ID A0A1H1U7L8_9ACTN Unreviewed; 581 AA.
AC A0A1H1U7L8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN04488543_2188 {ECO:0000313|EMBL:SDS68434.1};
OS Friedmanniella luteola.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Friedmanniella.
OX NCBI_TaxID=546871 {ECO:0000313|EMBL:SDS68434.1, ECO:0000313|Proteomes:UP000199092};
RN [1] {ECO:0000313|EMBL:SDS68434.1, ECO:0000313|Proteomes:UP000199092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21741 {ECO:0000313|EMBL:SDS68434.1,
RC ECO:0000313|Proteomes:UP000199092};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|HAMAP-Rule:MF_02112,
CC ECO:0000256|RuleBase:RU003651}.
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DR EMBL; LT629749; SDS68434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1U7L8; -.
DR STRING; 546871.SAMN04488543_2188; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000199092; Chromosome i.
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 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: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|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}; Proteasome {ECO:0000313|EMBL:SDS68434.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199092}.
FT DOMAIN 259..412
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 12..81
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 270..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 581 AA; 64322 MW; 2A833415A96B1284 CRC64;
MTGPVHDRPE ERGALVAQIS ALSEELTRLR ERLSSHPHDI AVLERRLADA RQDARSTAAN
NERLASTLRE ARDQIVTLKT EVDRLAQPPA SFGIFLADTG ENTADIYTSG RKMRVSVSPE
VDLGTVTPGR EVMINEAMNV VAALDFDEVG EVVLLKEVMD GGDRALVVGH GDEESVVRLA
QRLRDEKLRS GDSLLIDRRV HFAYERVPKM DVEELVLEEV PDIDYSVIGG LSGQIEAIRD
AVELPYLHKE LFAEHELKAP KGILLYGPPG CGKTLIAKAV ANSLAKKVTE RTGQEGRSFF
LNIKGPELLN KYVGETERHI RLVFQRARDK ASDGMPVIVF FDEMDSLFRT RGTGVSSDVE
NTIVPQLLSE IDGVEGLDNV IIIGASNRED MIDPAILRPG RLDVKIKIER PDVEAAREIF
SKYLTPTLPL HPEDLAEFGG NRGATVAGMI DRTVQRMYEE SEENQFLEVT YAGGDKEVLY
FKDFNSGAMI QNIVDRAKKM AIKDLLDAGV RGLRIGHLLQ ACLDEFAENE DLPNTTNPDD
WAKISGKKGE RIVFIRTLIS SNKGTQPGRS IDTVSNTGQY L
//