ID A0A1U6HPH7_9MICC Unreviewed; 583 AA.
AC A0A1U6HPH7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN06272721_102265 {ECO:0000313|EMBL:SLJ97686.1};
OS Arthrobacter sp. P2b.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1938741 {ECO:0000313|EMBL:SLJ97686.1, ECO:0000313|Proteomes:UP000189995};
RN [1] {ECO:0000313|EMBL:SLJ97686.1, ECO:0000313|Proteomes:UP000189995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P2b {ECO:0000313|EMBL:SLJ97686.1,
RC ECO:0000313|Proteomes:UP000189995};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FVZL01000002; SLJ97686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U6HPH7; -.
DR STRING; 1938741.SAMN06272721_102265; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000189995; 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, 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:SLJ97686.1}.
FT DOMAIN 260..414
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 583 AA; 64196 MW; 9ABC3CD9BCA309F3 CRC64;
METPNQDSGR TPAEHSAAND LSVADRQVNI LRDKLRHIDR QLAAATQNNT KLVSMLETAK
AEILRLKNAL DQEGQPPYSF GTILQLNPKR PPSPGSSGQA ATEESVDIFN AGRKMRVGIS
PLVNINQLAV GQEVLLNEAL LIVAGLGYER AGELATLKEM LGADRALVVG RADEERVVRL
SGALLTEKLR VGDALSIDSR TGYALEKVPR SEVENLVLEE VPDITYEDIG GLGPQIEQIR
DAVELPFLHP DLYREHGLKA PKGILLYGPP GCGKTLIAKA VANSLAARAA ERSGNVDLKS
YFLNIKGPEL LDKYVGETER HIRLIFSRAR EKASDGSPVV VFFDEMDSLF RTRGTGISSD
VETTIVPQLL SEIDGVERLD NVIVIGASNR EDMIDPAILR PGRLDVKVKI HRPDAEAAAD
IFNKYITPDL PFHESDLAEH DGDVQATVDA MVQRTVEAMY STDKSNEFLE VTYANGDTEM
LYFKDFNSGA VVQNVVDRAK KYAIKDLLTT QQKGLRIEHL LRAVVDEFRE HEDMPNTTNP
DDWARISGKK GERITYIRTI VQGKAGQEPG KSIETMPTTG QYL
//
