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Literature summary extracted from
- Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains (2006), Protein Sci., 15, 1815-1828.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | additional information | activity of yeast lon alpha-proteolytic fragment enhanced when it is coexpressed with a construct containing the N- and A-domains (residues 1-917) | Saccharomyces cerevisiae |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | lon-N119 | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | digestion of lonA by alpha-chymotrypsin yields a stable fragment consisting of residues 491-584 crystallized. Crystal structure of the proteolytic domain of lonA (residues 585-784) elucidates a unique fold, P31 space group | Escherichia coli |
| 3.4.21.53 | proteolytic domain | Archaeoglobus fulgidus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | D676N | is completely inactive for protein degradation, it retains some basal ATPase activity, but no activation of ATPase activity occurs upon binding of protein substrates | Escherichia coli |
| 3.4.21.53 | E614K | is a dominant-negative mutant, can form mixed oligomers with wild-type lon and interferes with its activity | Escherichia coli |
| 3.4.21.53 | K362Q | intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation | Escherichia coli |
| 3.4.21.53 | additional information | lon mutant altered in substrate specificity. A mutation in lon that converts Glu240 to Lys results in stabilization of lon substrate RcsA in vivo but does not affect the degradation of lon substrate SulA. lon lacking 107 N-terminal residues has drastically reduced protein degrading activity in vitro | Escherichia coli |
| 3.4.21.53 | S679A | inactive, intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation | Escherichia coli |
| 3.4.21.53 | T534A | retains significant proteolytic activity | Archaeoglobus fulgidus |
| 3.4.21.53 | T704A | retains significant proteolytic activity | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.53 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.53 | additional information | Saccharomyces cerevisiae | construct containing residues 793-1133 of yeast lon, which comprises the proteolytic domain along with most of the alpha-domain, exhibits low but significant proteolytic activity in vivo | ? | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | Archaeoglobus fulgidus | - |
- |
- |
| 3.4.21.53 | Bordetella parapertussis | - |
- |
- |
| 3.4.21.53 | Brevibacillus thermoruber | - |
- |
- |
| 3.4.21.53 | Escherichia coli | - |
- |
- |
| 3.4.21.53 | Methanocaldococcus jannaschii | - |
- |
- |
| 3.4.21.53 | Mycolicibacterium smegmatis | - |
- |
- |
| 3.4.21.53 | Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | - |
Bordetella parapertussis |
| 3.4.21.53 | lon-N119 purified. Digestion of lonA by alpha-chymotrypsin yields a stable fragment consisting of residues 491-584 purified. lon proteolytic domain purified | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.53 | additional information | construct containing residues 793-1133 of yeast lon, which comprises the proteolytic domain along with most of the alpha-domain, exhibits low but significant proteolytic activity in vivo | Saccharomyces cerevisiae | ? | - |
? | |
| 3.4.21.53 | additional information | lacks 90, 225, or 277 N-terminal residues, practically no proteolytic activity while exhibiting reduced protein binding activity | Mycolicibacterium smegmatis | ? | - |
? | |
| 3.4.21.53 | additional information | proteolytic domain and a a large N-terminal domain, active site has a Ser-Lys catalytic dyad. Proteolytic domain exhibits no detectable activity against protein substrates degraded by full-length lon, but retains a significant fraction of peptidase activity | Escherichia coli | ? | - |
? | |
| 3.4.21.53 | additional information | proteolytic domain and a large transmembrane domain insertion within the AAA+ module between the Walker motifs A and B | Archaeoglobus fulgidus | ? | - |
? | |
| 3.4.21.53 | additional information | yeast lon has a relatively poor ability to unravel proteins and is only able to degrade proteins that have unstable tertiary structure | Saccharomyces cerevisiae | ? | - |
? | |
| 3.4.21.53 | RcsA + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.21.53 | SulA + H2O | - |
Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | dimer | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | heptamer | electron microscopic image analysis | Saccharomyces cerevisiae |
| 3.4.21.53 | hexamer | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | hexamer | crystallography | Archaeoglobus fulgidus |
| 3.4.21.53 | hexamer | gel filtration, sedimentation velocity experiments and cross-linking of intact and truncated species | Brevibacillus thermoruber |
| 3.4.21.53 | hexamer | negative stain electron microscopy, crystallography of the proteolytic domain | Escherichia coli |
| 3.4.21.53 | monomer | proteolytic domain in solution | Escherichia coli |
| 3.4.21.53 | monomer | proteolytic domain in solution | Archaeoglobus fulgidus |
| 3.4.21.53 | octamer | sedimentation | Escherichia coli |
| 3.4.21.53 | tetramer | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | tetramer | sedimentation | Escherichia coli |
| 3.4.21.53 | trimer | - |
Mycolicibacterium smegmatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | ATP-dependent lon protease | - |
Escherichia coli |
| 3.4.21.53 | ATP-dependent lon protease | - |
Methanocaldococcus jannaschii |
| 3.4.21.53 | ATP-dependent lon protease | - |
Archaeoglobus fulgidus |
| 3.4.21.53 | BPP1347 | similarity between BPP1347 and fragments of the N-domain of lon | Bordetella parapertussis |
| 3.4.21.53 | lon | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | lon | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | lon | - |
Brevibacillus thermoruber |
| 3.4.21.53 | lon protease | - |
Escherichia coli |
| 3.4.21.53 | lon protease | - |
Methanocaldococcus jannaschii |
| 3.4.21.53 | lon protease | - |
Archaeoglobus fulgidus |
| 3.4.21.53 | lonA | - |
Escherichia coli |
| 3.4.21.53 | lonB | - |
Methanocaldococcus jannaschii |
| 3.4.21.53 | lonB | - |
Archaeoglobus fulgidus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | ATP | - |
Saccharomyces cerevisiae | |
| 3.4.21.53 | ATP | ATPase domain that includes AAA+ modules | Escherichia coli | |
| 3.4.21.53 | ATP | ATPase domain that includes AAA+ modules | Archaeoglobus fulgidus | |
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Release 2023.1 (January 2023)
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