F4QQY2 · F4QQY2_9CAUL
- ProteinLon protease
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids798 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 352-359 | ATP (UniProtKB | ChEBI) | |||
Active site | 674 | ||||
Active site | 717 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | cellular response to heat | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLon protease
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Asticcacaulis
Accessions
- Primary accessionF4QQY2
Proteomes
Subcellular Location
Expression
Induction
By heat shock.
Interaction
Subunit
Homohexamer. Organized in a ring with a central cavity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-200 | Lon N-terminal | |||
Coiled coil | 203-253 | ||||
Domain | 587-768 | Lon proteolytic | |||
Sequence similarities
Belongs to the peptidase S16 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length798
- Mass (Da)88,156
- Last updated2011-06-28 v1
- ChecksumFE4E2DD97C26BCD8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL883079 EMBL· GenBank· DDBJ | EGF90619.1 EMBL· GenBank· DDBJ | Genomic DNA |