HAMAP rule MF_02112

General rule information [?]

Accession	MF_02112
Dates	2-JUL-2010 (Created) 1-JUN-2023 (Last updated, Version 13)
Name	ARC_ATPase
Scope(s)	Bacteria Actinomycetota
Template(s)	P9WQN5 (ARC_MYCTU); O50202 (ARC_RHOER); [ Recover all ]
Triggered by	HAMAP; MF_02112 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	ARC
case <OC:Mycobacteriaceae> and <FTTag:Cterminus>
Protein name	RecName: Full=Proteasome-associated ATPase; AltName: Full=AAA ATPase forming ring-shaped complexes; Short=ARC; AltName: Full=Mycobacterial proteasome ATPase;
Gene name	Name=mpa;
end case
case not <OC:Mycobacteriaceae> and <FTTag:Cterminus>
Protein name	RecName: Full=Proteasome-associated ATPase; AltName: Full=AAA ATPase forming ring-shaped complexes; Short=ARC; AltName: Full=Proteasomal ATPase;
Gene name	Name=arc;
end case
case not <FTTag:Cterminus>
Protein name	RecName: Full=AAA ATPase forming ring-shaped complexes; Short=ARC;
Gene name	Name=arc;
end case

Comments [?]

case <FTTag:Cterminus>
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.
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.
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.
else
SUBUNIT	Homohexamer. Assembles into a hexameric ring structure.
end case
SIMILARITY	Belongs to the AAA ATPase family.

Keywords [?]

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0016887; Molecular function:ATP hydrolysis activity
case <FTTag:Cterminus>
GO:0032182; Molecular function:ubiquitin-like protein binding
GO:0010498; Biological process:proteasomal protein catabolic process
GO:0019941; Biological process:modification-dependent protein catabolic process
GO:0043335; Biological process:protein unfolding
GO:0000502; Cellular component:proteasome complex
GO:0022623; Cellular component:proteasome-activating nucleotidase complex
end case

Cross-references [?]

Features [?]

From: ARC_MYCTU (P9WQN5)

Key

From

Description

Tag

Condition

FTGroup

BINDING

296

301

/ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"

G-x-G-K-T-[LM]

REGION

608

609

/note="Docks into pockets in the proteasome alpha-ring"

Cterminus

Y-x

Additional information [?]

Size range	509-615 amino acids
Related rules	None
Fusion	Nter: None Cter: None
Comments	The protein performing the same function in archaea (called PAN) is in MF_00553. Some actinobacteria having a match in this family do not possess proteasome subunit sequences. The family members from these actinobacteria appear not to have the conserved C-terminus probably important for association with the proteasome, so the rule triggers a different annotation based on this fact.