Chlamydial protease-like activity factor (CPAF) is a Chlamydia trachomatis protease, which activity results in dampened host inflammation signaling, cytoskeletal remodeling, and suppressed neutrophil activation. We used series of bioin-formatics to analyze and predict CPAF protein, physicochemical properties and hydrophobicity, signal peptide, subcellular local-ization, transmembrane protein structure, conserved region and N-glycosylation sites and phosphorylation sites, the secondary and tertiary structure, ligand-binding regions and small molecular compounds, B-/T-cell epitopes and the interacting proteins. CPAF, which consist of 601 amino acids, the relative molecular weight is 67 252.57 Da, the theoretical isoelectric point is 5.68. The CPAF protein contains a signal peptide and has non-transmembrane regions. The conserved domain of CPAF protein is lo-