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Literature summary 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

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

Application

EC Number Application Comment Organism
3.4.21.53 medicine lon downregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins Pseudomonas syringae
3.4.21.53 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
3.4.21.53 medicine lon upregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins Yersinia pestis
3.4.21.53 additional information lon is involved in the control of swarmer cell differentiation Proteus mirabilis
3.4.21.53 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
3.4.21.53 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
3.4.21.53 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
3.4.21.53 additional information lonV gene is essential for viability, lonD gene is essential for spore and fruiting body formation Myxococcus xanthus

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.53 additional information attempts to construct a lonV mutant fail, lonD mutants are unable to sporulate Myxococcus xanthus
3.4.21.53 additional information lon mutants, accumulate abnormal proteins Salmonella enterica subsp. enterica serovar Typhimurium
3.4.21.53 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
3.4.21.53 additional information lon mutants, are unable to survive and proliferate murine macrophages, are extremely susceptible to hydrogen peroxide Salmonella enterica subsp. enterica serovar Typhimurium
3.4.21.53 additional information lon mutants, constitutively express the hrp regulon, hypersecrete effector proteins Pseudomonas syringae
3.4.21.53 additional information lon mutants, show defects in cell division, are unable to control initiation of DNA replication Caulobacter vibrioides
3.4.21.53 additional information lonB disruption does not affect sporulation Bacillus subtilis
3.4.21.53 additional information lonS mutants, constitutively differentiated in the swarmer mode Vibrio parahaemolyticus
3.4.21.53 additional information Pim1 mutants, are respiratory-deficient and unable to grow on non-fermentable carbon sources Saccharomyces cerevisiae
3.4.21.53 additional information total loss of lon activity leads to apoptosis Homo sapiens

Inhibitors

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

Localization

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

Organism

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.4.21.53 hexamer crystallography Escherichia coli

Synonyms

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