ID   ARC_BIFAB               Reviewed;         524 AA.
AC   D3R4I7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=BIF_01286;
OS   Bifidobacterium animalis subsp. lactis (strain BB-12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=552531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BB-12;
RX   PubMed=20190051; DOI=10.1128/jb.00109-10;
RA   Garrigues C., Johansen E., Pedersen M.B.;
RT   "Complete genome sequence of Bifidobacterium animalis subsp. lactis BB-12,
RT   a widely consumed probiotic strain.";
RL   J. Bacteriol. 192:2467-2468(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; CP001853; ADC85661.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3R4I7; -.
DR   SMR; D3R4I7; -.
DR   STRING; 552531.BIF_01286; -.
DR   EnsemblBacteria; ADC85661; ADC85661; BIF_01286.
DR   KEGG; bbb:BIF_01286; -.
DR   PATRIC; fig|552531.3.peg.1127; -.
DR   eggNOG; COG1222; Bacteria.
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..524
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396965"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          22..59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         250..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   524 AA;  57095 MW;  01B782F24F0C75A5 CRC64;
     MGMGQEKHTD AASQSRDPEA VAAHENDQLR QRNHALAKAL TRATEELRKA KAQLEQFMAP
     PLTMATMVRV HRCSTDEHGV RHASAEILNG NRRQIVPLSP TVNPAQLGSG QGVLLDANMV
     IVDSCETPTT GPMRAVSESL ADGRLIVSDV GGNRGVVMRA SAVARTPINV DDRVVIDPSG
     TYVLSVLPQE QAQDLLLEET PDVSFTDIGG LDEQIARIRD AVQLPFQHRD LFDRFDLKAP
     KGVLLYGPPG NGKTLIAKAI AHELAAGSGN DGVFLSVKGP ELLNKFVGES ERLIRRIFER
     AKELSGAGRP VIVFIDEMDS LLRTRGTGVS SDVETTIVPQ FLTELDGVES LDDVMVIGAS
     NRIDMIDPAV LRPGRLDVKI HVTRPDETAA MAITRHYLTD ALPLEPGRDA DALAASLVRD
     LFRRDESRLL ATLDEQGRRR GIYMADIVSG AMLRNIVDRA KTKAVKAEIL HGSVSRDDEP
     QGITEARIHE AIDDEYEQNR STINETDPGQ WLRINALTLA ADGV