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).
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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 |
---|
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