ID   ARC_RHOE4               Reviewed;         591 AA.
AC   C0ZZV2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Proteasome-associated ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
DE   AltName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE            Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
DE   AltName: Full=Proteasomal ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
GN   Name=arc {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=RER_31790;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000255|HAMAP-Rule:MF_02112}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02112}.
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       {ECO:0000255|HAMAP-Rule:MF_02112}.
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. {ECO:0000255|HAMAP-Rule:MF_02112}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_02112}.
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DR   EMBL; AP008957; BAH33887.1; -; Genomic_DNA.
DR   RefSeq; WP_003944870.1; NC_012490.1.
DR   AlphaFoldDB; C0ZZV2; -.
DR   SMR; C0ZZV2; -.
DR   STRING; 234621.RER_31790; -.
DR   EnsemblBacteria; BAH33887; BAH33887; RER_31790.
DR   GeneID; 64141013; -.
DR   KEGG; rer:RER_31790; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 2.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02112; ARC_ATPase; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR   InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR   InterPro; IPR022482; Proteasome_ATPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   Pfam; PF17758; Prot_ATP_OB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03689; pup_AAA; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Nucleotide-binding; Proteasome.
FT   CHAIN           1..591
FT                   /note="Proteasome-associated ATPase"
FT                   /id="PRO_0000397012"
FT   REGION          590..591
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          10..77
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         278..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   591 AA;  65354 MW;  361FFFAB64F07A50 CRC64;
     MSSTENPDSV AAAEELHALR VEAQVLRRQL AQSPEQVREL ESKVDSLSIR NSKLMDTLKE
     ARQQLIALRE EVDRLGQPPS GYGVLLSVHE DKTVDVFTSG RKMRLTCSPN IDTDTLALGQ
     TVRLNEALTI VEAGTYEQVG EISTLREVLD DGLRALVVGH ADEERIVWLA APLAAVFADP
     EADIIAYDAD SPTRKLRPGD SLLVDTKAGY AFERIPKAEV EDLVLEEVPD VHYDDIGGLG
     RQIEQIRDAV ELPFLHKDLF HEYSLRPPKG VLLYGPPGCG KTLIAKAVAN SLAKKIAEAR
     GQDSKDAKSY FLNIKGPELL NKFVGETERH IRMIFQRARE KASEGTPVIV FFDEMDSIFR
     TRGSGVSSDV ETTVVPQLLS EIDGVEGLEN VIVIGASNRE DMIDPAILRP GRLDVKIKIE
     RPDAESAQDI FSKYLVDGLP INADDLAEFG GDRTACLKAM IVRVVDRMYA ESEENRFLEV
     TYANGDKEVL FFKDFNSGAM IQNIVDRAKK YAIKSVLDTG APGLRVQHLF DSIVDEFAEN
     EDLPNTTNPD DWARISGKKG ERIVYIRTLV TGKNASASRA IDTESNTGQY L