ID   H6N2J6_GORPV            Unreviewed;       613 AA.
AC   H6N2J6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   03-MAY-2023, entry version 69.
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:AFA73421.1};
GN   OrderedLocusNames=GPOL_c23920 {ECO:0000313|EMBL:AFA73421.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73421.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA73421.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA73421.1; -; Genomic_DNA.
DR   RefSeq; WP_006370155.1; NC_016906.1.
DR   AlphaFoldDB; H6N2J6; -.
DR   STRING; 1112204.GPOL_c23920; -.
DR   EnsemblBacteria; AFA73421; AFA73421; GPOL_c23920.
DR   KEGG; gpo:GPOL_c23920; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   Proteomes; UP000009154; 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   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_C.
DR   InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR   InterPro; IPR022482; Proteasome_ATPase.
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; 1.
DR   Pfam; PF17758; Prot_ATP_OB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   TIGRFAMs; TIGR03689; pup_AAA; 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:AFA73421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          289..445
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          75..106
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT   COMPBIAS        22..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         300..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   613 AA;  67855 MW;  E372625AC7701DFD CRC64;
     MTESDRHEAS VENTGSNDPS ESTHARDVDP ARTRDVDAGE TFTPAYTPPL AAARAERERS
     AFTRASDPKD LQDRVDNLTA RNAKLLETLK EARQQLVALR EEVDRLGQPP SGYGVLLEIH
     PDQTVDVFTS GRKMRLTCSP NIDTEVLHKG QTLRLNEALT IVEACDFDSV GEISTLREVL
     GDGNRALVVG HADEERVVWL AEPLRGEVDG EDGKRRKLRP GDSLLIDTKA GFAFERVPKA
     EVEDLVLEEV PDVGYEDIGG LGRQIEQIRD AVELPFLHKD LFRDYALRPP KGVLLYGPPG
     CGKTLIAKAV ANSLAKKIAQ VRGDDAKEAK SYFLNIKGPE LLNKFVGETE RHIRLIFQRA
     REKASEGTPV IVFFDEMDSI FRTRGSGVSS DVETTVVPQL LSEIDGVEGL ENVIVIGASN
     REDMIDPAIL RPGRLDVKIK IERPDAESAI DIFSKYLTES LPVHADDLGE FGGDRTACVN
     AMIEKVVERM YAESDENRFL EVTYANGDKE VMYFKDFNSG AMIQNVVDRA KKYAIKSQLD
     TGAPGLRVQH LFDSILDEFA ENEDLPNTTN PDDWARISGK KGERIVYIRT LVTGKSSGAS
     RAIDTETNTG QYL
//