ID A0A7T0PXT7_9ACTO Unreviewed; 542 AA.
AC A0A7T0PXT7;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 19.
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:QPL06170.1};
GN ORFNames=ID810_04430 {ECO:0000313|EMBL:QPL06170.1};
OS Actinomyces respiraculi.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Actinomycetales;
OC Actinomycetaceae; Actinomyces.
OX NCBI_TaxID=2744574 {ECO:0000313|EMBL:QPL06170.1, ECO:0000313|Proteomes:UP000594637};
RN [1] {ECO:0000313|EMBL:QPL06170.1, ECO:0000313|Proteomes:UP000594637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ750 {ECO:0000313|EMBL:QPL06170.1,
RC ECO:0000313|Proteomes:UP000594637};
RA Zhou J.;
RT "Actinomyces sp. ZJ750.";
RL Submitted (NOV-2020) 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; CP063989; QPL06170.1; -; Genomic_DNA.
DR RefSeq; WP_166855482.1; NZ_CP063989.1.
DR AlphaFoldDB; A0A7T0PXT7; -.
DR KEGG; arep:ID810_04430; -.
DR Proteomes; UP000594637; 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:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR FunFam; 3.40.50.300:FF:001025; ATPase family, AAA domain-containing 2B; 1.
DR Gene3D; 1.10.8.60; -; 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; IPR050168; AAA_ATPase_domain.
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:SF144; PROTEASOME-ASSOCIATED ATPASE; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02112}; Proteasome {ECO:0000313|EMBL:QPL06170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000594637}.
FT DOMAIN 244..391
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..66
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT COMPBIAS 1..11
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 542 AA; 58701 MW; AE36E54A06828B44 CRC64;
MEEQPVGHRE PASGVQTIST VSNADTDVRD RLRELTEQAG VLNRKNASLA NALRAARQEL
AALHEDVKAL QLPPLAHATV LAVDATERTA DVSIAGRRHR VGVGPAVVAS SLHPGDDVVL
NEHLVITTTC PSPRFGEVVT VKETYDDGTV LVLARHDEEQ VLTLSATLTD HRPRVGDALV
ADLAVRMALR PVVRSEVEEL VLEEVPDVGY GDIGGLGEQI ELIRDAVELP FLHPDLYREH
RLTPPRGVLL YGPPGCGKTL IAKAVAASLS AGGRGEAYFL NIKGPQLLDK YVGETERRIR
VIFARAREKA ATGVPVVIFF DEMDSLFRTR GSGRSSDVET TVVPQMLAEI DGVDELDNVV
VIGATNREDM IDPAILRPGR LDVKIRIGRP DRNGAAEILA TYLTPDLPIS EELLDARGGA
QGAVDALIEQ VVATLYTRRR ATEMVELTHA DGQVEVLHVA DLVSGAMLAN IVDRAKKAAV
KDLVTSGRRG LTQEHLRCAV IDEIVENEGL PATVHPDDWA RVSGRRGTPV VSMSVLQRDR
EE
//
