A0A7T5UID9 · A0A7T5UID9_9BACT
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids631 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent zinc metalloprotease FtsH
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bdellovibrionota > Bdellovibrionia > Bdellovibrionales > Pseudobdellovibrionaceae > Micavibrio
Accessions
- Primary accessionA0A7T5UID9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 97-119 | Helical | ||||
Sequence: ISALGIFLSWFPMLLLIGVWIFF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MFWMAIGILLMFLFNVFQG | ||||||
Chain | PRO_5032337133 | 20-631 | ATP-dependent zinc metalloprotease FtsH | |||
Sequence: TQTQKPGAGEMMAYSDFMAEAAGGRISDITIKGQDVTGHYTGTGKEFSVLVPDNENVVERLSGTGVRITAEPQDPEKISALGIFLSWFPMLLLIGVWIFFMRQMQSKGGGGALGFGKSRARMLTEANGRVTFEDVAGIEEAKVELQEIVEFLKDPQKFQRLGGKIPRGALLVGSPGTGKTLIARAVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGVIILAATNRPDVLDPALLRPGRFDRQIVVPLPDVKGREKILQVHMKKVPLAKNVEPLVIARGTPGFSGADLANLVNEAALLAARRNKRVVGMEDFEEAKDKVMMGAERKSMVMSDNEKKLTAYHEAGHAVVAVHLEESDPVHKATIIPRGRALGMVMRLPEGDRVSMTRAKLKADLAVAMGGRLAEEIIFGYDKVTTGASSDISMATNMARRMVTEWGMSDKLGPLRYVSDQEEVFLGHSVTQSKNMSDETAKLVDAEVRVIVDEAYNKARDILTTYIDQLHNLAKALLEYETLTGDEIRGLLRGEPIIRVDDRLGSEDSKPKSSVPKTGGLGGGEVPQGV |
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 184-323 | AAA+ ATPase | ||||
Sequence: IPRGALLVGSPGTGKTLIARAVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGVIILAATNRPDVLDPALLRPGRFDRQIVVPLPD | ||||||
Region | 603-631 | Disordered | ||||
Sequence: DRLGSEDSKPKSSVPKTGGLGGGEVPQGV |
Sequence similarities
Belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length631
- Mass (Da)68,606
- Last updated2021-09-29 v1
- ChecksumC2260A9D37B04FB7