Signal peptidases are vital enzymes in the protein secretion pathway. In Archaea, type I signal peptidase, responsible for the cleavage of secretory signal peptides from the majority of secreted proteins, and prepilin peptidase-like signal peptidase, responsible for processing signal peptides from prepilin-like proteins like the preflagellins and various sugar-binding proteins, have been identified. In addition, the archaeal signal peptide peptidase, responsible for degradation of signal peptides after their removal from precursor proteins, has been characterized. These enzymes seem to have a mosaic of eukaryal and bacterial characteristics, and also possess unique archaeal traits. In this review, the most current knowledge with regard to these enzymes is summarized, including their cellular function, catalytic mechanism and distribution and conservation among archaeal species. Comparisons are drawn of these enzymes to their bacterial and eukaryal counterparts, and unique archaeal features highlighted.