ARC_CORJK
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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