In silico Characterization of Biofilm-Associated Protein (Bap) Identified in a Multi-drug Resistant Acinetobacter baumannii Clinical Isolate

dihedral angles, including the phi (φ) and psi (ψ) and backbone conformation using the PROCHECK module of the PDB Sum server was performed. The domains and key amino acids involved in protein structure were studied by the Pfam and Interpro softwares. Results: Analysis of the amino acid content of the Bap protein revealed the absence of Arg and Cys in the protein structure. Our Bap protein exhibited ~99.6% identity with other Bap sequences in the GenBank database. Stereochemical simulation identified 19 antiparallel β-sheets with two small α-helices. The N-terminal of Bap protein formed oligomers that mediate cellular adhesion. Conclusion: This study adds considerable information about Bap protein 3D structure, its conformation, domain analysis, and amino acids involved in cellular attachment.