ID   ARC_CORU7               Reviewed;         538 AA.
AC   B1VDV2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE            Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
GN   Name=arc {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=cu1040;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
CC   -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
CC       {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; AM942444; CAQ05000.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VDV2; -.
DR   SMR; B1VDV2; -.
DR   STRING; 504474.cu1040; -.
DR   EnsemblBacteria; CAQ05000; CAQ05000; cu1040.
DR   KEGG; cur:cu1040; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   Proteomes; UP000001727; Chromosome.
DR   GO; GO:0000502; C:proteasome complex; IEA:InterPro.
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; Coiled coil; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..538
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396981"
FT   COILED          14..54
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         240..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   538 AA;  58305 MW;  0E0DE4BAD83F595E CRC64;
     MTAQNPSDQP SPTARELRLA NHRLGAQNEK LTEALKASRE KLAEINSRLA DMAEPPSTYG
     TLLQLNGTGK TAEVFTSNRH MRLAVSPLLD RTDLQPGATV RLGENLQVVE VTGFADSGDV
     AAVVEVVGDR LIVADKLGEE AIVKAARPLQ SLITNRELTT GDSVVVDRRS GWAFHMIPRA
     EVSSLVLEEV PDVSYENIGG LSNQIEQIRD AVELPFLHPE IYRHYGLRPP KGVLLYGPPG
     NGKTLIAKAV ANSLSKSMGS SDKASRFADS YFLNVKGPEL LNKFVGETER QIRQIFERAR
     KIAHAGKPVI VFFDEMEAIF RTRGTGVSSD MESTVVPQLL SELDGVEGLD NVIVIGASNR
     EELIDPAILR PGRLDVKIRV DRPDQEAALD ILSKHIDASL PLAADLVAEH GGKEEAAAAL
     CRAIAEELFR RDAAHRYVTL HLADGQTKDL YWADFVSGAM LANIVDRAKT FAIKRALSQA
     ASTRDAAAEG GLNTADVLDA ITAEINDSEN LPDTTNPTEW ARISGHATGR VVDITLAD