A0A1A2PG84 · A0A1A2PG84_9MYCO
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids785 (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 | 203-210 | ATP (UniProtKB | ChEBI) | |||
Binding site | 425 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 426 | ||||
Binding site | 429 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 501 | 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 | 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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0A1A2PG84
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 7-26 | Helical | |||
Transmembrane | 115-132 | Helical | |||
Keywords
- Cellular component
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 195-334 | AAA+ ATPase | |||
Region | 662-785 | Disordered | |||
Compositional bias | 672-686 | Polar residues | |||
Compositional bias | 705-720 | Pro residues | |||
Compositional bias | 743-764 | Pro residues | |||
Compositional bias | 768-785 | 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
Family and domain databases
Sequence
- Sequence statusComplete
- Length785
- Mass (Da)84,970
- Last updated2016-10-05 v1
- MD5 Checksum99BCCF1A1338F36E3E1CC9078F730C10
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 672-686 | Polar residues | |||
Compositional bias | 705-720 | Pro residues | |||
Compositional bias | 743-764 | Pro residues | |||
Compositional bias | 768-785 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LZJL01000104 EMBL· GenBank· DDBJ | OBH26300.1 EMBL· GenBank· DDBJ | Genomic DNA |