Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (PubMed:24843043, PubMed:24821790, PubMed:28906250, PubMed:30858337, PubMed:31445887, PubMed:28712723). Specifically recognizes and binds exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane proteins (PubMed:30858337). Acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (PubMed:24843043, PubMed:24821790, PubMed:28906250, PubMed:30858337, PubMed:32541053, PubMed:28712723). Able to unfold protein substrates by processive threading through its central pore (PubMed:32541053). Once extracted from the mitochondrion outer membrane, substrate proteins are then transferred to the endoplasmic reticulum, where they are ubiquitinated and degraded by the proteasome (PubMed:31445887). Also mediates extraction of excess tail-anchored proteins from the peroxisomal membrane (PubMed:28906250). In normal conditions, MSP1 translocase activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of excess tail-anchored proteins (PubMed:28906250). [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate Interaction with PEX3 inhibits the translocase activity by preventing unfolding of target proteins. Homohexamer; in presence of ATP (PubMed:30858337, PubMed:32541053, PubMed:28712723). Interacts with PEX3; leading to inhibit the translocase activity (PubMed:28906250, PubMed:32541053). Impaired transmembrane tail-anchored protein localization, characterized by mislocalization of PEX15 to the mitochondrion outer membrane. Present with 3530 molecules/cell in log phase SD medium. Belongs to the AAA ATPase family. MSP1 subfamily.