ID A0A2M8W3H3_9MICO Unreviewed; 567 AA.
AC A0A2M8W3H3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CLV34_2999 {ECO:0000313|EMBL:PJI85486.1};
OS Luteimicrobium subarcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI85486.1, ECO:0000313|Proteomes:UP000231586};
RN [1] {ECO:0000313|EMBL:PJI85486.1, ECO:0000313|Proteomes:UP000231586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI85486.1,
RC ECO:0000313|Proteomes:UP000231586};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJI85486.1}.
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DR EMBL; PGTZ01000012; PJI85486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8W3H3; -.
DR Proteomes; UP000231586; Unassembled WGS sequence.
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; 1.20.5.170; -; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:PJI85486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231586}.
FT DOMAIN 230..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 241..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 567 AA; 61760 MW; 68F67A6AA578DDBF CRC64;
MTDAPYRDPY RPERGEDRRD QQLALLAAKN ERLVGALTAA RDQIVELKRQ IDELAKPPGT
YAVFVAAHAD GGVDIMSAGR KMHVGASPAL DLASLRPGQE VKLNEAMTVV EAGAYEVTGE
LVTVKELLGA DRVLVVGRAD EERVVRLAGS LVAQGADTVR VGDSLTVDTR AGFVYERIPK
SDVEELVLEE VPDIGYADIG GLGPQIDQIR DAVELPFSHP DLFREHGLRP PKGVLLYGPP
GCGKTLIAKA VASSLAQMVA DRREAEGGES VPATAEGASV RSYFLNVKGP ELLNKYVGET
ERHIRLIFAR AREKASQGIP VVVFFDEMES LFRTRGTGLS SDVETTIVPQ LLAEIDGVER
LDNVIVIGAS NREDMIDPAI LRPGRLDVKI RIERPDAEGA EEIFGKYLTT DLPIHADDLA
EHGGDRAAAV DAMIAAVVER IYSESDENRF LEVTYASGDK EVLYFKDFNS GAMIQNIVDR
AKKSAIKDLL ATGQRGLRVE HLLAACVDEF KENEDLPNTT NPDDWARISG KKGERIVFIR
TIVQNKDGQG SKAARTIDTV TNTGQYL
//
