W9VCB4 · W9VCB4_9GAMM
- ProteinLon protease
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids819 (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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Chromatiaceae > Imhoffiella
Accessions
- Primary accessionW9VCB4
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, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-212 | Lon N-terminal | ||||
Sequence: VPVLPLRDVVVYPHMVIPLFVGRDKSIRALDGAMASDKQILLIAQKSADVDDPAVKDLHEIGTLANILQLLKLPDGTVKVLVEGNQRAHIERFLTTEEAFSAVIQPLEETLEVDEREQEVLMRSAMSLFDQYVKLNKKVPPEVLSSLASIDDAGRLADTMAAHMSLKLDEKQHVLEMVDVQARLEHLMGLMESEN | ||||||
Domain | 600-781 | Lon proteolytic | ||||
Sequence: HDQIGQVTGLAWTEVGGELLRIESALVPGKGKFTYTGQLGDVMQESIQAAMTVVRARADALGVPEDFHNKFDAHIHVPEGATPKDGPSAGVAMCTALVSALTRIPVRATVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIETVIIPLENERDLTEIPKNIKQHLKIHPVRWIDEVLELALVE | ||||||
Region | 786-819 | Disordered | ||||
Sequence: KAANIDGGESMAEEEEARDAGVDASRDQNARLHH | ||||||
Compositional bias | 799-819 | Basic and acidic residues | ||||
Sequence: EEEARDAGVDASRDQNARLHH |
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length819
- Mass (Da)91,384
- Last updated2014-05-14 v1
- ChecksumD2C2C2594C79B553
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 799-819 | Basic and acidic residues | ||||
Sequence: EEEARDAGVDASRDQNARLHH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AONC01000061 EMBL· GenBank· DDBJ | EXJ13682.1 EMBL· GenBank· DDBJ | Genomic DNA |