ID   ARC_CORJK               Reviewed;         517 AA.
AC   Q4JVP5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=jk0948;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37112.1; -; Genomic_DNA.
DR   RefSeq; WP_011273533.1; NC_007164.1.
DR   AlphaFoldDB; Q4JVP5; -.
DR   SMR; Q4JVP5; -.
DR   STRING; 306537.jk0948; -.
DR   EnsemblBacteria; CAI37112; CAI37112; jk0948.
DR   KEGG; cjk:jk0948; -.
DR   PATRIC; fig|306537.10.peg.959; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   OrthoDB; 1115436at2; -.
DR   Proteomes; UP000000545; 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..517
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396979"
FT   COILED          25..53
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         233..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   517 AA;  56087 MW;  61BAAA1FE82D9DED CRC64;
     MTENTSAEGP QTLRELQIAN RQLGARNAKL VELLQASRTK LEEINGRLEA LAEPPSTYGT
     LLQANRDFTA EVFTAGRRMR LMVSPHVPQH ELVPGAMVRL GEGQQVVEVT GQPDFGDIAQ
     VVEVSGDRLI IADKVGEEYV VKAAGDLAKE VVTGDSVIVD RKSGWAFEAV PRAETNNLIL
     EEVPDVTYDD IGGLGQQITQ IRDAVELPFL HPEIYTRYGL RPPKGVLLYG PPGNGKTLIA
     KAVANSLAQS DSPYFLNIKG PELLNKFVGE TERQIRAIFE QARRVASSGR PVIVFFDEME
     ALFRTRGTGV SSDMESTVVP QLLAELDGVE AAGNVIVIGA SNREELIDPA ILRPGRLDVK
     IRIARPDAFG AAAILSKHLD ASLPIDADFS AATGSNEAAA AALRQSIVDE LFTRDEEHRY
     VTLHYADGSR EDLYWADFVS GAMLANIVDR AKTLAIKDAL HNGANGTDGL RPEHVNAAVL
     AEVGDSEDLP DTTNPAEWAR IYGHGTKRVV DIDVHKV