D3NT97 · D3NT97_AZOS1
- ProteinATP-dependent zinc metalloprotease FtsH
- GenehflB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids645 (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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent zinc metalloprotease FtsH
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Azospirillaceae > Azospirillum
Accessions
- Primary accessionD3NT97
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 104-124 | Helical | ||||
Sequence: LFSVLLSWFPMLLLIGVWIFF |
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 188-327 | AAA+ ATPase | ||||
Sequence: IPKGCLLVGPPGTGKTLTARAVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQGKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGVILIAATNRPDVLDPALLRPGRFDRQVVVPNPD | ||||||
Region | 599-645 | Disordered | ||||
Sequence: GEAIPRDEERETMAVPPRPTPGSGRRSSVPPSTGQESGGMGPEPQGT | ||||||
Compositional bias | 623-645 | Polar residues | ||||
Sequence: RRSSVPPSTGQESGGMGPEPQGT |
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
- Length645
- Mass (Da)70,176
- Last updated2010-04-20 v1
- Checksum0A37D0263DB152AE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 623-645 | Polar residues | ||||
Sequence: RRSSVPPSTGQESGGMGPEPQGT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP010946 EMBL· GenBank· DDBJ | BAI71626.1 EMBL· GenBank· DDBJ | Genomic DNA |