O50202 · ARC_RHOER
- ProteinProteasome-associated ATPase
- Genearc
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids591 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Activity regulation
ATPase activity is inhibited by N-ethylmaleimide (NEM) but not by sodium azide.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
200 μM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
268 pmol/min/ug |
Is also able to cleave CTP at half the rate of ATP hydrolysis, but GTP or UTP are not substrates.
pH Dependence
Optimum pH is 7-8.
Pathway
Protein degradation; proteasomal Pup-dependent pathway.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | proteasome complex | |
Cellular Component | proteasome-activating nucleotidase complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | CTPase 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 > Mycobacteriales > Nocardiaceae > Rhodococcus > Rhodococcus erythropolis group
Accessions
- Primary accessionO50202
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000383481 | 2-591 | Proteasome-associated ATPase | |||
Sequence: SSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELLNKFVGETERHIRMIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVDGLPINADDLAEFGGDRTACLKAMIVRVVDRMYAESEENRFLEVTYANGDKEVLFFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL |
Expression
Induction
Constitutively expressed.
Interaction
Subunit
Homohexamer. Assembles into a hexameric ring structure that likely caps the 20S proteasome core. Can form a complex composed of two stacked hexameric rings in vitro. Probably interacts with the prokaryotic ubiquitin-like protein Pup through a hydrophobic interface; the expected interacting region of ARC lies in its N-terminal coiled-coil domain. There is likely one Pup binding site per ARC hexamer ring. Upon ATP-binding, the C-terminus of ARC probably 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 10-77 | |||||
Sequence: VAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQ | ||||||
Region | 590-591 | Docks into pockets in the proteasome alpha-ring | ||||
Sequence: YL |
Domain
Consists of three main regions, an N-terminal coiled-coil domain (residues 1-77) that probably binds to protein Pup and functions as a docking station, an interdomain (residues 78-227) involved in Mpa hexamerization, and a C-terminal ATPase domain of the AAA type (residues 228-533).
Sequence similarities
Belongs to the AAA ATPase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length591
- Mass (Da)65,354
- Last updated1998-06-01 v1
- Checksum361FFFAB64F07A50
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF088800 EMBL· GenBank· DDBJ | AAC68690.1 EMBL· GenBank· DDBJ | Genomic DNA |