O50202 · ARC_RHOER

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 μMATP
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.

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

GO annotations

AspectTerm
Cellular Componentproteasome complex
Cellular Componentproteasome-activating nucleotidase complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionCTPase 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

Organism names

Accessions

  • Primary accession
    O50202

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00003834812-591Proteasome-associated ATPase

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

Family & Domains

Features

Showing features for coiled coil, region.

TypeIDPosition(s)Description
Coiled coil10-77
Region590-591Docks into pockets in the proteasome alpha-ring

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    591
  • Mass (Da)
    65,354
  • Last updated
    1998-06-01 v1
  • Checksum
    361FFFAB64F07A50
MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELLNKFVGETERHIRMIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVDGLPINADDLAEFGGDRTACLKAMIVRVVDRMYAESEENRFLEVTYANGDKEVLFFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF088800
EMBL· GenBank· DDBJ
AAC68690.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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