A0A517PMS3 · A0A517PMS3_9PLAN
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH_1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids664 (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 > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia
Accessions
- Primary accessionA0A517PMS3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 32-50 | Helical | ||||
Sequence: TGPWLIILLILVIGSLMMM | ||||||
Transmembrane | 144-166 | Helical | ||||
Sequence: IGTYILPWLIGPLLIIGFFWFML |
Keywords
- Cellular component
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MASPQENPQRTPPPGKDPQKPSSKETQGAPS | ||||||
Domain | 231-370 | AAA+ ATPase | ||||
Sequence: IPKGVLLMGSPGTGKTLLARATAGEAGVPFYSINGSEFIQMFVGVGASRVRDLFRNAKENAPCIIFVDEIDAVGRIRGAGLGGGHDEREQTLNQMLSEMDGFQQNEAVIVIAATNRPDVLDPALLRPGRFDRHITVDRPT | ||||||
Region | 644-664 | Disordered | ||||
Sequence: QANLDNAKQAGTDTENEQPPE | ||||||
Compositional bias | 645-664 | Polar residues | ||||
Sequence: ANLDNAKQAGTDTENEQPPE |
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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length664
- Mass (Da)73,132
- Last updated2019-10-16 v1
- Checksum4B60F52E6C1EA011
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 645-664 | Polar residues | ||||
Sequence: ANLDNAKQAGTDTENEQPPE |