ID   ARC_CORK4               Reviewed;         572 AA.
AC   C4LIL2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 67.
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=ckrop_0913;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACR17667.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001620; ACR17667.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041628810.1; NC_012704.1.
DR   AlphaFoldDB; C4LIL2; -.
DR   SMR; C4LIL2; -.
DR   STRING; 645127.ckrop_0913; -.
DR   EnsemblBacteria; ACR17667; ACR17667; ckrop_0913.
DR   KEGG; ckp:ckrop_0913; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   Proteomes; UP000001473; 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..572
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396980"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          42..70
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         258..263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   572 AA;  62540 MW;  C56F9E7504D68B5F CRC64;
     MTTASQQTSS HSTASSTSRK GNNNDATPSL KELQLANRTL GTRNAKLVEM LKASRDKLDA
     LNEQIRALSD PPSTYGTLLE LNPGGHSAEV FTSNRRMRLV VAPGVDTSQL TPGALVRLGE
     GQEVVEHCGF SDFGDIAVVK EFLPGGSRVV VADTMGDLRV LKIAAPLYEL WSQKNVGAGD
     QVLVDYRAGY AFESIPKADV ENLILEEIPE VSYEDIGGLH NQIEMIHDAV ELPFTHPDLY
     RKFDLQPPKG VLLYGPPGCG KTLIAKAVAH SLAEKMGSGG ESYFLNIKGP ELLNKFVGET
     ERQIRQIFDR ARSIAEDGRP VIVFFDEMDA IFRTRGSGIS SDLENTVVPQ LLSEIDGVED
     LRNVIVIGAS NREEMIDPAI LRPGRLDVKI RVERPDEKSA REIAELYLVD TLPLDPALVE
     ETGDRHAAVA ALIDELSSRM YAQHSDNEFV ELTFVDGSRE VLYYRDFASG AMIANIVDRA
     KKNALKRALA SGQPDNHGVS LEDVRTAVDQ EFAENDDLPN TANPDEWARI SGRTGQRVTE
     VTVAHHNRKT TTETEATEPE GTDSGKGHTD AS