AC   MF_02112;
DC   Protein; auto
TR   HAMAP; MF_02112; -; 1; level=0
XX
Names: ARC_ATPase
XX
ID   ARC
case <OC:Mycobacteriaceae> and <FTTag:Cterminus>
DE   RecName: Full=Proteasome-associated ATPase;
DE   AltName: Full=AAA ATPase forming ring-shaped complexes;
DE            Short=ARC;
DE   AltName: Full=Mycobacterial proteasome ATPase;
GN   Name=mpa;
end case
case not <OC:Mycobacteriaceae> and <FTTag:Cterminus>
DE   RecName: Full=Proteasome-associated ATPase;
DE   AltName: Full=AAA ATPase forming ring-shaped complexes;
DE            Short=ARC;
DE   AltName: Full=Proteasomal ATPase;
GN   Name=arc;
end case
case not <FTTag:Cterminus>
DE   RecName: Full=AAA ATPase forming ring-shaped complexes;
DE            Short=ARC;
GN   Name=arc;
end case
XX
case <FTTag:Cterminus>
CC   -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC       unfolding and translocation of pupylated proteins into the bacterial
CC       20S proteasome core particle. May be essential for opening the gate of
CC       the 20S proteasome via an interaction with its C-terminus, thereby
CC       allowing substrate entry and access to the site of proteolysis. Thus,
CC       the C-termini of the proteasomal ATPase may function like a 'key in a
CC       lock' to induce gate opening and therefore regulate proteolysis.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC   -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure that
CC       caps the 20S proteasome core. Strongly interacts with the prokaryotic
CC       ubiquitin-like protein Pup through a hydrophobic interface; the
CC       interacting region of ARC lies in its N-terminal coiled-coil domain.
CC       There is one Pup binding site per ARC hexamer ring. Upon ATP-binding,
CC       the C-terminus of ARC interacts with the alpha-rings of the proteasome
CC       core, possibly by binding to the intersubunit pockets.
CC   -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC       domain that binds to protein Pup and functions as a docking station, an
CC       interdomain involved in ARC hexamerization, and a C-terminal ATPase
CC       domain of the AAA type.
else
CC   -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
end case
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
XX
DR   PROSITE; PS00674; AAA; 1; trigger=no
DR   Pfam; PF00004; AAA; 1; trigger=no
DR   NCBIfam; TIGR03689; Pup_AAA; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=yes
XX
KW   ATP-binding
KW   Nucleotide-binding
case <FTTag:Cterminus>
KW   Chaperone
KW   Proteasome
end case
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016887; F:ATP hydrolysis activity
case <FTTag:Cterminus>
GO   GO:0032182; F:ubiquitin-like protein binding
GO   GO:0010498; P:proteasomal protein catabolic process
GO   GO:0019941; P:modification-dependent protein catabolic process
GO   GO:0043335; P:protein unfolding
GO   GO:0000502; C:proteasome complex
GO   GO:0022623; C:proteasome-activating nucleotidase complex
end case
XX
FT   From: ARC_MYCTU (P9WQN5)
FT   BINDING         296..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x-G-K-T-[LM]
FT   REGION          608..609
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT   Tag: Cterminus; Condition: Y-x
XX
Size: 509-615;
Related: None;
Template: P9WQN5; O50202;
Scope:
 Bacteria; Actinomycetota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.13 2023/06/01
//