A0A4D7DKG7 · A0A4D7DKG7_9HYPH
- ProteinLon protease
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids805 (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
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Agrobacterium
Accessions
- Primary accessionA0A4D7DKG7
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 | 13-206 | Lon N-terminal | ||||
Sequence: YPVLPLRDIVVFPHMIVPLFVGREKSIRALEEVMGSDRQIMLVTQINASDDDPDPSAIHKVGTVANVLQLLKLPDGTVKVLVEGKGRAKIDEYTGREDFYEATAVLLDEPAEDPVEIEALSRSVVSEFESYVKLNKKISPEVVGAAGQIDDYSKLADTVASHLSIKITEKQEMLETVSVKQRLEKALGFMEGEI | ||||||
Coiled coil | 192-229 | |||||
Sequence: KQRLEKALGFMEGEISVLQVEKRIRSRVKRQMEKTQRE | ||||||
Coiled coil | 253-283 | |||||
Sequence: MAELEERIAKTKLSKEAKEKAEAEMKKLRQM | ||||||
Domain | 593-774 | Lon proteolytic | ||||
Sequence: EDQVGVVTGLAWTEVGGELLTIEGVMMPGKGRMTVTGNLKDVMKESISAAASYVRSRAVDFGIEPPRFDKSDIHVHVPEGATPKDGPSAGVAMATAIVSIMTGIPVSKDVAMTGEITLRGRVLPIGGLKEKLLAALRGGIKKVLIPEENAKDLADIPDNVKNEMEIIPVSRMGEVLQHALTR |
Sequence similarities
Belongs to the peptidase S16 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length805
- Mass (Da)88,861
- Last updated2019-07-31 v1
- ChecksumF1FB464FBE00E508
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP039691 EMBL· GenBank· DDBJ | QCI98083.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP124733 EMBL· GenBank· DDBJ | WHA40121.1 EMBL· GenBank· DDBJ | Genomic DNA |