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3.A.29.1.7
ATP-dependent zinc metalloprotease, FtsH, of 610 aas and 2 TMSs. It acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins, and it plays a role in the quality control of integral membrane proteins.The cryo-EM structure in a fully ADP-bound symmetric state has been solved (Liu et al. 2022). Comparisons of the ADP-state structure with its apo-state and a substrate-engaged yeast YME1 structure show conformational changes in the ATPase domains, rather than the protease domains. A reconstruction of the full-length TmFtsH provides structural insights for the dynamic transmembrane and the periplasmic domains. The structural analyses expand the understanding of conformational switches between different nucleotide states in ATP hydrolysis by FtsH (Liu et al. 2022).

Accession Number:Q9WZ49
Protein Name:ATP-dependent zinc metalloprotease FtsH
Length:610
Molecular Weight:68099.00
Species:Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) [243274]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2 / Cytoplasmic side3
Substrate protein

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FASTA formatted sequence
1:	MNRSNIWNLL FTILIIVTLF WLARFFYVEN SPVSKLSYTS FVQMVEDERS VVSEVVIRDD 
61:	GVLRVYTKDG RVYEVDAPWA VNDSQLIEKL VSKGIKVSGE RSGSSSFWIN VLGTLIPTIL 
121:	FIVVWLFIMR SLSGRNNQAF TFTKSRATMY KPSGNKRVTF KDVGGAEEAI EELKEVVEFL 
181:	KDPSKFNRIG ARMPKGILLV GPPGTGKTLL ARAVAGEANV PFFHISGSDF VELFVGVGAA 
241:	RVRDLFAQAK AHAPCIVFID EIDAVGRHRG AGLGGGHDER EQTLNQLLVE MDGFDSKEGI 
301:	IVMAATNRPD ILDPALLRPG RFDKKIVVDP PDMLGRKKIL EIHTRNKPLA EDVNLEIIAK 
361:	RTPGFVGADL ENLVNEAALL AAREGRDKIT MKDFEEAIDR VIAGPARKSK LISPKEKRII 
421:	AYHEAGHAVV STVVPNGEPV HRISIIPRGY KALGYTLHLP EEDKYLVSRN ELLDKLTALL 
481:	GGRAAEEVVF GDVTSGAAND IERATEIARN MVCQLGMSEE LGPLAWGKEE QEVFLGKEIT 
541:	RLRNYSEEVA SKIDEEVKKI VTNCYERAKE IIRKYRKQLD NIVEILLEKE TIEGDELRRI 
601:	LSEEFEKVVE