ID A0A0P0SK65_9PSEU Unreviewed; 593 AA.
AC A0A0P0SK65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=AD017_26545 {ECO:0000313|EMBL:ALL85085.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL85085.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL85085.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL85085.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL85085.1; -; Genomic_DNA.
DR RefSeq; WP_060576630.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SK65; -.
DR STRING; 1096856.AD017_26545; -.
DR KEGG; pecq:AD017_26545; -.
DR PATRIC; fig|1096856.3.peg.5599; -.
DR Proteomes; UP000066228; 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; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT DOMAIN 269..425
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 37..78
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 280..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 593 AA; 65536 MW; 29CA0F57A8BD40A4 CRC64;
MQSGHDLGPA ETAEHIRHLE SEIATLRQRL TETPRHARVL EQRLAETTSR LSALNARNEK
LTETLKEARG QLVALREEVD RLAQPPSGYG VFLGRYDDDT VDVFTSGRRM RVPVSPAVEG
EQLRSGQSVR LNEALTVVEA MGFEQVGDLY SLREIVSKPG DDGSAGRGLV VGHSDEERVV
WLAAPLFDLG DEEGTSPLKS GDSLMVDSRA GYAYERVAKA EVEDLVLEEV PDIAYHDIGG
LSRQIEQIQD AVELPFLHTE LFTTYELRPP KGVLLYGPPG CGKTLIAKAV ANSLAKKIAK
QRGDDPDEGR AFFLNIKGPE LLNKFVGETE RHIRLIFQRA REKASAGTPV IVFFDEMDSI
FRTRGSGVSS DVETTIVPQL LAEIDGVEGL ENVIVIGASN REDMIDPAIL RPGRLDVKIK
IERPDAEGAQ DIFSKYITET LPIHDDDVAE FGGSRKACVD GMIQRIVERM YDESEENRFL
EVTYANGDKE TLYFKDFNSG AMIQNIVDRA KKSAIKSVLE SGQTGLRVQH LLDAIVDEFA
ENEDLPNTTN PDDWARISGK KGERIVYIRT LVTGKNEATG RAIDTASNTG QYL
//
