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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).

Accession Number:P0AAI3
Protein Name:ATP-dependent zinc metalloprotease FtsH
Length:644
Molecular Weight:70708.00
Species:Escherichia coli (strain K12) [83333]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate

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Structure:
1LV7   4V0B     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNNDQVREAR INGREINVTK 
61:	KDSNRYTTYI PVQDPKLLDN LLTKNVKVVG EPPEEPSLLA SIFISWFPML LLIGVWIFFM 
121:	RQMQGGGGKG AMSFGKSKAR MLTEDQIKTT FADVAGCDEA KEEVAELVEY LREPSRFQKL 
181:	GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA 
241:	KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP 
301:	DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL APDIDAAIIA RGTPGFSGAD 
361:	LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI 
421:	IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY 
481:	GPEHVSTGAS NDIKVATNLA RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE 
541:	TARIIDQEVK ALIERNYNRA RQLLTDNMDI LHAMKDALMK YETIDAPQID DLMARRDVRP 
601:	PAGWEEPGAS NNSGDNGSPK APRPVDEPRT PNPGNTMSEQ LGDK