Splits dipeptides with a prolyl in the C-terminal position and a nonpolar amino acid at the N-terminal position. Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. Binds 2 cobalt ions per subunit. Co(2+) can be replaced by Mn(2+), resulting in a 25% decrease in activity, but not by Mg(2+), Ca(2+), Fe(2+), Zn(2+), Cu(2+), or Ni(2+). Optimum pH is 7.0. Optimum temperature is 100 degrees Celsius. Highly thermostable. Homodimer. Cobalt 1 is the tight-binding and cobalt 2 is the loose-binding metal center. Belongs to the peptidase M24B family. Archaeal-type prolidase subfamily.