ID   ARC_BIFLB               Reviewed;         522 AA.
AC   C6A7B2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, 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=Balac_0637;
OS   Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 /
OS   SD5219).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=580050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bl-04 / DGCC2908 / RB 4825 / SD5219;
RX   PubMed=19376856; DOI=10.1128/jb.00155-09;
RA   Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA   Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA   Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA   Roberts R.F.;
RT   "Comparison of the complete genome sequences of Bifidobacterium animalis
RT   subsp. lactis DSM 10140 and Bl-04.";
RL   J. Bacteriol. 191:4144-4151(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; CP001515; ACS46010.1; -; Genomic_DNA.
DR   RefSeq; WP_004218902.1; NC_012814.1.
DR   AlphaFoldDB; C6A7B2; -.
DR   SMR; C6A7B2; -.
DR   GeneID; 66532990; -.
DR   KEGG; blc:Balac_0637; -.
DR   PATRIC; fig|442563.4.peg.1223; -.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
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; -; 1.
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..522
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396966"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..57
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         248..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   522 AA;  56906 MW;  01B79ADEB6322CA5 CRC64;
     MGQEKHTDAA SQSRDPEAVA AHENDQLRQR NHALAKALTR ATEELRKAKA QLEQFMAPPL
     TMATMVRVHR CSTDEHGVRH ASAEILNGNR RQIVPLSPTV NPAQLGSGQG VLLDANMVIV
     DSCETPTTGP MRAVSESLAD GRLIVSDVGG NRGVVMRASA VARTPINVDD RVVIDPSGTY
     VLSVLPQEQA QDLLLEETPD VSFTDIGGLD EQIARIRDAV QLPFQHRDLF DRFDLKAPKG
     VLLYGPPGNG KTLIAKAIAH ELAAGSGNDG VFLSVKGPEL LNKFVGESER LIRRIFERAK
     ELSGAGRPVI VFIDEMDSLL RTRGTGVSSD VETTIVPQFL TELDGVESLD DVMVIGASNR
     IDMIDPAVLR PGRLDVKIHV TRPDETAAMA ITRHYLTDAL PLEPGRDADA LAASLVRDLF
     RRDESRLLAT LDEQGRRRGI YMADIVSGAM LRNIVDRAKT KAVKAEILHG SVSRDDEPQG
     ITEARIHEAI DDEYEQNRST INETDPGQWL RINALTLAAD GV