ARC_ROTMD
ID ARC_ROTMD Reviewed; 608 AA.
AC D2NT89;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 57.
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=RMDY18_10330;
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX NCBI_TaxID=680646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18;
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAI64865.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP011540; BAI64865.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044150438.1; NC_013715.1.
DR AlphaFoldDB; D2NT89; -.
DR SMR; D2NT89; -.
DR STRING; 680646.RMDY18_10330; -.
DR EnsemblBacteria; BAI64865; BAI64865; RMDY18_10330.
DR KEGG; rmu:RMDY18_10330; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR Proteomes; UP000001883; 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..608
FT /note="AAA ATPase forming ring-shaped complexes"
FT /id="PRO_0000397015"
FT COILED 45..79
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 302..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 608 AA; 64970 MW; 4A0B42A3078D293D CRC64;
MSTHESADQA GTPQYGTAHS AASAAPHYSA AFGATSLPGS QPVSAQEYDA VLRRLSAAEA
TRDNMSRQIR GAGEKNRKLV EAITSMRYQV ERLRASLSQN VMPPLNSAIV LAVHEGQTMT
YEQVADDKTP AEIDTYLDVQ VSGRMMRIPV SPLIDLSTLT PGMTVLLNDK TEAVLALDTE
PFGDVVTVRE VLDEQRVLVD TSSGAQQVAR VAGSLNIEQL RTGDAVTLDT RTRMLTSQVP
ASRSQELVLE EIPDVTYEQI GGLGAQIEQI RDAVELPYLH PEIFERYHLA PPKGILLYGP
PGNGKTMIAK AVANSLAARA AALNPGSATR GYFLNIKGPE LLDKFVGETE RQIRDIFVAA
REKAEAGHPV VVFFDEMESL FRMRGSGRSS DIETTIVPQL LAEIDGVESL QNVIVIGATN
REDLIDAAVM RPGRLDLKIR INRPDAAGAA EIFGLYLTED LPLDATEVAA AGSTRAALTA
MIAAAAGQLY ARTPSTAYAV ATVDSSMVVG SGASANLSTH TLYRGDFASG AVIRNIVDRA
KKAAIKEQLQ ALTAGADASS VGIGTRHLLE AVRAEFEDQV DLPPLPDIED ALTVAGVRGR
LVSVEPPR
