Clostridium perfringens, a strictly anaerobic spore-forming bacterium, is a pathogenic bacterium that causes gas gangrene and food poisoning in humans. We found that human fibronectin (Fn), one of such extracellular matrix proteins, binds to C. perfringens cells, and exhibits several fibronectin-binding proteins (Fbps) [FbpA (CPE0737), FbpB (CPE0847), FbpC (CPE0625), and FbpD (CPE0630)] in C. perfringens. These Fbps are all hypothetical proteins. In this study, we focused on FbpC (CPE0625). FbpC were predicted physiochemical characterization and functional using several server. Analyses using ExPAsy and GO term predictions via D-I-TASSER suggest that FbpC is one of a cell-wall binding protein. The results of these prediction supported our previous reports. FbpC was identified as a potential carboxypeptidase through feature-based annotation (NCBI-CD, Prosite, and InterPro), similarity-based annotation (BLASTp), and structure-similarity-based annotation (DALI and Foldseek). Moreover, it was revealed that FbpC possessed carboxypeptidase activity. In conclusion, FbpC is carboxypeptidase associated with cell wall.
