ARC_CORA7
ID ARC_CORA7 Reviewed; 524 AA.
AC C3PGA0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=cauri_1261;
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=548476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP32854.1; -; Genomic_DNA.
DR RefSeq; WP_010186636.1; NZ_ACLH01000002.1.
DR AlphaFoldDB; C3PGA0; -.
DR SMR; C3PGA0; -.
DR STRING; 548476.cauri_1261; -.
DR EnsemblBacteria; ACP32854; ACP32854; cauri_1261.
DR GeneID; 31923884; -.
DR KEGG; car:cauri_1261; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR Proteomes; UP000002077; 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..524
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396974"
FT COILED 4..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 524 AA; 56980 MW; 64253B89060C6B40 CRC64;
MNDATHSQEL GQQRRQIEQL AERNAKLAAL LKDARTKLQQ MLAEVDALAE PASTYGVFLG
YSGRAHDSRR DAEVYTNGRA MRVKISPNLE PGSLKVGQQV RLGEGFVIVE ACAPVNTGAL
ATLQERLGTD RAVVINSSGE EQVILLAAAL RDTVRAGDTL LVEPKSGVAT ERVHKTEVAQ
LTLEEVPDVS YEDIGGLDEQ ISLIRDSVEL PFLHPELYRK YDLQPPKGVL LYGPPGCGKT
LIAKAVAHSL SVSLGATAPS YFLNVKGPEL LNKFVGETER RIRLIFERAR ELASEPTEDG
SQRPVIIFFD EMESIFRTRG SGVSSDMETT VVPQLLTELD GVEKLSNVIV IGATNREELI
DPAIMRPGRL DIKIRVNRPT KQGAREIFAR HFPESVPHEG DLSQLIDTAV EDLYAERPFV
TLHFANADPR VLHYRDFVSG AMIANIVSRA KKLAIKEALD AATTSEGAQP AGITAAHLHQ
AIAAEQAESE YVPTSANPEE WAKIVAGTSA GAHVTGVELM GVKP