3.A.29.1.8
ATP-dependent zinc metalloprotease, FtsH, of 639 aas and 2 TMSs (N-terminal at residues 30 and 130. The structure of this ATP-dependent metalloprotease in its functionally relevant hexameric form has been determined (Brangulis et al. 2023). ATP-dependent FtsH proteases are conserved in bacteria, mitochondria, and chloroplasts, where they play essential roles in the degradation of misfolded/unneeded membrane and cytosolic proteins. It is crucial for mouse and tick infectivity and in vitro growth of the Lyme disease-causing agent Borrelia burgdorferi. It is functionally active, possessing both protease and ATPase activities (Brangulis et al. 2023).
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| Accession Number: | B7J0N5 |
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| Protein Name: | ATP-dependent zinc metalloprotease FtsH |
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| Length: | 639 |
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| Molecular Weight: | 70802.00 |
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| Species: | Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi) [445985] |
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| Number of TMSs: | 2 |
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| Location1 / Topology2 / Orientation3: |
Cell inner membrane1 / Multi-pass membrane protein2 / Cytoplasmic side3 |
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| Substrate |
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1: MNGNNNMNNN GKSNNKKKNK NWILGLVVVF LISAIFMSYF IRGGESYKNV PYSTFQSYLD
61: NGLVESVVII DKNLIQFVVK GSNFAKSYFS TSIPYLDINL LSELKNKKVE LSSGKSQASL
121: IGVLLQTLPW ILFFIFFFFI FRQTQGGGGK VFTFGKSNAQ KYEAGKNKIT FKDVAGQEEV
181: KQELREVVEF LKNPKKFEKI GAKIPKGVLL VGSPGTGKTL LAKAVAGEAG VSFFHMSGSD
241: FVEMFVGVGA SRVRDLFDNA RKNSPCIIFI DELDAVGRSR GAGLGGGHDE REQTLNQLLV
301: EMDGFGTHTN VIVMAATNRP DVLDSALLRP GRFDRQVTVS LPDIKEREAI LNIHSLKTKL
361: SKDINLQVIA RATPGASGAD LANLINEGAL IAARNNQDEI LMKDMEEARD KILMGVAKKS
421: MTITDRQKLE TAYHEAGHAL LHYYLEHADP LHKVTIIPRG RALGVAFSLP REDRLSINKH
481: QILDKIKICY GGYASEQINL GVTTAGVQND LMQATSLAKK MVTEWGMGEE VGPIFLVDDE
541: APIFLPKEFS KAKAYSENTA DKVDREVKRI LEECLKEASD ILLKHKDQLV KLAKELVLKE
601: TLTDKEVREL LGFEANKDEY DLFSSDSTTK EVKGEDVKG