A0A3S5DJ88 · A0A3S5DJ88_AVIVO

Function

function

ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.

Catalytic activity

  • Hydrolysis of proteins in presence of ATP.
    EC:3.4.21.53 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

1804100200300400500600700800
TypeIDPosition(s)Description
Binding site356-363ATP (UniProtKB | ChEBI)
Active site679
Active site722

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Biological Processcellular response to heat
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease
  • EC number
  • Alternative names
    • ATP-dependent protease La

Gene names

    • Name
      lon
    • ORF names
      NCTC3438_00844

Organism names

Accessions

  • Primary accession
    A0A3S5DJ88

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-31Helical

Keywords

Expression

Induction

By heat shock.

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity.

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain11-204Lon N-terminal
Coiled coil234-261
Domain592-773Lon proteolytic
Region780-804Disordered
Compositional bias781-804Basic and acidic residues

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    804
  • Mass (Da)
    89,624
  • Last updated
    2019-04-10 v1
  • Checksum
    3DCF4B43AB616BBA
MNARRTKQKTMPVLPLRDVVVFPYMVMPLFVGREKSIASLEEAMENGKQLLLVSQKAAELEQPTVDDVYDVGTVANIIQLLNLPDGTVKVLVEGQQRAKISHLEDNGRFFEAKIELIDTQFGDETELEVAQNTALKEFEKYIELNKKVQPDVLSALKNIADPERLSDTMAAHMPVSVARKQEVLGIANVAERFEYLLGLMINEAGILEVEKRIRGRVKKQMEKSQRDYYLNEQIKAIQKELGETESTVDEVEQLRQKVEEAKMPKEAREKVEAELQKLKMMSPMSAEATVVRSYIDWMLQVPWYKRSKVKKDIVKAQEILDADHYGLERVKDRILEYLAVQSRLNQLKGPILCLVGPPGVGKTSLGQSIANATGRKYVRMALGGVRDEAEIRGHRKTYIGSLPGKLIQKMAKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNANFNDHYLEVDYDLSDVMFVATSNSMNIPGPLLDRMEVIRLSGYTEDEKLNIATRHLLNKQIERNGLKKGELKIEDSAILDIIRYYTREAGVRGLEREISKICRKAVKNLLLNPKLKSITVNSDNLNEYLGVKRFEFGRADTQNRVGEVTGLAWTQVGGDLLTIEATSVIGKGKLTYTGSLGDVMKESIQAAMTVVRSRAEKLGIAPDFHEKRDIHIHVPDGATPKDGPSAGIAMCTALVSCLTGNPVKSEVAMTGEISLRGKVLPIGGLKEKLLAAHRGGIKTVIIPKDNVKDLEEIPENAKNSLDIRPVETIDEVLSIALENPPEGVDFSHLIAKEEKTTPRRKSKRAESAVN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias781-804Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR134167
EMBL· GenBank· DDBJ
VEB23161.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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