ARC_BIFAA
ID ARC_BIFAA Reviewed; 515 AA.
AC A1A0U4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=BAD_0546;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF39327.1; -; Genomic_DNA.
DR RefSeq; WP_011742988.1; NC_008618.1.
DR AlphaFoldDB; A1A0U4; -.
DR SMR; A1A0U4; -.
DR STRING; 1680.BADO_0559; -.
DR EnsemblBacteria; BAF39327; BAF39327; BAD_0546.
DR KEGG; bad:BAD_0546; -.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR Proteomes; UP000008702; 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..515
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396963"
FT COILED 2..49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 240..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 515 AA; 55781 MW; E4DD0E81A0F6A054 CRC64;
MNDHDEETLA SLQQANDQLM AKNHALVKAL SRATQEMTKT KAQLNQLAGP PMTFATMVRV
HSAKTDGQGV QHASAEVAAG ARRMIVPIAA NLQASRLEPG RTVLLNENMV VVSQLDTDTL
GAVRSVRQVC DDGRLLVADG GGNVTLVRCS GTLAKQAISA GDRVNVDASL RFALSLVPPE
NDDDLVLEEV PDVTFADIGG LDEQIERIRD AVQMPFQHRE LFERYDLKPP KGVLLYGPPG
NGKTLIAKAV ANALAEGTDA GSGVFLSVKG PELLNKFVGE SERLIRMIFK RARERAADGK
PVIVFIDEMD SLLRTRGTGV SSDVETTIVP QFLTELDGVE SLDNVMVIGA SNRIDMIDPA
VLRPGRLDVK IRVDRPGIQQ ATQIVRHYLT DKLPLSPNVD AKALIGVLVN DIYAQDEHRH
LCDICDDHGQ WRPVYLADVV SGAVLKNIVD RAKTYAVKLS ITTGQAAAIG INLLAKAVDE
EYGETRDALL DADPEQWSRI NGLEPGRVTG IRPVA