Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 (Comment) | Organism |
---|---|
lon-N119 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
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 |
proteolytic domain | Archaeoglobus fulgidus |
Protein Variants | Comment | Organism |
---|---|---|
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 |
E614K | is a dominant-negative mutant, can form mixed oligomers with wild-type lon and interferes with its activity | Escherichia coli |
K362Q | intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation | Escherichia coli |
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 |
S679A | inactive, intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation | Escherichia coli |
T534A | retains significant proteolytic activity | Archaeoglobus fulgidus |
T704A | retains significant proteolytic activity | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Bordetella parapertussis | - |
- |
- |
Brevibacillus thermoruber | - |
- |
- |
Escherichia coli | - |
- |
- |
Methanocaldococcus jannaschii | - |
- |
- |
Mycolicibacterium smegmatis | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bordetella parapertussis |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
additional information | lacks 90, 225, or 277 N-terminal residues, practically no proteolytic activity while exhibiting reduced protein binding activity | Mycolicibacterium smegmatis | ? | - |
? | |
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 | ? | - |
? | |
additional information | proteolytic domain and a large transmembrane domain insertion within the AAA+ module between the Walker motifs A and B | Archaeoglobus fulgidus | ? | - |
? | |
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 | ? | - |
? | |
RcsA + H2O | - |
Escherichia coli | ? | - |
? | |
SulA + H2O | - |
Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Mycolicibacterium smegmatis |
heptamer | electron microscopic image analysis | Saccharomyces cerevisiae |
hexamer | - |
Mycolicibacterium smegmatis |
hexamer | crystallography | Archaeoglobus fulgidus |
hexamer | gel filtration, sedimentation velocity experiments and cross-linking of intact and truncated species | Brevibacillus thermoruber |
hexamer | negative stain electron microscopy, crystallography of the proteolytic domain | Escherichia coli |
monomer | proteolytic domain in solution | Escherichia coli |
monomer | proteolytic domain in solution | Archaeoglobus fulgidus |
octamer | sedimentation | Escherichia coli |
tetramer | - |
Mycolicibacterium smegmatis |
tetramer | sedimentation | Escherichia coli |
trimer | - |
Mycolicibacterium smegmatis |
Synonyms | Comment | Organism |
---|---|---|
ATP-dependent lon protease | - |
Escherichia coli |
ATP-dependent lon protease | - |
Methanocaldococcus jannaschii |
ATP-dependent lon protease | - |
Archaeoglobus fulgidus |
BPP1347 | similarity between BPP1347 and fragments of the N-domain of lon | Bordetella parapertussis |
lon | - |
Saccharomyces cerevisiae |
lon | - |
Mycolicibacterium smegmatis |
lon | - |
Brevibacillus thermoruber |
lon protease | - |
Escherichia coli |
lon protease | - |
Methanocaldococcus jannaschii |
lon protease | - |
Archaeoglobus fulgidus |
lonA | - |
Escherichia coli |
lonB | - |
Methanocaldococcus jannaschii |
lonB | - |
Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae | |
ATP | ATPase domain that includes AAA+ modules | Escherichia coli | |
ATP | ATPase domain that includes AAA+ modules | Archaeoglobus fulgidus |