PAN_ARCFU
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 03-AUG-2022, entry version 130.
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 SMR; O28303; -.
DR IntAct; O28303; 2.
DR STRING; 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 OMA; YNMTTFE; -.
DR OrthoDB; 30571at2157; -.
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:0036402; F:proteasome-activating activity; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00553; PAN; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
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_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 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
