A0A2K2HEB3 · A0A2K2HEB3_9BACT
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids621 (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 | cell division | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- 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 > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter
Accessions
- Primary accessionA0A2K2HEB3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 7-25 | Helical | ||||
Sequence: NLALWLVISLVMILLFNMM | ||||||
Transmembrane | 100-121 | Helical | ||||
Sequence: FWFTLLVSWGPILLLIGVWIFF |
Keywords
- Cellular component
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 185-324 | AAA+ ATPase | ||||
Sequence: IPKGVLLVGAPGTGKTLLARAIAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFVQGKKQAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFESNEGVILIAATNRPDVLDPALLRPGRFDRQVVVPRPD | ||||||
Region | 588-621 | Disordered | ||||
Sequence: LKDLVFPAEQTPADRDSDRRAVPENAPEADPPES | ||||||
Compositional bias | 599-613 | Basic and acidic residues | ||||
Sequence: PADRDSDRRAVPENA |
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
- Length621
- Mass (Da)68,494
- Last updated2018-03-28 v1
- Checksum54AC099BACDFE11E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 599-613 | Basic and acidic residues | ||||
Sequence: PADRDSDRRAVPENA |