Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity). Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity (By similarity). [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) The N-terminal region consists of two globular folded domains that contain prolyl isomerase and chaperone activities. The C-terminal region binds nickel ions. Belongs to the FKBP-type PPIase family.