ID   ARC_KOCRD               Reviewed;         572 AA.
AC   B2GIP2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=KRH_13880;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(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; AP009152; BAG29735.1; -; Genomic_DNA.
DR   RefSeq; WP_012398456.1; NC_010617.1.
DR   AlphaFoldDB; B2GIP2; -.
DR   SMR; B2GIP2; -.
DR   STRING; 378753.KRH_13880; -.
DR   EnsemblBacteria; BAG29735; BAG29735; KRH_13880.
DR   KEGG; krh:KRH_13880; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   OrthoDB; 1115436at2; -.
DR   Proteomes; UP000008838; 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_0000396989"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COMPBIAS        536..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270..275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   572 AA;  62606 MW;  73915D5FE32644B1 CRC64;
     MTEPRHESGS AAPQRPATDP VQRQVNLLRD QKRNLDKQAA ALASQNEKLV RLLNASRQEI
     VGLKKTLAAE AEPPATYAVV LQVNHGRRPV GEATGDGPVV TGPTLDVLAA GRRMRVAVSP
     LVSFGACEPG LGVLLNENYV VVALLEYERT GEVATVKEVV DHDRVLTVGR SDEERVLLLS
     GRLRRERPKP GDAVTVDHRT GFALEPVTRT DVEQLVLEEV PDVSYTDIGG LGPQIEAIRD
     AVELPHVHPE IFREHGLRPP KGILLYGPPG NGKTLIAKAV ARSLAERSAA KAGRSRPEGY
     FLNIKGPELL DKYVGETERQ IRSIFANARE QAARGVPVVV FFDEMDSLFR VRGSGLSSDV
     ETTIVPQLLT EIDGVEQLDN VMVVGATNRE DMIDPAVLRP GRLDVKIRID RPDREGAREI
     FSLYLTPDLP LRDEDVARAG SRALAAEELV AAAVQRMYAR EPETEFLTIG YRNGTSETLY
     FSDYASGAVI RNVVDRAKKQ AIKTLLTTGR RGITAEHLVA AVDEEFHEQQ DLPDTEDSED
     WARLTGRRGD TIDSVHMASH RPQGEPGPGA TP