ID   PAN_ARCFU               Reviewed;         398 AA.
AC   O28303;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Proteasome-activating nucleotidase {ECO:0000255|HAMAP-Rule:MF_00553};
DE            Short=PAN {ECO:0000255|HAMAP-Rule:MF_00553};
DE   AltName: Full=Proteasomal ATPase {ECO:0000255|HAMAP-Rule:MF_00553};
DE   AltName: Full=Proteasome regulatory ATPase {ECO:0000255|HAMAP-Rule:MF_00553};
DE   AltName: Full=Proteasome regulatory particle {ECO:0000255|HAMAP-Rule:MF_00553};
GN   Name=pan {ECO:0000255|HAMAP-Rule:MF_00553}; OrderedLocusNames=AF_1976;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-134 OF WILD-TYPE AND MUTANT
RP   ALA-61, FUNCTION AS A CHAPERONE, AND SUBUNIT.
RX   PubMed=19481487; DOI=10.1016/j.molcel.2009.04.030;
RA   Djuranovic S., Hartmann M.D., Habeck M., Ursinus A., Zwickl P., Martin J.,
RA   Lupas A.N., Zeth K.;
RT   "Structure and activity of the N-terminal substrate recognition domains in
RT   proteasomal ATPases.";
RL   Mol. Cell 34:580-590(2009).
CC   -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC       unfolding and translocation of substrate proteins into the archaeal 20S
CC       proteasome core particle. Is essential for opening the gate of the 20S
CC       proteasome via an interaction with its C-terminus, thereby allowing
CC       substrate entry and access to the site of proteolysis. Thus, the C-
CC       termini of the proteasomal ATPase function like a 'key in a lock' to
CC       induce gate opening and therefore regulate proteolysis. Unfolding
CC       activity requires energy from ATP hydrolysis, whereas ATP binding alone
CC       promotes ATPase-20S proteasome association which triggers gate opening,
CC       and supports translocation of unfolded substrates (Probable).
CC       {ECO:0000305|PubMed:19481487}.
CC   -!- SUBUNIT: Homohexamer. The hexameric complex has a two-ring architecture
CC       resembling a top hat that caps the 20S proteasome core at one or both
CC       ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-
CC       rings of the proteasome core by binding to the intersubunit pockets
CC       (Probable). {ECO:0000305|PubMed:19481487}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}.
CC   -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC       domain that may assist in substrate recognition, an interdomain
CC       involved in PAN hexamerization, and a C-terminal ATPase domain of the
CC       AAA type. {ECO:0000255|HAMAP-Rule:MF_00553}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00553}.
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DR   EMBL; AE000782; AAB89280.1; -; Genomic_DNA.
DR   PIR; G69496; G69496.
DR   RefSeq; WP_010879468.1; NC_000917.1.
DR   PDB; 2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=57-134.
DR   PDB; 2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=57-134.
DR   PDB; 6HE4; EM; 4.85 A; H/I/J/K/L/M=123-389.
DR   PDB; 6HE5; EM; 4.12 A; H/I/J/K/L/M=2-398.
DR   PDB; 6HE8; EM; 6.86 A; H/I/J/K/L/M=9-398.
DR   PDB; 6HE9; EM; 6.35 A; H/I/J/K/L/M=9-398.
DR   PDB; 6HEA; EM; 7.04 A; H/I/J/K/L/M=9-398.
DR   PDB; 6HEC; EM; 6.95 A; H/I/J/K/L/M=9-398.
DR   PDB; 6HED; EM; 6.95 A; H/I/J/K/L/M=9-398.
DR   PDBsum; 2WG5; -.
DR   PDBsum; 2WG6; -.
DR   PDBsum; 6HE4; -.
DR   PDBsum; 6HE5; -.
DR   PDBsum; 6HE8; -.
DR   PDBsum; 6HE9; -.
DR   PDBsum; 6HEA; -.
DR   PDBsum; 6HEC; -.
DR   PDBsum; 6HED; -.
DR   AlphaFoldDB; O28303; -.
DR   EMDB; EMD-0209; -.
DR   EMDB; EMD-0210; -.
DR   EMDB; EMD-0212; -.
DR   EMDB; EMD-0213; -.
DR   EMDB; EMD-0214; -.
DR   EMDB; EMD-0215; -.
DR   EMDB; EMD-0216; -.
DR   SMR; O28303; -.
DR   IntAct; O28303; 2.
DR   STRING; 224325.AF_1976; -.
DR   PaxDb; 224325-AF_1976; -.
DR   EnsemblBacteria; AAB89280; AAB89280; AF_1976.
DR   GeneID; 24795719; -.
DR   KEGG; afu:AF_1976; -.
DR   eggNOG; arCOG01306; Archaea.
DR   HOGENOM; CLU_000688_2_0_2; -.
DR   OrthoDB; 77269at2157; -.
DR   PhylomeDB; O28303; -.
DR   BRENDA; 5.6.1.5; 414.
DR   EvolutionaryTrace; O28303; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0022623; C:proteasome-activating nucleotidase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00553; PAN; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR023501; Nucleotidase_PAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR   NCBIfam; TIGR01242; proteasome-activating nucleotidase; 1.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW   Nucleotide-binding; Proteasome; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Proteasome-activating nucleotidase"
FT                   /id="PRO_0000084739"
FT   REGION          396..398
FT                   /note="Docks into pockets in the proteasome alpha-ring to
FT                   cause gate opening"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT   COILED          3..60
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT   BINDING         185..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT   STRAND          63..71
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:2WG5"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:2WG5"
SQ   SEQUENCE   398 AA;  44964 MW;  F3293BB7D6A646B4 CRC64;
     MGDSEIQYLL EKLKKLEEDY YKLRELYRRL EDEKKFIESE RIRYEREVRR LRSEVERLRS
     PPLLVGVVSD ILEDGRVVVK SSTGPKFVVN TSQYINEEEL KPGARVALNQ QTLAIVNVLP
     TSKDPMVYGF EVEEKPEVSY EDIGGLDVQI EEIREAVELP LLKPELFAEV GIEPPKGVLL
     YGPPGTGKTL LAKAVANQTR ATFIRVVGSE FVQKYIGEGA RLVREVFQLA KEKAPSIIFI
     DELDAIAARR TNSDTSGDRE VQRTMMQLLA ELDGFDPRGD VKVIGATNRI DILDPAILRP
     GRFDRIIEVP LPTFEGRIQI FKIHTRKMKL AEDVDFKELA RITEGASGAD IKAICTEAGM
     FAIREERAKV TMLDFTKAIE KVLKKTTPIP DLKGVMFV
//