PAN1_HALVD
ID PAN1_HALVD Reviewed; 406 AA.
AC D4GUJ7; Q5UT57;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Proteasome-activating nucleotidase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
DE Short=PAN 1 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasomal ATPase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory ATPase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory particle 1 {ECO:0000255|HAMAP-Rule:MF_00553};
GN Name=pan1 {ECO:0000255|HAMAP-Rule:MF_00553}; Synonyms=panA;
GN OrderedLocusNames=HVO_0850;
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).
RN [4]
RP FUNCTION, ATPASE ACTIVITY, NUCLEOTIDE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH SAMPYLATED
RP PROTEINS.
RC STRAIN=DS2 / DS70;
RX PubMed=24343376; DOI=10.1007/s00792-013-0615-8;
RA Prunetti L., Reuter C.J., Hepowit N.L., Wu Y., Barrueto L., Miranda H.V.,
RA Kelly K., Maupin-Furlow J.A.;
RT "Structural and biochemical properties of an extreme 'salt-loving'
RT proteasome activating nucleotidase from the archaeon Haloferax volcanii.";
RL Extremophiles 18:283-293(2014).
RN [5]
RP INTERACTION WITH NCSA.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:24906001};
RX PubMed=24906001; DOI=10.1371/journal.pone.0099104;
RA Chavarria N.E., Hwang S., Cao S., Fu X., Holman M., Elbanna D.,
RA Rodriguez S., Arrington D., Englert M., Uthandi S., Soell D.,
RA Maupin-Furlow J.A.;
RT "Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is
RT associated with ubiquitin-proteasome, translation, and RNA processing
RT system homologs.";
RL PLoS ONE 9:e99104-e99104(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 terminus of the proteasomal ATPase functions 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 (Probable). Is also
CC able to cleave other nucleoside triphosphates including GTP and TTP,
CC but the rate of hydrolysis is 4- to 5-fold slower than for ATP.
CC {ECO:0000269|PubMed:24343376, ECO:0000305}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:24343376}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=438 uM for ATP (at 42 degrees Celsius, pH 8 and 2 M NaCl)
CC {ECO:0000269|PubMed:24343376};
CC Vmax=471 nmol/h/mg enzyme for ATPase activity (at 42 degrees Celsius,
CC pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius. ATPase activity is 1.5-
CC fold decreased at 25 degrees Celsius and 37 degrees Celsius, 4.7-fold
CC at 20 degrees Celsius. The protein is not active at 50 degrees
CC Celsius. {ECO:0000269|PubMed:24343376};
CC -!- SUBUNIT: Homododecamer, in a proposed two stacked hexameric ring
CC configuration, but may also form homohexamer. The hexameric complex has
CC likely a two-ring architecture resembling a top hat that caps the 20S
CC proteasome core at one or both ends. Upon ATP-binding, the C-terminus
CC of PAN probably interacts with the alpha-rings of the proteasome core
CC by binding to the intersubunit pockets. Interacts with SAMP1-MoaE
CC conjugate in vitro, but does not bind to SAMP1 or MoaE alone
CC (PubMed:24343376). Interacts with NcsA (PubMed:24906001).
CC {ECO:0000269|PubMed:24343376, ECO:0000269|PubMed:24906001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}.
CC -!- INDUCTION: Up-regulated at the mRNA level during transition from
CC exponential to stationary phase. However, at the protein level, PanA is
CC expressed at a high and relatively constant level throughout growth.
CC {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 panA gene alone display
CC relatively normal growth rate and overall cell yield, but they are more
CC sensitive to growth on organic versus inorganic nitrogen sources and
CC hypo-osmotic stress, they show limited growth in the presence of L-
CC canavanine and display enhanced thermotolerance. 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 -!- MISCELLANEOUS: The biochemical properties of PAN 1 are highly dependent
CC on molar concentrations of salt with a significant loss of ATPase
CC activity and complex dissociation detected at 0.75 M NaCl.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00553}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADE04646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY627303; AAV38126.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04646.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; D4GUJ7; -.
DR SMR; D4GUJ7; -.
DR STRING; 309800.C498_14488; -.
DR EnsemblBacteria; ADE04646; ADE04646; HVO_0850.
DR KEGG; hvo:HVO_0850; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
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 Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Proteasome; Reference proteome.
FT CHAIN 1..406
FT /note="Proteasome-activating nucleotidase 1"
FT /id="PRO_0000397030"
FT REGION 404..406
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 13..72
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 194..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
SQ SEQUENCE 406 AA; 45802 MW; 1EC8C32BC0FA8D6F CRC64;
MMTDTVDDVD LPYDKDSASQ QEKITALQER LEVLETQNEE MRDKLLDTNA ENNKYQQKLE
RLTHENKKLK QSPLFVATVQ EITDEGVIIK QHGNNQEALT EVTDEMREEL EPDARVAVNN
SLSIVKRLDK ETDVRARVMQ VEHSPDVTYE DIGGLEEQMQ EVRETVEMPL DRPEMFAEVG
IDPPSGVLLY GPPGTGKTML AKAVANQTNA SFIKMAGSEL VHKFIGEGAK LVRDLFEVAR
ENEPAVIFID EIDAIASKRT DSKTSGDAEV QRTMMQLLAE MDGFDERGNI RIIAATNRFD
MLDPAILRPG RFDRLIEVPK PNEDGREIIF QIHTRKMNVS DDVDFVELAE MADNASGADI
KAVCTEAGMF AIRDDRTEIF MQDFVDAWEK IQQEASDETE VSRAFA
