ID   ARC_BIFLO               Reviewed;         521 AA.
AC   Q8G3G6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=BL1794;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25577.1; -; Genomic_DNA.
DR   RefSeq; NP_696941.1; NC_004307.2.
DR   RefSeq; WP_007053165.1; NC_004307.2.
DR   AlphaFoldDB; Q8G3G6; -.
DR   SMR; Q8G3G6; -.
DR   STRING; 206672.BL1794; -.
DR   EnsemblBacteria; AAN25577; AAN25577; BL1794.
DR   KEGG; blo:BL1794; -.
DR   PATRIC; fig|206672.9.peg.1847; -.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   PhylomeDB; Q8G3G6; -.
DR   Proteomes; UP000000439; 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..521
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396969"
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;  56478 MW;  F81C226BA583E331 CRC64;
     MSDTEDLAAL NDRLMAKNHA LAEALSRAGK ELTKAKSQLA QLAQPPLTFA TMVKVDSTRT
     DEDGIQHASA EVISGTRRMV VPVASNVNAA RLTAGATVML NEKLVLVEQR DADTVGQIRS
     VKQVLDDGRL IVTDASGNPV LIRRSGALAY AGINQGDRII VDPSVRLAIE ALPAEGDKDL
     VLEETPDVTF ADIGGLDSEI GRIRDAVQLP FQHRALFERY DLKPPKGVLL YGPPGNGKTM
     IAKAVANALC EGGYDTNGDG SISPAETHVK 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