ID A0A059MQ16_9NOCA Unreviewed; 591 AA.
AC A0A059MQ16;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000256|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000256|HAMAP-Rule:MF_02112};
GN Name=arc {ECO:0000256|HAMAP-Rule:MF_02112,
GN ECO:0000313|EMBL:UYF91881.1};
GN ORFNames=OCS65_15225 {ECO:0000313|EMBL:UYF91881.1};
OS Rhodococcus aetherivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=191292 {ECO:0000313|EMBL:UYF91881.1, ECO:0000313|Proteomes:UP001163947};
RN [1] {ECO:0000313|EMBL:UYF91881.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N1 {ECO:0000313|EMBL:UYF91881.1};
RA Jiang W.;
RT "The genome sequence of Rhodococcus aetherivorans N1.";
RL Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
CC {ECO:0000256|HAMAP-Rule:MF_02112}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000256|HAMAP-
CC Rule:MF_02112, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP106982; UYF91881.1; -; Genomic_DNA.
DR RefSeq; WP_029543755.1; NZ_JACCFD010000002.1.
DR GeneID; 83621796; -.
DR Proteomes; UP001163947; Chromosome.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_2nd.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR NCBIfam; TIGR03689; pup_AAA; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR Pfam; PF17758; Prot_ATP_ID_OB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02112}; Isomerase {ECO:0000313|EMBL:UYF91881.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:UYF91881.1}.
FT COILED 9..71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 591 AA; 64968 MW; DCE5AE1E8E6A4CA6 CRC64;
MSSTENPDSV AAAQELEALR AEATALRRRL VEPSEQVRDL EARIDSLTVR NGKLMDTLKE
ARQQLITLRE EVDRLGQPPS GYGVLLGIYD DQTVDVFTSG RKMRVTVSPN LEPDGFVSGQ
TVRLNEALTV VEAGGFERVG EITTLREVLD DGTRALVVGH ADEERIVWLA APLAAAAAAA
AGTVEVSEDA EPSFKLRPGD SLLVDSKAGY AFERIPKAEV EDLVLEEVPD VDYNDIGGLG
RQIEQIRDAV ELPFLHKDLF REYALRPPKG VLLYGPPGCG KTLIAKAVAN SLAKKIAEAR
GEDSKEAKSY FLNIKGPELL NKFVGETERH IRLIFQRARE KASEGTPVIV FFDEMDSIFR
TRGSGVSSDV ETTVVPQLLS EIDGVEGLEN VIVIGASNRE DMIDPAILRP GRLDVKIKIE
RPDAEAALDI FSKYLTEGLP VHADDLAEFG GHRGACVRAM IERVVDRMYA ESEENRFLEV
TYANGDKEVL YFKDFNSGAM IQNIVDRAKK YAIKSVLETG APGLRVQHLL DSIVDEFAEN
EDLPNTTNPD DWARISGKKG ERIVYIRTLV TGKNASASRA IDTESNTGQY L
//
