ID   ARC_COREF               Reviewed;         526 AA.
AC   Q8FTE3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=CE1626;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18436.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FTE3; -.
DR   SMR; Q8FTE3; -.
DR   STRING; 196164.23493466; -.
DR   PRIDE; Q8FTE3; -.
DR   EnsemblBacteria; BAC18436; BAC18436; BAC18436.
DR   KEGG; cef:CE1626; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   Proteomes; UP000001409; 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..526
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396976"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         257..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   526 AA;  58354 MW;  73E54947374A9BBB CRC64;
     MGDMASSTDP AAHNSFSDFN REEMTRLADN VRSLQRTNQD LSARNTKLAE MLKSSRDKLS
     MMYQQLEDMA QPPSLYGTFL EMSKDGTNAE IFAGGRRMRV AMSPMLCAGD LMPGVQVRLG
     EGNQILEACD FEQTGDLATL MEMIGRDRAL ISDRSGEERV VKLAGPLMDR TRKLPRPGDT
     LLVDRRAGYA FENIPKTEIS KLALEEAPDV SYVDIGGLDD QIELIQDAVE LPFLHPEMYR
     SYKLHPPKGV LLYGPPGCGK TLIAKAVANS LSQRIGDAGT SYFINVKGPE LLNKYVGETE
     RQIRVIFERA RELAGDGRPV IIFFDEMESI FRTRGSGISS DMETTVVPQL LAELDGVEDL
     SNVIVIGATN REELIDPAIL RPGRLDIKIR VQRPNRSGAR DIFARYITDA IPLAAPVDEL
     IDTAVDHLFT PRPYVRLTLI DGTVETLNYH DFVSGAMIAN IVDRAKKSAI KDHIDGRTTG
     LSAEHLIHAI DQENQQSEDL PNTSNPDEWT RIIGRQGKRV AEVEVV