C9Z319 · ARC_STRSW
- ProteinProteasome-associated ATPase
- Genearc
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids588 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | proteasome complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Biological Process | modification-dependent protein catabolic process | |
Biological Process | proteasomal protein catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProteasome-associated ATPase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionC9Z319
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000397025 | 1-588 | Proteasome-associated ATPase | |||
Sequence: MAAHDDDMNRGIRPGRGSDDPSGQIAYLEQEIAVLRRKLADSPRHTRILEERIVELQTNLAGVSAQNERLANTLREARDQIVALKEEVDRLAQPPAGFGVFLTANEDGTADIFTGGRKLRVNVSPSVDLEELRRGQEVMLNEALNVVEAMEYESVGDIVTLKEILEDGERALVQGHTDEERVVRLAEPLLDITIRPGDALLLEPRSGYVYEVVPKSEVEELVLEEVPDIGYEQIGGLGNQIEMIRDAVELPYLYPDLFKEHELRPPKGVLLYGPPGCGKTLIAKAVANSLAKKVAEVTGQAQGKSFFLNIKGPELLNKYVGETERQIRLVFQRAREKASEGTPVIVFFDEMESLFRTRGSGVSSDVENTIVPQLLAEIDGVEGLQNVVVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAAKDIFQKYLTERLPLHTDDLGEHGGSKATTVQSMIQTAVEHMYAESEENRFLEVTYANGDKEVLYFKDFNSGAMIENIVGRAKKMAIKDFLDKNQKGLRVSHLLQACVDEFKENEDLPNTTNPDDWARISGKKGERIVYIRTLITGKQGADTGRSIDTVANTGQYL |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MAAHDDDMNRGIRPGRGSDDPSG | ||||||
Coiled coil | 47-94 | |||||
Sequence: RILEERIVELQTNLAGVSAQNERLANTLREARDQIVALKEEVDRLAQP | ||||||
Region | 587-588 | Docks into pockets in the proteasome alpha-ring | ||||
Sequence: YL |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length588
- Mass (Da)65,300
- Last updated2010-08-10 v2
- ChecksumD8CABE5C5A09BCA2
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FN554889 EMBL· GenBank· DDBJ | CBG74328.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |