ARC_RHOOB
ID ARC_RHOOB Reviewed; 591 AA.
AC C1ASQ2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=ROP_05870;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
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-2009) 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; AP011115; BAH48834.1; -; Genomic_DNA.
DR RefSeq; WP_012687839.1; NC_012522.1.
DR AlphaFoldDB; C1ASQ2; -.
DR SMR; C1ASQ2; -.
DR STRING; 632772.ROP_05870; -.
DR EnsemblBacteria; BAH48834; BAH48834; ROP_05870.
DR KEGG; rop:ROP_05870; -.
DR PATRIC; fig|632772.20.peg.645; -.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000002212; 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_0000397013"
FT REGION 590..591
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 8..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; 65836 MW; 8F552D3CBF1F0EA9 CRC64;
MSSTENPDSV AAARELEALR AEASALRRQL AESPEQLREM ESRVDSLSIR NTKLMDTLKE
ARQQLIALRE EVDRLGQPPS GYGVLLGVHD DQTVDVFTSG RKMRLTCSPN VDAETLKLGQ
TVRLNEALTI VEAGNFERVG EISTLREVLD DGQRALVVGH ADEERIVWLA EPLATVFEES
ERESVAYDAE SPTRKLRPGD SLLVDTKAGY AFERIPKAEV EDLVLEEVPD VHYDDIGGLG
RQIEQIRDAV ELPFLHKDLF HEYELRPPKG VLLYGPPGCG KTLIAKAVAN SLAKKIAEAR
GQDSKEAKSY FLNIKGPELL NKFVGETERH IRLIFQRARE KASEGTPVIV FFDEMDSIFR
TRGSGVSSDV ETTVVPQLLS EIDGVEGLEN VIVIGASNRE DMIDPAILRP GRLDVKIKIE
RPDAESAQDI FSKYLVETLP VHSDDLAEFG GDRTACIRVM IERVVDRMYA ESEENRFLEV
TYANGDKEVL YFKDFNSGAM IQNIVDRAKK YAIKSVLDTG APGLRVQHLF DSIVDEFSEN
EDLPNTTNPD DWARISGKKG ERIVYIRTLV TGKNASASRA IDTESNTGQY L
