system (T6SS). The 3-dimensional structure of this protein was validated through molecular docking involving 6 different compounds. Among these, ceforanide demonstrated the strongest binding scores, -7.5 kcal/mol for the hypothetical protein and -7.2 kcal/mol for its main template protein (PDB ID: 4UQX.1). Conclusion: -mediated disorders.