3.A.29.1.5
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).