PAN_METMJ
ID PAN_METMJ Reviewed; 412 AA.
AC A3CV35;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Memar_1305;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(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. {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; CP000562; ABN57235.1; -; Genomic_DNA.
DR RefSeq; WP_011844146.1; NC_009051.1.
DR AlphaFoldDB; A3CV35; -.
DR SMR; A3CV35; -.
DR STRING; 368407.Memar_1305; -.
DR EnsemblBacteria; ABN57235; ABN57235; Memar_1305.
DR GeneID; 4847412; -.
DR KEGG; mem:Memar_1305; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OMA; YNMTTFE; -.
DR OrthoDB; 30571at2157; -.
DR Proteomes; UP000002146; 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.
FT CHAIN 1..412
FT /note="Proteasome-activating nucleotidase"
FT /id="PRO_1000017924"
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 15..73
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; 46681 MW; 81EAB15811455757 CRC64;
MGDIARQAPD KDTGEDIYQY LLERITNLEN RNLELREQFR QMESEKRYVE TQKIRYEREL
RKLKSEIEQL RSPPLVIGTV TDVIDNSRVI VRSSAGPRFL VRTSQLIDPD LLKPGVRCTL
NQQSLAIVDV LPTSYDAQIY GMELVESPEE TYENIGGLEP QIEEIREAVE LPLTKPQLFE
KVGISPPKGV LLYGPPGTGK TLLARAVAHQ TNAHFLRVVG SELVQKYIGE GARLVRELFD
LAKQRAPSII FIDEIDAIGA HRNDSTTSGD REVQRTLMQL LAEMDGFDNR GDVKIVAATN
RIDILDRALL RPGRFDRMIE IPLPDHQGRL AILKIHTQYM NIGEDVNLSE VSRLTEGKNG
ADLRAICMEA GMFAIRMERD AVNSEDFMKA IDKLALDFDR HHFHTTFGEM FA
