Q9HJ89 · LONB_THEAC

Function

function

ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.196 mMATP

Features

Showing features for binding site, active site.

165750100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site57-64ATP (UniProtKB | ChEBI)
Active site525
Active site568

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 Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processprotein catabolic process
Biological Processproteolysis
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Gene names

    • Ordered locus names
      Ta1081

Organism names

Accessions

  • Primary accession
    Q9HJ89

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-123Cytoplasmic
Transmembrane124-144Helical
Topological domain145Extracellular
Transmembrane146-166Helical
Topological domain167-657Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis63Completely abolishes ATPase activity and makes peptidase activity independent on ATP stimulus.
Mutagenesis241Retains 5% ATPase activity. Proteolytic activity is greatly impaired and cannot be stimulated by nucleotides.
Mutagenesis293Severely reduces ATPase and proteolytic activity.
Mutagenesis305Decreases ATPase activity. Completely abolishes peptidase activity in the absence of ATP, but ATP-stimulated peptidase activity i close to wild-type levels.
Mutagenesis375Almost completely abolishes ATPase activity and severely reduces proteolytic activity.
Mutagenesis382Decreases ATPase activity. Completely abolishes peptidase activity in the absence of ATP, but ATP-stimulated peptidase activity i close to wild-type levels.
Mutagenesis525Abolishes peptidase activity, but retains ATPase activity.
Mutagenesis568Abolishes peptidase activity, but retains ATPase activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000761541-657Archaeal Lon protease

Proteomic databases

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain433-618Lon proteolytic

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    657
  • Mass (Da)
    71,601
  • Last updated
    2001-03-01 v1
  • Checksum
    FD465CD99F5B38F7
MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRSRSIMFVIFSVVLLGIIAAIVLRSITLIFFAIMAAAFLYMAMAFNPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDYMDDNDENRRKLVQFIAQEVEKDKKIPHFDKSAIIEVIKEAQKRSGRRNKLTLRLRELGGLVRVAGDIAVSQKKTVVTAADVIAAKNLAKPLEQQIADRSIEIKKIYKTFRTEGSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVNSPEKEKLFDRISNLINAAKIIKPQRPATPATTRAGNNAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL445066
EMBL· GenBank· DDBJ
CAC12209.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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