ARC_CORDI
ID ARC_CORDI Reviewed; 509 AA.
AC Q6NH92;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=DIP1248;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(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; BX248357; CAE49777.1; -; Genomic_DNA.
DR RefSeq; WP_010934926.1; NC_002935.2.
DR AlphaFoldDB; Q6NH92; -.
DR SMR; Q6NH92; -.
DR STRING; 257309.DIP1248; -.
DR DNASU; 2649803; -.
DR EnsemblBacteria; CAE49777; CAE49777; DIP1248.
DR KEGG; cdi:DIP1248; -.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR Proteomes; UP000002198; 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..509
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396975"
FT COILED 11..50
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 236..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 509 AA; 55668 MW; 8B58DBF5A1641851 CRC64;
MLTSDPSEST AHLQRTISNL SARNAKLAEL LKASRDKLSI LQDQLEDLAA PPSTYGTFLE
FSGGRETAEV FTAGRHMRLR ISPDVEKAEL VPGVQVRLGE ASQVVEVCDI STTGQLATLV
ELLADNRGLI CDHTGEERVV KLAAALTEGV DKLPKAGDTL LVDPRAGYAF EVIPKTEVST
LALEEVPDVT YADIGGLNSQ IELIHDAVEL PFTQPDLYRA YDLKPPKGVL LYGPPGCGKT
LIAKAVANSL AQRIGAGNRS YFINVKGPEL LNKYVGETER RIRLIFERAR ELAEEGRPVI
VFFDEMESIF RTRGSGVSSD METTVVPQLL TELDGVESLS NVIIIGATNR EELIDPAILR
PGRLDVKIRV ERPDKQAARD VFARHLKQNI PTAEPIDSLI NNAVDHLYAD NPYVELSLID
GSTEILHYRD FVSGAMIANI VDRAKKCAIK DHIAGRHSGV ASEHLIAAIN AENHESEDLP
NTSNPDDWSR IIGRHGLRVA HARVLGGQR