ARC_BRAFD
ID ARC_BRAFD Reviewed; 533 AA.
AC C7MCZ0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Bfae_16200;
OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; Brachybacterium.
OX NCBI_TaxID=446465;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 / NCIMB
RC 9860 / 6-10;
RX PubMed=21304631; DOI=10.4056/sigs.492;
RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachybacterium faecium type strain
RT (Schefferle 6-10).";
RL Stand. Genomic Sci. 1:3-11(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; CP001643; ACU85447.1; -; Genomic_DNA.
DR RefSeq; WP_015775656.1; NC_013172.1.
DR RefSeq; YP_003155037.1; NC_013172.1.
DR AlphaFoldDB; C7MCZ0; -.
DR SMR; C7MCZ0; -.
DR STRING; 446465.Bfae_16200; -.
DR EnsemblBacteria; ACU85447; ACU85447; Bfae_16200.
DR KEGG; bfa:Bfae_16200; -.
DR PATRIC; fig|446465.5.peg.1613; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR Proteomes; UP000001919; 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..533
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000396972"
FT COILED 1..42
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 226..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 533 AA; 57839 MW; AFAF48CABEB4E08C CRC64;
MKTYAEMTAE LEQLAAHNDR LTAGLRSARA QIVELKSDLE RVGDPPNSYA TYLRRCEGTT
IDVLHHGRRL RVATAASLDL DSLTPGAELR LNESLAAVEA VPPSDAGNVV PVVEALADSR
LLVAVAPDDT RVLRRAGSLT TEQLHPGDHV LVDLKSQLVL ERIDRAEITD LVLEQVPDVA
FDQIGGLGEQ IEAIRDAVEL PFLQQDLYRT YGLRPPQGVL LYGPPGCGKT MIAKAVAHEL
VLRSAEVRGV SVAEALENSA FLNVKGPELL NKYVGETERS IRLVFERARE KAAADHPVVI
FFDEMEALFR TRGTGLSSDV ETTIVPQLLA EIDGVEGLDN VIVIGASNRE DMIDPAILRP
GRLDVKIRVR RPNLRAGREI LGLYLDDAVP VREDREELLD LAAREIYDES PASAFVRVEY
SDGGSDTLHF RDFVSGATLR NIVDRAKKLA VKDQLATGEV GVAAQHLRDA ITTEFVENED
MPSAAHPEDW ARVSGLPGGG RRRVDAVVPL QGRTLTTPDI AGTAAAGEDG ATA