This review presents a systematization of available data on subtilisin-like serine proteinases of plants. Enzymatic and physicochemical properties of the enzymes, their structure and processing, as well as their biological functions and origin are considered. Subtilisin-like proteinases of plants have a number of substantial differences from such typical subtilisins as subtilisin BPN or subtilisin Carlsberg. The plant subtilisins are characterized by much greater molecular mass, long inserts and C-terminal regions, and several cysteine residues, while typical subtilisins have no cysteine residues, and thiol-dependent bacterial subtilisins contain only one cysteine residue required for enzymatic activity.