C1ASQ2 · ARC_RHOOB

Function

function

ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Pathway

Protein degradation; proteasomal Pup-dependent pathway.

Features

Showing features for binding site.

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TypeIDPosition(s)Description
Binding site278-283ATP (UniProtKB | ChEBI)

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 Componentproteasome complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Biological Processmodification-dependent protein catabolic process
Biological Processproteasomal protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Proteasome-associated ATPase
  • Alternative names
    • AAA ATPase forming ring-shaped complexes
      (ARC
      )
    • Proteasomal ATPase

Gene names

    • Name
      arc
    • Ordered locus names
      ROP_05870

Organism names

Accessions

  • Primary accession
    C1ASQ2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003970131-591Proteasome-associated ATPase

Interaction

Subunit

Homohexamer. Assembles into a hexameric ring structure that caps the 20S proteasome core. Strongly interacts with the prokaryotic ubiquitin-like protein Pup through a hydrophobic interface; the interacting region of ARC lies in its N-terminal coiled-coil domain. There is one Pup binding site per ARC hexamer ring. Upon ATP-binding, the C-terminus of ARC interacts with the alpha-rings of the proteasome core, possibly by binding to the intersubunit pockets.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for coiled coil, region.

TypeIDPosition(s)Description
Coiled coil8-77
Region590-591Docks into pockets in the proteasome alpha-ring

Domain

Consists of three main regions, an N-terminal coiled-coil domain that binds to protein Pup and functions as a docking station, an interdomain involved in ARC hexamerization, and a C-terminal ATPase domain of the AAA type.

Sequence similarities

Belongs to the AAA ATPase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    591
  • Mass (Da)
    65,836
  • Last updated
    2009-05-26 v1
  • Checksum
    8F552D3CBF1F0EA9
MSSTENPDSVAAARELEALRAEASALRRQLAESPEQLREMESRVDSLSIRNTKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLGVHDDQTVDVFTSGRKMRLTCSPNVDAETLKLGQTVRLNEALTIVEAGNFERVGEISTLREVLDDGQRALVVGHADEERIVWLAEPLATVFEESERESVAYDAESPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYELRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKEAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVETLPVHSDDLAEFGGDRTACIRVMIERVVDRMYAESEENRFLEVTYANGDKEVLYFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFSENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP011115
EMBL· GenBank· DDBJ
BAH48834.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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