ID L0HFJ9_METFS Unreviewed; 436 AA.
AC L0HFJ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=Metfor_1538 {ECO:0000313|EMBL:AGB02571.1};
OS Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB02571.1, ECO:0000313|Proteomes:UP000010824};
RN [1] {ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA Liu W.-T., Woyke T.;
RT "Complete sequence of Methanoregula formicicum SMSP.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB02571.1, ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RX PubMed=25189582;
RA Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT Sludge Blanket Reactor.";
RL Genome Announc. 2:e00870-14(2014).
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; CP003167; AGB02571.1; -; Genomic_DNA.
DR AlphaFoldDB; L0HFJ9; -.
DR STRING; 593750.Metfor_1538; -.
DR KEGG; mfo:Metfor_1538; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_1_2; -.
DR InParanoid; L0HFJ9; -.
DR Proteomes; UP000010824; 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 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|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00553}; Cytoplasm {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}; Reference proteome {ECO:0000313|Proteomes:UP000010824}.
FT DOMAIN 211..350
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 25..91
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 222..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 436 AA; 48793 MW; C8A8CDFA595C224B CRC64;
MSDTIHQSPE PQTPEELYRL YRTLSEQLRE QLAQIEGDKH DLEVQMMERV GNLESRNLEL
REQLRQIEAD KRYIETQKIR YEREVRKLKS ESEQLRSPPL IIGTVTDIVD ANRVIVRSSA
GPRFLVRSSP SISADDLKPG VRCTLNQQSL AIVELLPSSF DAQVYGMELV DSPQENYMDI
GGLEQQINEI KEAVELPLKR PELFERIGVE PPKGVLLHGP PGTGKTLLAK AVAHETNAHF
MRVVGSELVQ KYIGEGARLV RELFDLAKKK APTIIFIDEI DAVGASRTEA NTSGDREVQR
TLMQLLAGMD GFENRGDVKI IGATNRIDIL DKALLRPGRF DRIIEIPLPD EKGRLSILKV
HCRSLTVDEG VNLAEVARLT EGKNGADLRA ICMEAGMFAI RKERSAITQE DFLSAIEKVG
LDFHRGLPGT EGVMFA
//
