HAMAP rule MF_01973
General rule information
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| Accession | MF_01973 |
| Dates | 18-JUN-2010 (Created)
1-JUN-2023 (Last updated, Version 19) |
| Name | lon_bact |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P0A9M0 (LON_ECOLI); P37945 (LON1_BACSU); [ Recover all ] |
| Triggered by |
HAMAP; MF_01973 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LON |
| Protein name | RecName: Full=Lon protease; EC=3.4.21.53; AltName: Full=ATP-dependent protease La; |
| Gene name | Name=lon; |
Comments
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| case <OC:Escherichia> or <OC:Shigella> | |
| 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. |
| else | |
| 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. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; |
| case <OC:Escherichia> or <OC:Shigella> | |
| ACTIVITY REGULATION | Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation. |
| end case | |
| case <OC:Escherichia> or <OC:Shigella> | |
| SUBUNIT | Homohexamer. Organized in a ring with a central cavity. ATP binding and hydrolysis do not affect the oligomeric state of the enzyme. |
| else | |
| SUBUNIT | Homohexamer. Organized in a ring with a central cavity. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| case <OC:Escherichia> or <OC:Shigella> | |
| INDUCTION | By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions. |
| else | |
| INDUCTION | By heat shock. |
| end case | |
| SIMILARITY | Belongs to the peptidase S16 family. |
Keywords
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| case <FTTag:ATP> | |
| ATP-binding | |
| Nucleotide-binding | |
| end case | |
| Cytoplasm | |
| Hydrolase | |
| Protease | |
| Serine protease | |
| Stress response | |
Gene Ontology
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| GO:0005737; Cellular component:cytoplasm |
| GO:0005524; Molecular function:ATP binding |
| GO:0016887; Molecular function:ATP hydrolysis activity |
| GO:0004176; Molecular function:ATP-dependent peptidase activity |
| GO:0004252; Molecular function:serine-type endopeptidase activity |
| GO:0043565; Molecular function:sequence-specific DNA binding |
| GO:0034605; Biological process:cellular response to heat |
| GO:0006515; Biological process:protein quality control for misfolded or incompletely synthesized proteins |
Cross-references
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| PROSITE | PS51787; LON_N; 1; |
| PROSITE | PS51786; LON_PROTEOLYTIC; 1; |
| PROSITE | PS01046; LON_SER; 1; |
| Pfam | PF00004; AAA; 1; |
| Pfam | PF02190; LON; 1; |
| PRINTS | PR00830; ENDOLAPTASE; 1; |
| NCBIfam | TIGR00763; lon; 1; |
Features
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| From: LON_ECOLI (P0A9M0) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 356 | 363 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
ATP | G-[AP]-P-G-[ITV]-G-K-[ST] | |||||||
| ACT_SITE | 679 | 679 | S | |||||||||
| ACT_SITE | 722 | 722 | K | |||||||||
Additional information
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| Size range | 768-996 amino acids |
| Related rules |
MF_03120 MF_03121 |
| Fusion | Nter: None Cter: None |