C5EBC7 · C5EBC7_BIFLI
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids697 (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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 257-264 | ATP (UniProtKB | ChEBI) | |||
Binding site | 479 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 480 | ||||
Binding site | 483 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 555 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent zinc metalloprotease FtsH
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionC5EBC7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 53-71 | Helical | |||
Transmembrane | 166-185 | Helical | |||
Keywords
- Cellular component
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-45 | Disordered | |||
Domain | 249-388 | AAA+ ATPase | |||
Region | 667-697 | Disordered | |||
Compositional bias | 670-697 | Basic and acidic residues | |||
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
- Length697
- Mass (Da)76,050
- Last updated2009-07-28 v1
- Checksum3F4C8271C9F77938
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 670-697 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS990240 EMBL· GenBank· DDBJ | EEQ55321.1 EMBL· GenBank· DDBJ | Genomic DNA |