ID   ARC_BIFLD               Reviewed;         521 AA.
AC   B3DRN4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=BLD_1971;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(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; CP000605; ACD99416.1; -; Genomic_DNA.
DR   RefSeq; WP_010080941.1; NZ_AABM02000004.1.
DR   AlphaFoldDB; B3DRN4; -.
DR   SMR; B3DRN4; -.
DR   PRIDE; B3DRN4; -.
DR   EnsemblBacteria; ACD99416; ACD99416; BLD_1971.
DR   KEGG; blj:BLD_1971; -.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   Proteomes; UP000002419; 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..521
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396970"
FT   COILED          4..44
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         235..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   521 AA;  56462 MW;  59D12F45C0461A01 CRC64;
     MSDTEDLAAL NDRLMAKNHA LAEALSRAGK ELTKAKSQLA QLAQPPLTFA TMVKVDSTRT
     DEDGIQHASA EVISGTRRMV VPVASNVNAA RLTAGATVML NEKLVLVEQR DADTVGQIRS
     VKQVLDDGRL IVTDASGNPV LIRRSGALAY AGINQGDRII IDPSVRLAIE ALPAEGDKDL
     VLEETPDVTF ADIGGLDSEI GRIRDAVQLP FQHRALFERY DLKPPKGVLL YGPPGNGKTM
     IAKAVANALC EGGYDSNGDG AISPAETHVK GVFLSVKGPE LLNKYVGESE RLIRLIFQRA
     RERAADGNPV VVFIDEMDSL LRTRGSGVSS DVETTIVPQF LSELDGVESL DNVMVIGASN
     RVDMIDPAVL RPGRLDVKIR VGRPKTNQAI AIVDHYLTDD LPLEDGVDAH ALSAVLVHDI
     YGTSERRHLC DVQEENGQWH ALFLADVVSG AMLKNIVDRA KTRAVKESIE TGLDVALTVP
     LLAAAVEDEY RETRDSMADV DPEQWSRING MDPIRRIRTA E