A0A1X3IBE1 · A0A1X3IBE1_ECOLX
- ProteinLon protease
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids799 (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. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.
Catalytic activity
Activity regulation
Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 371-378 | ATP (UniProtKB | ChEBI) | |||
Active site | 694 | ||||
Active site | 737 | ||||
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 > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A1X3IBE1
Proteomes
Subcellular Location
Expression
Induction
By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions.
Interaction
Subunit
Homohexamer. Organized in a ring with a central cavity. ATP binding and hydrolysis do not affect the oligomeric state of the enzyme.
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 26-219 | Lon N-terminal | |||
Coiled coil | 205-242 | ||||
Domain | 607-788 | Lon proteolytic | |||
Sequence similarities
Belongs to the peptidase S16 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length799
- Mass (Da)89,149
- Last updated2017-07-05 v1
- Checksum7F56494E10BA148A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADIK01000006 EMBL· GenBank· DDBJ | OSK32119.1 EMBL· GenBank· DDBJ | Genomic DNA |