Acinetobacter baumannii, an opportunistic human pathogen, targets critically ill patients as its primary target. A. baumannii, which was previously considered benign, is now recognized as a global hazard in the healthcare context. Its propensity to acquire multidrug, extensive drug, and even pan-drug resistance phenotypes at previously unanticipated rates is the primary reason for this. The objective of this investigation was to characterize the physicochemical properties, functional annotation, structure anticipation with active site determination, and antigenicity of the selected uncharacterized protein of A. baumannii. The protein's acidic nature was indicated by its putative pI (4.43), while its hydrophilicity was indicated by its GRAVY (-0.404). The functional annotation indicated that the protein was involved in catalytic reactions that led to the synthesis of L-asparaginyl-tRNA (Asn) and L-glutaminyl-tRNA (Gln). The protein was linked to both molecular functions and biological processes, as evidenced by the GO analyses. The protein's involvement with ten additional proteins was also demonstrated by the PPI network. The structural analyses demonstrated that nearly 50% of the residues were involved in the formation of an alpha-helix, while nearly 46.15% were involved in the formation of a random coil. The Swiss Model was found to be the most appropriate model for the uncharacterized protein in the 3D structural comparison. Furthermore, we quantified the active site's volume (4235.245 ų) and surface area (896.977 Ų). The protein was identified as non-antigenic. In order to verify the results of this investigation, an experimental investigation should be implemented.