A0A2V4HYF9 · A0A2V4HYF9_9PSED
- ProteinATP-dependent zinc metalloprotease FtsH
- GenehflB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids634 (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 > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A2V4HYF9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 98-120 | Helical | ||||
Sequence: IWTQLLVASFPILVIIAVFMFFM |
Keywords
- Cellular component
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 186-325 | AAA+ ATPase | ||||
Sequence: IPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKHAPCIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPD | ||||||
Compositional bias | 594-617 | Basic and acidic residues | ||||
Sequence: DIMAGRTPREPRDWDDDKDSGTPA | ||||||
Region | 594-634 | Disordered | ||||
Sequence: DIMAGRTPREPRDWDDDKDSGTPAAQNDRPESPIGGPAAQH |
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
- Length634
- Mass (Da)69,280
- Last updated2018-09-12 v1
- ChecksumF7EEAD7A3AC488FD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 594-617 | Basic and acidic residues | ||||
Sequence: DIMAGRTPREPRDWDDDKDSGTPA |