O84348 · LON_CHLTR
- ProteinLon protease
- Genelon
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids819 (go to sequence)
- Protein existenceInferred from homology
- 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 | 392-399 | ATP (UniProtKB | ChEBI) | |||
Active site | 724 | ||||
Active site | 767 | ||||
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
Names & Taxonomy
Protein names
- Recommended nameLon protease
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Chlamydiota > Chlamydiia > Chlamydiales > Chlamydiaceae > Chlamydia/Chlamydophila group > Chlamydia
Accessions
- Primary accessionO84348
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000076132 | 1-819 | Lon protease | ||
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 compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | |||
Region | 1-40 | Disordered | |||
Compositional bias | 18-38 | Basic and acidic residues | |||
Domain | 42-239 | Lon N-terminal | |||
Domain | 634-818 | Lon proteolytic | |||
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length819
- Mass (Da)91,965
- Last updated1998-11-01 v1
- ChecksumFEA7802A5441557C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | |||
Compositional bias | 18-38 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE001273 EMBL· GenBank· DDBJ | AAC67939.1 EMBL· GenBank· DDBJ | Genomic DNA |