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HAMAP rule MF_02112

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General rule information [?]

Accession MF_02112
Dates 2-JUL-2010 (Created)
1-JUN-2023 (Last updated, Version 13)
Name ARC_ATPase
Scope(s) Bacteria
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;
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;
AltName: Full=Proteasomal ATPase;
Gene name Name=arc;
end case
case not <FTTag:Cterminus>
Protein name RecName: Full=AAA ATPase forming ring-shaped complexes;
Gene name Name=arc;
end case

Comments [?]

case <FTTag:Cterminus>
FUNCTIONATPase 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.
PATHWAYProtein degradation; proteasomal Pup-dependent pathway.
SUBUNITHomohexamer. 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.
DOMAINConsists 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.
SUBUNITHomohexamer. Assembles into a hexameric ring structure.
end case
SIMILARITYBelongs to the AAA ATPase family.

Keywords [?]

case <FTTag:Cterminus>
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;
NCBIfam TIGR03689; Pup_AAA; 1;
General Coiled_coil; -; 0-unlimited;

Features [?]

Key From To Description Tag Condition FTGroup
BINDING 296 301 /ligand="ATP"
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.

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