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HAMAP rule MF_02112

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General rule information [?]

Accession MF_02112
Dates 2-JUL-2010 (Created)
13-JAN-2023 (Last updated, Version 12)
Name ARC_ATPase
Scope
Bacteria; Actinomycetota
Templates P9WQN5 (ARC_MYCTU); O50202 (ARC_RHOER): [Recover all]
Triggered by

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
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
arc
end case
case not <FTTag:Cterminus>
Protein name
RecName: Full=AAA ATPase forming ring-shaped complexes;
Short=ARC;
Gene 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 [?]

ATP-binding
Nucleotide-binding
case <FTTag:Cterminus>
Chaperone
Proteasome
end case

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 [?]

PROSITE PS00674; AAA; 1;
Pfam PF00004; AAA; 1;
TIGRFAMs TIGR03689; Pup_AAA; 1;

Computed features [?]

General Coiled_coil; -; 0-unlimited; trigger=yes;

Features [?]

From: ARC_MYCTU (P9WQN5)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     296     301       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G-x-G-K-T-[LM]  
REGION     608     609       Docks into pockets in the proteasome alpha-ring   Cterminus   Y-x  

Additional information [?]

Size range 509-615 amino acids
Related rules None
Fusion 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.


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