PAN2_HALVD
ID PAN2_HALVD Reviewed; 412 AA.
AC Q5UT56;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Proteasome-activating nucleotidase 2 {ECO:0000255|HAMAP-Rule:MF_00553};
DE Short=PAN 2 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasomal ATPase 2 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory ATPase 2 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory particle 2 {ECO:0000255|HAMAP-Rule:MF_00553};
GN Name=pan2 {ECO:0000255|HAMAP-Rule:MF_00553}; Synonyms=panB;
GN OrderedLocusNames=HVO_1957;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=15516591; DOI=10.1128/jb.186.22.7763-7772.2004;
RA Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.;
RT "Differential regulation of the PanA and PanB proteasome-activating
RT nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax
RT volcanii.";
RL J. Bacteriol. 186:7763-7772(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=18931121; DOI=10.1128/jb.01180-08;
RA Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.;
RT "Proteasomal components required for cell growth and stress responses in
RT the haloarchaeon Haloferax volcanii.";
RL J. Bacteriol. 190:8096-8105(2008).
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 -!- INDUCTION: Up-regulated at mRNA and protein levels during transition
CC from exponential to stationary phase. {ECO:0000269|PubMed:15516591}.
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 -!- DISRUPTION PHENOTYPE: Strains lacking panB gene alone display
CC relatively normal growth rate and overall cell yield. Moreover, strains
CC lackings both panA and panB still show robust growth, demonstrating
CC that the PAN proteins are not essential. {ECO:0000269|PubMed:18931121}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00553}.
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DR EMBL; AY627304; AAV38127.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04575.1; -; Genomic_DNA.
DR RefSeq; WP_013035572.1; NC_013967.1.
DR AlphaFoldDB; Q5UT56; -.
DR SMR; Q5UT56; -.
DR STRING; 309800.C498_05055; -.
DR EnsemblBacteria; ADE04575; ADE04575; HVO_1957.
DR GeneID; 8926708; -.
DR KEGG; hvo:HVO_1957; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_4_2; -.
DR OMA; HEKAAMG; -.
DR BRENDA; 5.6.1.5; 2561.
DR Proteomes; UP000008243; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Proteasome; Reference proteome.
FT CHAIN 1..412
FT /note="Proteasome-activating nucleotidase 2"
FT /id="PRO_0000397031"
FT REGION 409..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 28..74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 196..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
SQ SEQUENCE 412 AA; 45589 MW; CA7A255BBC1BA45C CRC64;
MSRSPSLPER PHLDLDPEMS DAERLSALRQ HFERMVDVNR ELDQRLQNAD DRHAELVDEV
DQMKARNEAL KTASYYIATV EELTDDGVII KQHGNNQEVL TEFAPSLNID DIEPGDRVAI
NDSFAVQTVL DDETDARAQA MEVVESPTVT YDDIGGIDEQ VREVREAVEQ PLENPEMFAE
VGIDPPSGVL LYGPPGTGKT MLAKAVANET NASFIKMAGS ELVQKFIGEG ARLVRDLFKL
AAEREPVVVF IDEIDAVASK RTDSKTSGDA EVQRTMMQLL SEMDGFDDRG DIRIIAATNR
FDMLDEAILR PGRFDRLIEV PKPAVEGRRH ILDIHTRDMN VADDVDLDAL AEELDDYSGA
DIASLTTEAG MFAIRDGRTE VTGADFDAAH EKLSNVDESG TGPISGFTDY QY
