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Literature summary for 3.4.21.53 extracted from

  • Tsilibaris, V.; Maenhaut-Michel, G.; Van Melderen, L.
    Biological roles of the Lon ATP-dependent protease (2006), Res. Microbiol., 157, 701-713.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ethanol
-
Bacillus subtilis
H2O2
-
Bacillus subtilis
additional information lon gene is heat shock-induced Escherichia coli
additional information lon gene is heat shock-induced Streptomyces lividans
additional information lon gene is not heat shock-induced Brevibacillus brevis
additional information lon gene is not heat shock-induced Myxococcus xanthus
additional information lonA gene is induced by heat and salt, lonB is not stress-induced Bacillus subtilis
Polyphosphate stimulates lon proteolytic activity, affects substrate preference and oligomeric state of the enzyme Escherichia coli
puromycin
-
Bacillus subtilis

Application

Application Comment Organism
medicine lon downregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins Pseudomonas syringae
medicine lon downregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins. Oppositely modulates infection stages (epithelial invasion and survival within murine macrophages) Salmonella enterica subsp. enterica serovar Typhimurium
medicine lon upregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins Yersinia pestis
additional information lon is involved in the control of swarmer cell differentiation Proteus mirabilis
additional information lon is required for cell cycle-dependent regulation of methylation, correct completion of cell division and normal progression of the cell cycle Caulobacter vibrioides
additional information lon plays a role in protein quality control by destroying unfolded proteins, it participates in regulatory circuits by controlling amount and availability of specific substrates Escherichia coli
additional information lonA plays a major role in initiating sporulation in response to environmental conditions, lonB is forespore-specific and may have a limited role in the regulation of sporulation Bacillus subtilis
additional information lonV gene is essential for viability, lonD gene is essential for spore and fruiting body formation Myxococcus xanthus

Crystallization (Commentary)

Crystallization (Comment) Organism
carboxy-terminal domain crystallized Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information attempts to construct a lonV mutant fail, lonD mutants are unable to sporulate Myxococcus xanthus
additional information lon mutants, accumulate abnormal proteins Salmonella enterica subsp. enterica serovar Typhimurium
additional information lon mutants, accumulate abnormal proteins, form mucoid colonies and long filaments, fail to adapt rapidly to a nutrional downshift, are sensitive to UV at 30°C because of SulA accumulation, at higher temperatures they lose their sensitivity because ClpYQ takes over SulA degredation Escherichia coli
additional information lon mutants, are unable to survive and proliferate murine macrophages, are extremely susceptible to hydrogen peroxide Salmonella enterica subsp. enterica serovar Typhimurium
additional information lon mutants, constitutively express the hrp regulon, hypersecrete effector proteins Pseudomonas syringae
additional information lon mutants, show defects in cell division, are unable to control initiation of DNA replication Caulobacter vibrioides
additional information lonB disruption does not affect sporulation Bacillus subtilis
additional information lonS mutants, constitutively differentiated in the swarmer mode Vibrio parahaemolyticus
additional information Pim1 mutants, are respiratory-deficient and unable to grow on non-fermentable carbon sources Saccharomyces cerevisiae
additional information total loss of lon activity leads to apoptosis Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibition of activity by the T4-encoded PinA protein, non-competetive inhibitor Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Brevibacillus brevis
-
-
-
Caulobacter vibrioides
-
-
-
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Myxococcus xanthus
-
-
-
no activity in Lactobacillus sp.
-
-
-
no activity in Mycobacterium leprae
-
-
-
no activity in Mycobacterium tuberculosis
-
-
-
no activity in Streptococcus sp.
-
-
-
Proteus mirabilis
-
-
-
Pseudomonas syringae
-
-
-
Saccharomyces cerevisiae
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Streptomyces lividans
-
-
-
Vibrio parahaemolyticus
-
-
-
Yersinia pestis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
spore
-
Myxococcus xanthus
-
spore lonA is involved in the control of sporulation initiation, lonB is only present in the forespore Bacillus subtilis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CcdA + H2O
-
Escherichia coli ?
-
?
CcrM + H2O
-
Caulobacter vibrioides ?
-
?
FlhC + H2O
-
Proteus mirabilis ?
-
?
FlhD + H2O
-
Proteus mirabilis ?
-
?
heat shock sigma factor 32 + H2O degraded by synergistic action of lon, Clp and HflB Escherichia coli ?
-
?
HemA + H2O conditional proteolysis mediated by lon and ClpAP Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?
HilC + H2O
-
Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?
HilD + H2O
-
Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?
homoserine trans-succinylase + H2O degraded by synergistic action of lon, ClpYQ, ClpXP and/or ClpAP Escherichia coli ?
-
?
HrpR + H2O
-
Pseudomonas syringae ?
-
?
MarA + H2O
-
Escherichia coli ?
-
?
MazE antitoxin + H2O
-
Escherichia coli ?
-
?
PasA + H2O
-
Escherichia coli ?
-
?
PemI + H2O
-
Escherichia coli ?
-
?
RelB antitoxin + H2O
-
Escherichia coli ?
-
?
ribosomal L13 protein + H2O
-
Escherichia coli ?
-
?
ribosomal L9 protein + H2O
-
Escherichia coli ?
-
?
ribosomal S2 protein + H2O
-
Escherichia coli ?
-
?
sigma factor G + H2O lonA Bacillus subtilis ?
-
?
sigma factor H + H2O lonA Bacillus subtilis ?
-
?
SMC protein + H2O lonA Bacillus subtilis ?
-
?
SoxS + H2O
-
Escherichia coli ?
-
?
StpA + H2O
-
Escherichia coli ?
-
?
SulA + H2O
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
hexamer crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
lon
-
Salmonella enterica subsp. enterica serovar Typhimurium
lon
-
Brevibacillus brevis
lon
-
Escherichia coli
lon
-
Homo sapiens
lon
-
Saccharomyces cerevisiae
lon
-
Proteus mirabilis
lon
-
Yersinia pestis
lon
-
Pseudomonas syringae
lon
-
Caulobacter vibrioides
lon
-
Streptomyces lividans
lon ATP-dependent protease
-
Salmonella enterica subsp. enterica serovar Typhimurium
lon ATP-dependent protease
-
Brevibacillus brevis
lon ATP-dependent protease
-
Bacillus subtilis
lon ATP-dependent protease
-
Escherichia coli
lon ATP-dependent protease
-
Homo sapiens
lon ATP-dependent protease
-
Saccharomyces cerevisiae
lon ATP-dependent protease
-
Proteus mirabilis
lon ATP-dependent protease
-
Myxococcus xanthus
lon ATP-dependent protease
-
Yersinia pestis
lon ATP-dependent protease
-
Pseudomonas syringae
lon ATP-dependent protease
-
Caulobacter vibrioides
lon ATP-dependent protease
-
Vibrio parahaemolyticus
lon ATP-dependent protease
-
Streptomyces lividans
lonA
-
Bacillus subtilis
lonB
-
Bacillus subtilis
lonD
-
Myxococcus xanthus
lonS
-
Vibrio parahaemolyticus
lonV
-
Myxococcus xanthus
PIM1
-
Saccharomyces cerevisiae