ID A0A075LTJ6_9EURY Unreviewed; 399 AA.
AC A0A075LTJ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Proteasome-activating nucleotidase {ECO:0000256|HAMAP-Rule:MF_00553};
DE Short=PAN {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasomal ATPase {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory ATPase {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory particle {ECO:0000256|HAMAP-Rule:MF_00553};
GN Name=pan {ECO:0000256|HAMAP-Rule:MF_00553};
GN ORFNames=PAP_08420 {ECO:0000313|EMBL:AIF70070.1};
OS Palaeococcus pacificus DY20341.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Palaeococcus.
OX NCBI_TaxID=1343739 {ECO:0000313|EMBL:AIF70070.1, ECO:0000313|Proteomes:UP000027981};
RN [1] {ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|Proteomes:UP000027981};
RA Zeng X., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Palaeococcus pacificus
RT DY20341T, Isolated from a Deep-Sea Hydrothermal Sediments.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIF70070.1, ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|EMBL:AIF70070.1,
RC ECO:0000313|Proteomes:UP000027981};
RX PubMed=26383653;
RA Zeng X., Jebbar M., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Piezophilic Archaeon
RT Palaeococcus pacificus DY20341T, Isolated from Deep-Sea Hydrothermal
RT Sediments.";
RL Genome Announc. 3:e01080-e01015(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_00553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00553}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|HAMAP-Rule:MF_00553,
CC ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP006019; AIF70070.1; -; Genomic_DNA.
DR RefSeq; WP_048165562.1; NZ_CP006019.1.
DR AlphaFoldDB; A0A075LTJ6; -.
DR STRING; 1343739.PAP_08420; -.
DR GeneID; 24842786; -.
DR KEGG; ppac:PAP_08420; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OrthoDB; 77269at2157; -.
DR Proteomes; UP000027981; 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; cd00890; Prefoldin; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW ECO:0000256|RuleBase:RU003651};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00553};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00553};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00553};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_00553}.
FT DOMAIN 173..312
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 19..60
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 184..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 399 AA; 45080 MW; 532DF8EF2008459B CRC64;
MSFEDDVKFE REETYDDYVI YLKRRIRQLE LQVRTLEADK ERLERELSRL RMEMSRMKQP
PAFAGTLIEM LDDERAIVQN FNGPRFVVRI APWIEREKLK PGSRVALDQR TMAVIELLPS
QKDPSVLGFE VIDKPRVSYS DIGGLKKQMH ELREAVELPL KHPDLFEKIG IDPPKGVLLY
GPPGCGKTLM AKAVAKEVNA TFIRVVGSEL VRKYIGEGAR LVGELFELAR EKAPTIIFID
EIDAIGAKRM DETTGGEREV NRTLMQLLAE LDGFDPRGNV KVIAATNRPD ILDPALLRPG
RFDRLIEVPL PDFVGRLEIL KVHTRKMNLK DVDLKAIAEM TDGASGADLK AIVTEAGMFA
IRARRGYIKH EDFIKAVEKV IGGEQKLAQQ IAAHEVIYG
//
