C9Z319 · ARC_STRSW

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.

158850100150200250300350400450500550
TypeIDPosition(s)Description
Binding site276-281ATP (UniProtKB | ChEBI)

GO annotations

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
      SCAB_73441

Organism names

Accessions

  • Primary accession
    C9Z319

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003970251-588Proteasome-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 region, coiled coil.

TypeIDPosition(s)Description
Region1-23Disordered
Coiled coil47-94
Region587-588Docks 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
    588
  • Mass (Da)
    65,300
  • Last updated
    2010-08-10 v2
  • Checksum
    D8CABE5C5A09BCA2
MAAHDDDMNRGIRPGRGSDDPSGQIAYLEQEIAVLRRKLADSPRHTRILEERIVELQTNLAGVSAQNERLANTLREARDQIVALKEEVDRLAQPPAGFGVFLTANEDGTADIFTGGRKLRVNVSPSVDLEELRRGQEVMLNEALNVVEAMEYESVGDIVTLKEILEDGERALVQGHTDEERVVRLAEPLLDITIRPGDALLLEPRSGYVYEVVPKSEVEELVLEEVPDIGYEQIGGLGNQIEMIRDAVELPYLYPDLFKEHELRPPKGVLLYGPPGCGKTLIAKAVANSLAKKVAEVTGQAQGKSFFLNIKGPELLNKYVGETERQIRLVFQRAREKASEGTPVIVFFDEMESLFRTRGSGVSSDVENTIVPQLLAEIDGVEGLQNVVVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAAKDIFQKYLTERLPLHTDDLGEHGGSKATTVQSMIQTAVEHMYAESEENRFLEVTYANGDKEVLYFKDFNSGAMIENIVGRAKKMAIKDFLDKNQKGLRVSHLLQACVDEFKENEDLPNTTNPDDWARISGKKGERIVYIRTLITGKQGADTGRSIDTVANTGQYL

Sequence caution

The sequence CBG74328.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN554889
EMBL· GenBank· DDBJ
CBG74328.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

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