A0A2U2EB27 · A0A2U2EB27_MYCAV
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids799 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- Strains
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)
Accessions
- Primary accessionA0A2U2EB27
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 | ||||
Sequence: IRTITAIAVVVLLGWSFFYF | ||||||
Transmembrane | 115-132 | Helical | ||||
Sequence: LLVYVLPLLLLVGLFVMF |
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 | ||||
Sequence: IPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFDQAKQNNPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFDPRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPD | ||||||
Region | 616-649 | Disordered | ||||
Sequence: DFGGRIPSDKPPIKTPGELAIERGEPWPPPAPEP | ||||||
Region | 671-799 | Disordered | ||||
Sequence: RNANGGNGSHANQGGNRQGPTQPDYGAPAGWRAPGWPPQQSQQPNYWHPPAQPPYWQQPAHGYPGQQPYPGQQPYPGQPGGPAQSGPPQARPPYPPYPPYPPPGQPAPEGGSPDRQDDDVSRSNPPAHG | ||||||
Compositional bias | 675-690 | Polar residues | ||||
Sequence: GGNGSHANQGGNRQGP | ||||||
Compositional bias | 713-727 | Pro residues | ||||
Sequence: QPNYWHPPAQPPYWQ | ||||||
Compositional bias | 739-779 | Pro residues | ||||
Sequence: YPGQQPYPGQPGGPAQSGPPQARPPYPPYPPYPPPGQPAPE | ||||||
Compositional bias | 782-799 | Basic and acidic residues | ||||
Sequence: SPDRQDDDVSRSNPPAHG |
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
- Length799
- Mass (Da)86,097
- Last updated2018-09-12 v1
- ChecksumE45992FA832ACBF4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 675-690 | Polar residues | ||||
Sequence: GGNGSHANQGGNRQGP | ||||||
Compositional bias | 713-727 | Pro residues | ||||
Sequence: QPNYWHPPAQPPYWQ | ||||||
Compositional bias | 739-779 | Pro residues | ||||
Sequence: YPGQQPYPGQPGGPAQSGPPQARPPYPPYPPYPPPGQPAPE | ||||||
Compositional bias | 782-799 | Basic and acidic residues | ||||
Sequence: SPDRQDDDVSRSNPPAHG |