P0A9M0 · LON_ECOLI
- ProteinLon protease
- Genelon
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids784 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. 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, UmuD and at least type II antitoxins CcdA, HipB and MazE (PubMed:16460757, PubMed:22720069, PubMed:24375411, PubMed:8022284).
Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system (PubMed:15009896).
Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system (PubMed:15009896).
Miscellaneous
Both its proteolytic and protein-activated ATPase activities are stimulated by DNA, especially single-stranded DNA.
Both high- and low-affinity ATPase sites are present in the homooligomer. Optimal peptidase activity requires ATP binding and hydrolysis at both sites, but ATP hydrolysis is not stoichiometrically linked to peptide hydrolysis.
Catalytic activity
Activity regulation
Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.201 mM | ATP for ATPase activity |
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | DNA binding | |
Molecular Function | 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 | |
Biological Process | proteolysis | |
Biological Process | response to heat | |
Biological Process | response to X-ray |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLon protease
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A9M0
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
When both lon and ycgE are disrupted levels of OmpF decrease, leading to lower drug susceptibility, with a greater effect at 26 degrees than at 37 degrees Celsius. The mechanism is not yet understood (PubMed:19721064).
Decreased persister cell formation upon antibiotic challenge due probably due to increased levels of MazF toxin (PubMed:24375411).
Decreased persister cell formation upon antibiotic challenge due probably due to increased levels of MazF toxin (PubMed:24375411).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 362 | Loss of proteolytic activity and ATP-binding. No increased persister cell formation. | ||||
Sequence: K → A | ||||||
Mutagenesis | 665 | Loss of proteolytic activity. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 667 | Loss of proteolytic activity. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 676 | Loss of proteolytic activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 679 | Loss of proteolytic activity. No increased persister cell formation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 743 | No effect. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000076133 | 2-784 | Lon protease | |||
Sequence: NPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK |
Proteomic databases
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0A9M0 | rplI P0A7R1 | 4 | EBI-547203, EBI-546437 | |
BINARY | P0A9M0 | torA P33225 | 2 | EBI-547203, EBI-557008 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-204 | Lon N-terminal | ||||
Sequence: IPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEI | ||||||
Domain | 592-773 | Lon proteolytic | ||||
Sequence: ENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQN |
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length784
- Mass (Da)87,438
- Last updated2005-07-19 v1
- Checksum4042499C97694EF8
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 264-317 | in Ref. 5; AAA24078 | ||||
Sequence: PKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ → RKRQKRKRTGVAEAENDVSDVGRSDRSAWLYRLDGTGAVECAYEGQKRPASGA | ||||||
Sequence conflict | 273 | in Ref. 4; AAA16837 | ||||
Sequence: A → R | ||||||
Sequence conflict | 307 | in Ref. 4; AAA16837 | ||||
Sequence: S → T | ||||||
Sequence conflict | 539-563 | in Ref. 5; AAA24078 | ||||
Sequence: AGVRGLEREISKLCRKAVKQLLLDK → RACVVWSVKSPNCVAKRLSSYCSIT | ||||||
Sequence conflict | 772 | in Ref. 4; AAA16837 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 779-784 | in Ref. 2; AAA24079 | ||||
Sequence: QVVTAK → HHSLRRRCSTASTYYWAKS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L12349 EMBL· GenBank· DDBJ | AAC36871.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
M38347 EMBL· GenBank· DDBJ | AAA24079.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L20572 EMBL· GenBank· DDBJ | AAA16837.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
J03896 EMBL· GenBank· DDBJ | AAA24078.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U82664 EMBL· GenBank· DDBJ | AAB40195.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC73542.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76219.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M10153 EMBL· GenBank· DDBJ | AAA23537.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift |