ID   ARC_BIFLS               Reviewed;         521 AA.
AC   B7GUP3; E8MMK5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   OrderedLocusNames=Blon_2128, BLIJ_2205;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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; CP001095; ACJ53189.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ69782.1; -; Genomic_DNA.
DR   RefSeq; WP_012578393.1; NZ_JDTT01000015.1.
DR   AlphaFoldDB; B7GUP3; -.
DR   SMR; B7GUP3; -.
DR   PRIDE; B7GUP3; -.
DR   EnsemblBacteria; ACJ53189; ACJ53189; Blon_2128.
DR   KEGG; bln:Blon_2128; -.
DR   KEGG; blon:BLIJ_2205; -.
DR   PATRIC; fig|391904.8.peg.2207; -.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   BRENDA; 5.6.1.5; 849.
DR   Proteomes; UP000001360; 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.
FT   CHAIN           1..521
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396971"
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;  56539 MW;  6E3403CE9951EC0D CRC64;
     MSDTEDLAAL NDRLMAKNHA LAEALNRAGK ELTKAKSRLA QLAQPPLTFA TMVKVDSTRT
     DADGIQHASA EVISGTRRMV VPVASNVNAA RLTAGATVML NEKLVLVEQR DADTVGQIRS
     VKQVLDDGRL IVTDASGNPV LIRRSGALAY ADINQGDRII VDPSVRLAIE ALPAEGDKDL
     VLEETPDVTF ADIGGLDSEI GRIRDAVQLP FRHRALFERY DLKPPKGVLL YGPPGNGKTM
     IAKAVANALC EGGYDSNGDG SISPAETRVK GVFLSVKGPE LLNKYVGESE RLIRLIFQRA
     RERAADGNPV VVFIDEMDSL LRTRGSGVSS DVETTIVPQF LSELDGVESL DNVMVIGASN
     RVDMIDPAVL RPGRLDVKIR VGRPKTNQAI AIVDHYLTDD LPLENGVDAH ALSAVLVHDI
     YGTSERRHLC DVQEENGQWH ALFLADVVSG AMLKNIVDRA KTRAVKESIE TGSDVALTVP
     LLAAAVEDEY RETRDSMADV DPEQWSRING MDPIRRIRTA E