ID D5U343_THEAM Unreviewed; 404 AA.
AC D5U343;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=Tagg_1280 {ECO:0000313|EMBL:ADG91543.1};
OS Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermosphaera.
OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG91543.1, ECO:0000313|Proteomes:UP000002376};
RN [1] {ECO:0000313|EMBL:ADG91543.1, ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX PubMed=21304709;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [2] {ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX DOI=10.4056/sigs.821804;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain
RT (M11TLT).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11486;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001939; ADG91543.1; -; Genomic_DNA.
DR RefSeq; WP_013130136.1; NC_014160.1.
DR AlphaFoldDB; D5U343; -.
DR STRING; 633148.Tagg_1280; -.
DR GeneID; 9166325; -.
DR KEGG; tag:Tagg_1280; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OrthoDB; 77269at2157; -.
DR Proteomes; UP000002376; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW ECO:0000256|RuleBase:RU003651};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00553};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00553};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00553};
KW Hydrolase {ECO:0000313|EMBL:ADG91543.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000002376}.
FT DOMAIN 168..307
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 14..48
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 179..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 404 AA; 45158 MW; 60DF8A45BF08B982 CRC64;
MSSEIENLDR LDVVVNEEDY IRYLENKIKT LENERKNLLL KLNYYRSELD KLLASPLIEA
IVENVLQDGK VVVKSSTGPT LVVTVSDSVD KSKIVPGARV ALNQRGSTIV EVLPEYVDAL
VQSMEVIEKP SVKYEDIGGL SEQIRELREV VELPLKNPEL FQEVGIEPPK GVLLYGPPGC
GKTMLAKAVA SEAGATFISI VGSELVQKFI GEGARIVREL FAYARRKAPA IIFIDEIDAI
AAKRIDIGTS GEREVQRTLM QLLAELDGFK PLDRIKVIAA TNRIDILDPA ILRPGRLDRL
IEVPLPDLNG RLEILRIHTR RMKLDSDVDL KAIAKATQGF SGAELKAVVT EAGYNAIREN
RKVVSMSDFQ RAVEKVKSKK QYRRVDEFSP EVKDKGEYVK YVYQ
//
