ARC_BIFDB
ID ARC_BIFDB Reviewed; 529 AA.
AC D2Q9C6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=BDP_0751;
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=401473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1;
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
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; CP001750; ADB09412.1; -; Genomic_DNA.
DR RefSeq; WP_003840824.1; NC_013714.1.
DR AlphaFoldDB; D2Q9C6; -.
DR SMR; D2Q9C6; -.
DR STRING; 401473.BDP_0751; -.
DR EnsemblBacteria; ADB09412; ADB09412; BDP_0751.
DR GeneID; 31605969; -.
DR KEGG; bde:BDP_0751; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR Proteomes; UP000008693; 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.
FT CHAIN 1..529
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396968"
FT COILED 15..62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 253..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 529 AA; 57648 MW; 93A56E0EFBA4F02E CRC64;
MGILDGESKK ARVGMERQDE RLRSLSEAND RLMAKNHALA KALTRATQEL TKAKAQLNQL
AGPPMTFATM IRVHAANTDE QGVQHASAEV ISGTRRMIVP VAANVQASRL EAGRTVLLNE
NMVIVDQHDT DTLGSVRTVR QVLDDGRLLV ADSGGNVTLV RRAGTLAKEN VNTGDRVSVD
SSVRFALTLI PVEDDADLVL EETPDVTFDD IGGLDEQIER IRDAVQMPFL HRELFERYDL
KPPKGVLLYG PPGNGKTLIA KAVANALAEG SGAGSGVFLS VKGPELLNKF VGESERLIRM
IFRRARERAA DGRPVIVFID EMDSLLRTRG SGVSSDVETT IVPQFLSELD GVESLDNVMV
IGASNRIDMI DPAVLRPGRL DVKIRVERPK AKQAEQIIRH YLTDDLPLTP GIEAKALTSV
LVADIYAVSE HRHLCDVCDE HGQWSPVYLA DVVSGAVLKN VVDRAKTKAV KISIESAEPA
AIGVNLLAKA VQEEFEETRD AVLDADPVQW SRINGFEAGH VTRIRPTAQ