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The mitochondrial i-AAA protease complex involved in inner membrane insertion and turnover.  It consists of Yta10, Yta11 and Yta12 (Lee et al. 2017).

Protease complex of Saccharomyces cerevisiae
Yta10, Afg3 of 761 aas with 2 TMSs
Yta11, Yme1, Osd1, of 747 aas and 2 TMSs
Yta12, RCA1, of 825 aas

Mitochondrial AAA protease complex of two enzymes, Yta10/12 (Afg3-like or Spg-7) and Yta11 (Ymel-1). It is a mitochondrial ATP-dependent metalloprotease complex mediating degradation of non-assembled mitochondrial inner membrane proteins and necessary for the assembly of the mitochondrial respiratory chain and ATPase complexes. It functions both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides (Nargund et al. 2012, Pellegrino et al. 2014, Nargund et al. 2015).

Protease complex of Caenorhabditis elegans
Spg-7 (Ata10/12), 782 aas and 2 TMSs
Yme1 (Ata11; Ymel-1), 723 aas and 1 TMS

Uncharacterized protein of 960 aas and 6 - 9 TMSs in a 2 + 4 + 3 TMS arrangement.  The last 3 peaks of hydrophobicity are small and may not be TMSs.  The large hydrophiic C-terminal domain is homologous to the proteases of this family.  The first six strongly hydrophobic TMSs are not part of this protease domain. This region is homologous to a part (residues 2220 - 2380) of the Orf1a polyprotein (YP_009725295) of the SARS coronavirus.

Candidatus Spechtbacteria
UP of Candidatus Spechtbacteria bacterium

FtsH zinc metaloprotease of 634 aas and 2 TMSs.  3-d structures have been determined (Uthoff and Baumann 2018). The active FtsH is a dodecamer, which consists of two FtsH hexamers. A tilted conformation of the cytosolic domain in the FtsH dodecamer, visualized by negative stain TEM suggests a lateral substrate entrance between the membrane and cytosolic domains. Such a substrate path was resolved in the cryo-EM structure of the FtsH hexamer (Carvalho et al. 2020).

FtsH of Aquifex aeolicus

ATP-dependent zinc metaloprotease, FtsH of 644 aas and 2 TMSs. Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It plays a role in the quality control of integral membrane proteins and degrades a few membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA. It also degrades cytoplasmic proteins, sigma-32, LpxC, KdtA and the phage lambda cII protein among others. Membrane proteins are digested in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, in a process that probably requires ATP (Bittner et al. 2017).

FtsH of E. coli

FtsH cell division protease of 637 aas and 2 N-terminal TMSs.

Candidatus Peregrinibacteria
FtsH of Candidatus Peribacter riflensis