Trypsin-like serine endopeptidase involved in the processing of glyoxysomal higher molecular weight precursor. The dimeric form carries out the specific cleavages needed to remove PTS2-containing presequences, whereas the monomeric form degrades the removed presequences and misfolded proteins (Probable). Not required for degradation of glyoxylate cycle enzymes during seedling development. Inhibited by N-methylmaleimide (NEM), but not by E64, benzamidine, aprotinin, leupeptin, pefabloc, pepstatin A, EGTA, EDTA and 1,10-phenanthroline. Monomer and homodimer. Multimerization requires calcium ions (By similarity). No visible phenotype, but loss of processing of glyoxysomal precursor proteins. Increased resistance to the herbicide precursor 4-(2,4-dichlorophenoxy) butyric acid (2,4-DB) and to the inhibitory effects of indole-3-butyric acid (IBA) on root elongation. Belongs to the peptidase S1B family.