Bacterial endophytes are a promising source of novel fibrinolytic enzymes with unique metabolic pathways and desirable characteristics that may not be present from conventionally explored sources. This study aimed to characterize fibrinolytic enzymes from selected endophytic bacteria isolated from papaya (Carica papaya L.) leaves and the genes encoding the enzymes. A strain BFP1 (InaCC-B1657) that showed the highest fibrinolytic activity was identified as Bacillus cereus based on the phylogenetic analysis of the 16S rRNA sequence. The enzyme exhibited optimum activity at 50°C and pH 7.0, and remained stable until 80°C and pH 6 - 10 for 24 h. The assay of metal ions and inhibitors on the fibrinolytic enzyme activity found that adding Cu2+ stimulated, while Fe2+ reduced the activity. PMSF and TPCK inhibited the enzyme activity, while adding EDTA and EGTA increased the activity. These suggest that the fibrinolytic enzymes belong to the serine protease group. Of the 21 proteases/peptidases determined from the 5,257,484 base pairs (bp) genome, minor extracellular protease Vpr and S8 family peptidase genes were found related to the fibrinolytic enzyme activity. The Vpr gene has a molecular weight of 98.5 kDa. The subtilase domain (peptidase S8 family) and the catalytic triad subtilase active sites (Asp204, His237, and Ser531) were detected. A prediction of physicochemical characteristics of the Vpr gene showed that the enzyme is hydrophilic and exhibited alkali-halo tolerant and thermo tolerant over a broad range of temperatures.