PAN_METHJ
ID PAN_METHJ Reviewed; 412 AA.
AC Q2FQ56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Mhun_1038;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00553}.
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 {ECO:0000255|HAMAP-Rule:MF_00553}.
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; CP000254; ABD40788.1; -; Genomic_DNA.
DR RefSeq; WP_011448067.1; NC_007796.1.
DR AlphaFoldDB; Q2FQ56; -.
DR SMR; Q2FQ56; -.
DR STRING; 323259.Mhun_1038; -.
DR EnsemblBacteria; ABD40788; ABD40788; Mhun_1038.
DR GeneID; 3924751; -.
DR KEGG; mhu:Mhun_1038; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OMA; YNMTTFE; -.
DR OrthoDB; 30571at2157; -.
DR Proteomes; UP000001941; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Proteasome; Reference proteome.
FT CHAIN 1..412
FT /note="Proteasome-activating nucleotidase"
FT /id="PRO_1000017921"
FT REGION 410..412
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 18..72
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 197..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
SQ SEQUENCE 412 AA; 46218 MW; C93F84A0B4E8E9E4 CRC64;
MAEAARHPDD MKTPDELYRY LVDRVAGMES QNQELKEQIR QLESDKRYIE TQKIRYEREV
RKLKSEIEHL KTPPLIVGTI TDIIDSGRVV VRSSAGPRFL VRVSQAVNPT TLKAGVRCTL
NQQSLAIVEV LPSTYDSQVY GMELVDAPTE TYEDIGGLEK QIMEIREAVE LPMTRPDLFE
KIGINPPKGV LLYGPPGTGK TLLAKAVAHE THAIFLHTVG SELVQKYIGE GARLVRELFD
LAKEKAPSIV FIDEIDAIGA SRTEAMTSGD REVQRTLMQL LAAMDGFEPR GDVKIIGATN
RIDILDAALL RPGRFDRIIE IPLPDTEGRY SILKVHTRCM NLSEDVDLME VARLTEGRNG
AELNAICMEA GMFAIRKEHP QVDQEDFLTA LNKFRCDFER DHRLTTAGVM FA
