A0A9D2KMR3 · A0A9D2KMR3_9BACT
- ProteinLon protease
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids925 (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.
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 > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Mailhella
Accessions
- Primary accessionA0A9D2KMR3
Proteomes
Subcellular Location
Expression
Induction
By heat shock.
Interaction
Subunit
Homohexamer. Organized in a ring with a central cavity.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-110 | Disordered | ||||
Sequence: MTDAAFLPDGGLSEPSLAVSGPSYKDPAEGRLDASFDDAIPLPAADVPAPESPDGEVEENESGEGERSDDGSEANDTPEERDMPNRPRRRRIRRPSAVTVTPERPGGADN | ||||||
Compositional bias | 52-66 | Acidic residues | ||||
Sequence: SPDGEVEENESGEGE | ||||||
Compositional bias | 67-86 | Basic and acidic residues | ||||
Sequence: RSDDGSEANDTPEERDMPNR | ||||||
Domain | 122-317 | Lon N-terminal | ||||
Sequence: LPVVPLRDSVVFNSMIVPLYEGREKSILAVDTALGSNRFLLLCTQKDASVDDPGPGDLYEVGSVVMILRMLKMPDGQVKILVQGLARAQIKSFVATEPFLAARMELLQEKEAGPRDVRQEALIRSAREQSEKILNLRGIPTGDIMGVLMAVDDPGRLADLIAANMRLRVTDAQALLESLDPVERLQMVNDHLSREV | ||||||
Region | 354-385 | Disordered | ||||
Sequence: LGDNADQEEELEELTKSLDKAGLPSDARKEAD | ||||||
Domain | 705-886 | Lon proteolytic | ||||
Sequence: ALMPGVALGLAWTQAGGEVLHVEVTTMKGKGHLTLTGQLGDVMKESAQAAMSYARSHAGELGLDPDFTDKVDIHVHVPAGATPKDGPSAGVTLVTALVSALTCRPARNDTCMTGEITLRGRVLPVGGIKEKILGAVARGLEHAVIPSQNVKDLEDIPADLRRKIDIKSVDSIDQLLPLVLTP | ||||||
Region | 890-925 | Disordered | ||||
Sequence: DTCKRPAPAKKGRTSSVKEQPAKPGAKRPGRAAAAR |
Sequence similarities
Belongs to the peptidase S16 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length925
- Mass (Da)101,040
- Last updated2023-05-03 v1
- Checksum8C5B2FF9860C9E17
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-66 | Acidic residues | ||||
Sequence: SPDGEVEENESGEGE | ||||||
Compositional bias | 67-86 | Basic and acidic residues | ||||
Sequence: RSDDGSEANDTPEERDMPNR |