ARC_BIFA0
ID ARC_BIFA0 Reviewed; 522 AA.
AC B8DTX4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, 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=BLA_1165;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(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; CP001213; ACL29453.1; -; Genomic_DNA.
DR RefSeq; WP_004218902.1; NC_011835.1.
DR AlphaFoldDB; B8DTX4; -.
DR SMR; B8DTX4; -.
DR STRING; 442563.BLA_1165; -.
DR EnsemblBacteria; ACL29453; ACL29453; BLA_1165.
DR GeneID; 66532990; -.
DR KEGG; bla:BLA_1165; -.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR Proteomes; UP000002456; 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; -; 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; Reference proteome.
FT CHAIN 1..522
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396964"
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
