Q9HSC3 · LONB_HALSA

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 (By similarity).

Features

Showing features for binding site, active site.

170250100150200250300350400450500550600650700
TypeIDPosition(s)Description
Binding site117-124ATP (UniProtKB | ChEBI)
Active site574
Active site617

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
      VNG_0303G

Organism names

Accessions

  • Primary accession
    Q9HSC3

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-183Cytoplasmic
Transmembrane184-201Helical
Topological domain202-206Extracellular
Transmembrane207-223Helical
Topological domain224-702Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000761521-702Archaeal Lon protease

Proteomic databases

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-63Disordered
Compositional bias9-23Acidic residues
Compositional bias29-63Acidic residues
Domain487-667Lon proteolytic

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    702
  • Mass (Da)
    76,017
  • Last updated
    2001-03-01 v1
  • Checksum
    203624C9836B2736
MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSIDEDNAEDDLLGGLRIDDTSDITVPDRLVDQVIGQEAAREIVKRAAKQHRHVMMIGSPGTGKSLLAKAMSRLLPKESLQDVLVYHNPDDSNEPKVRTVPAGKGEQIVDAHKEEARKRNQMRSFLMWIMILLAVGYALLIATPARPLLALLSAAGIYLLFRYTNRGSDAMVPKLLINNADRQVAPFEDATGAHAGAMLGDVRHDPFQSGGMATPSHERVEAGSIQKANKGVLFIDEINTLDVRSQQKLMTAIQEGEFSITGQSERSSGAMVQTEAVPCDFIMVAAGNMDAMENMHPALRSRIKGYGYEVYMDDTIEDTPDMRRKYARFVAQEVEKDGNLPHFAPDAIRELILEAKRRAGRKDSLTLKLRDLGGLVRVAGDIARSEGHDLTQRSDVLEAKKRSRSIEQQFVDNYIQRRKDYELGTTSEEAVGRVNGLAVMGGDSGIMLPVMAEITPAQSQEEGRIYATGQLKEMAEEAVENVSAIIKKFSDENMSEKDTHIQFVQAGEGGVDGDSASITVATAVISALEDIPVAQELAMTGSLSVRGDVLPVGGVTHKIEAAAKAGCERVIIPKANEDDVMIEDEYEEQIEIIPVTHISEVLDVALVGEPEKDSLVDRLKSITGKALDSASDSGTTGGNPSPQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-23Acidic residues
Compositional bias29-63Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE004437
EMBL· GenBank· DDBJ
AAG18884.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp