U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

lon Lon protease [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945085, updated on 30-Jul-2025
Official Symbol
lon
Official Full Name
Lon protease
Primary source
ECOCYC:EG10542
Locus tag
b0439
See related
ASAP:ABE-0001521
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
capR; deg; dir; ECK0433; lopA; muc
Summary
Lon dependent lethality is due to induction of yefM-yoeb toxin/antitoxin pair. [More information is available at EcoGene: EG10542]. Lon is an ATP-dependent protease responsible for degradation of misfolded proteins as well as a number of rapidly degraded regulatory proteins. [More information is available at EcoCyc: EG10542].
NEW
Try the new Gene table
Try the new Transcript table
Sequence:
NC_000913.3 (458888..461242)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP-dependent Clp protease proteolytic subunit Neighboring gene ATP-dependent Clp protease ATP-binding subunit ClpX Neighboring gene DNA-binding protein HU-beta Neighboring gene periplasmic folding chaperone

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity. Ebel W, et al. J Bacteriol, 1999 Apr. PMID 10094703, Free PMC Article
  2. The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Chung CH, et al. Proc Natl Acad Sci U S A, 1981 Aug. PMID 6458037, Free PMC Article
  3. DNA stimulates ATP-dependent proteolysis and protein-dependent ATPase activity of protease La from Escherichia coli. Chung CH, et al. Proc Natl Acad Sci U S A, 1982 Feb. PMID 6461007, Free PMC Article
  4. Identification of the gene lon (capR) product as a 94-kilodalton polypeptide by cloning and deletion analysis. Schoemaker JM, et al. J Bacteriol, 1981 Jul. PMID 7016844, Free PMC Article
  5. A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli. Fischer H, et al. FEBS Lett, 1994 Dec 12. PMID 7988699

See all (168) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Divergent Roles of Escherichia Coli Encoded Lon Protease in Imparting Resistance to Uncouplers of Oxidative Phosphorylation: Roles of marA, rob, soxS and acrB.
    Title: Divergent Roles of Escherichia Coli Encoded Lon Protease in Imparting Resistance to Uncouplers of Oxidative Phosphorylation: Roles of marA, rob, soxS and acrB.
  2. A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.
    Title: A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.
  3. Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.
    Title: Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.
  4. Escherichia coli, the ATP-dependent Lon protease is crucial for protein quality control and regulatory processes; data suggests previously unrecognized fundamental functions of Lon in sulfur assimilation, nucleotide biosynthesis, amino acid and central energy metabolism.
    Title: An Integrated Proteomic Approach Uncovers Novel Substrates and Functions of the Lon Protease in Escherichia coli.
  5. the ability of Lon to bind DNA is determined by its ATPase domain, that this binding is required for processing protein substrates in nucleoprotein complexes, and that Lon may help regulate DNA replication in response to growth conditions.
    Title: Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.
  6. These mutant rpoB RNA polymerases affect rcsA transcription, but per se are not defective either at rcsA or at cps promoters ande hence lead to increased capsular polysaccharide synthesis in Deltalon strains of Escherichia coli.
    Title: Suppression of capsule expression in Δlon strains of Escherichia coli by two novel rpoB mutations in concert with HNS: possible role for DNA bending at rcsA promoter.
  7. (p)ppGpp and Lon protease contribute to the robustness of the cell division.
    Title: Inactivation of Cell Division Protein FtsZ by SulA Makes Lon Indispensable for the Viability of a ppGpp0 Strain of Escherichia coli.
  8. Ec-Lon-protease was found to form complexes with the previously obtained thrombin aptamers whose molecules comprise the duplex domains and G-quadruplex region.
    Title: [Interaction of DNA Aptamers with the ATP-Dependent Lon Protease from Escherichia coli].
  9. Role of mutation of alpha-helical domains in the functioning of ATP-dependent Lon protease of Escherichia coli.
    Title: [The Effect of Mutations in the Inserted Domain of ATP-Dependent Lon Protease from E. coli on the Enzyme Function].
  10. The participation of HI(CC) domain in formation of the spatial structures of LonA proteases and/or formation of their complexes with DNA is suggested.
    Title: [Role of the α-helical domains in the functioning of ATP-dependent Lon protease of Escherichia coli].
Submit: New GeneRIF Correction See all GeneRIFs (33)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
enables ATP hydrolysis activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP-dependent peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP-dependent peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables sequence-specific DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type endopeptidase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables serine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type peptidase activity RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Process Evidence Code Pubs
involved_in cellular response to heat IEA
Inferred from Electronic Annotation
more info
  
involved_in protein catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in protein quality control for misfolded or incompletely synthesized proteins IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within protein quality control for misfolded or incompletely synthesized proteins IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to X-ray IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within response to heat IEP
Inferred from Expression Pattern
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
Lon protease
NP_414973.1

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    458888..461242
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414973.1 Lon protease

    See identical proteins and their annotated locations for NP_414973.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A376X353
    Conserved Domains (1) summary
    PRK10787
    Location:1 → 784
    PRK10787; DNA-binding ATP-dependent protease La; Provisional
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.