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Proteasome-activating nucleotidase 1 (PAN 1) (Proteasomal ATPase 1) (Proteasome regulatory ATPase 1) (Proteasome regulatory particle 1)

 PAN1_HALVD              Reviewed;         406 AA.
D4GUJ7; Q5UT57;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 2.
28-FEB-2018, entry version 36.
RecName: Full=Proteasome-activating nucleotidase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
Short=PAN 1 {ECO:0000255|HAMAP-Rule:MF_00553};
AltName: Full=Proteasomal ATPase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
AltName: Full=Proteasome regulatory ATPase 1 {ECO:0000255|HAMAP-Rule:MF_00553};
AltName: Full=Proteasome regulatory particle 1 {ECO:0000255|HAMAP-Rule:MF_00553};
Name=pan1 {ECO:0000255|HAMAP-Rule:MF_00553}; Synonyms=panA;
OrderedLocusNames=HVO_0850;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
PubMed=15516591; DOI=10.1128/JB.186.22.7763-7772.2004;
Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.;
"Differential regulation of the PanA and PanB proteasome-activating
nucleotidase and 20S proteasomal proteins of the haloarchaeon
Haloferax volcanii.";
J. Bacteriol. 186:7763-7772(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[3]
DISRUPTION PHENOTYPE.
PubMed=18931121; DOI=10.1128/JB.01180-08;
Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.;
"Proteasomal components required for cell growth and stress responses
in the haloarchaeon Haloferax volcanii.";
J. Bacteriol. 190:8096-8105(2008).
[4]
FUNCTION, ATPASE ACTIVITY, NUCLEOTIDE SPECIFICITY, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, SUBUNIT, AND INTERACTION WITH
SAMPYLATED PROTEINS.
STRAIN=DS2 / DS70;
PubMed=24343376; DOI=10.1007/s00792-013-0615-8;
Prunetti L., Reuter C.J., Hepowit N.L., Wu Y., Barrueto L.,
Miranda H.V., Kelly K., Maupin-Furlow J.A.;
"Structural and biochemical properties of an extreme 'salt-loving'
proteasome activating nucleotidase from the archaeon Haloferax
volcanii.";
Extremophiles 18:283-293(2014).
-!- FUNCTION: ATPase which is responsible for recognizing, binding,
unfolding and translocation of substrate proteins into the
archaeal 20S proteasome core particle. Is essential for opening
the gate of the 20S proteasome via an interaction with its C-
terminus, thereby allowing substrate entry and access to the site
of proteolysis. Thus, the C-terminus of the proteasomal ATPase
functions like a 'key in a lock' to induce gate opening and
therefore regulate proteolysis. Unfolding activity requires energy
from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S
proteasome association which triggers gate opening, and supports
translocation of unfolded substrates (Probable). Is also able to
cleave other nucleoside triphosphates including GTP and TTP, but
the rate of hydrolysis is 4- to 5-fold slower than for ATP.
{ECO:0000269|PubMed:24343376, ECO:0000305}.
-!- ENZYME REGULATION: ATPase activity is inhibited by EDTA in vitro.
{ECO:0000269|PubMed:24343376}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=438 uM for ATP (at 42 degrees Celsius, pH 8 and 2 M NaCl)
{ECO:0000269|PubMed:24343376};
Vmax=471 nmol/h/mg enzyme for ATPase activity (at 42 degrees
Celsius, pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376};
Temperature dependence:
Optimum temperature is 42 degrees Celsius. ATPase activity is
1.5-fold decreased at 25 degrees Celsius and 37 degrees Celsius,
4.7-fold at 20 degrees Celsius. The protein is not active at 50
degrees Celsius. {ECO:0000269|PubMed:24343376};
-!- SUBUNIT: Homododecamer, in a proposed two stacked hexameric ring
configuration, but may also form homohexamer. The hexameric
complex has likely a two-ring architecture resembling a top hat
that caps the 20S proteasome core at one or both ends. Upon ATP-
binding, the C-terminus of PAN probably interacts with the alpha-
rings of the proteasome core by binding to the intersubunit
pockets. Interacts with SAMP1-MoaE conjugate in vitro, but does
not bind to SAMP1 or MoaE alone. {ECO:0000269|PubMed:24343376}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}.
-!- INDUCTION: Up-regulated at the mRNA level during transition from
exponential to stationary phase. However, at the protein level,
PanA is expressed at a high and relatively constant level
throughout growth. {ECO:0000269|PubMed:15516591}.
-!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
domain that may assist in substrate recognition, an interdomain
involved in PAN hexamerization, and a C-terminal ATPase domain of
the AAA type. {ECO:0000255|HAMAP-Rule:MF_00553}.
-!- DISRUPTION PHENOTYPE: Strains lacking panA gene alone display
relatively normal growth rate and overall cell yield, but they are
more sensitive to growth on organic versus inorganic nitrogen
sources and hypo-osmotic stress, they show limited growth in the
presence of L-canavanine and display enhanced thermotolerance.
Moreover, strains lackings both panA and panB still show robust
growth, demonstrating that the PAN proteins are not essential.
{ECO:0000269|PubMed:18931121}.
-!- MISCELLANEOUS: The biochemical properties of PAN 1 are highly
dependent on molar concentrations of salt with a significant loss
of ATPase activity and complex dissociation detected at 0.75 M
NaCl.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
Rule:MF_00553}.
-!- SEQUENCE CAUTION:
Sequence=ADE04646.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY627303; AAV38126.1; -; Genomic_DNA.
EMBL; CP001956; ADE04646.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; D4GUJ7; -.
SMR; D4GUJ7; -.
STRING; 309800.HVO_0850; -.
EnsemblBacteria; ADE04646; ADE04646; HVO_0850.
KEGG; hvo:HVO_0850; -.
eggNOG; arCOG01306; Archaea.
eggNOG; COG1222; LUCA.
HOGENOM; HOG000225143; -.
KO; K03420; -.
OrthoDB; POG093Z04M9; -.
BRENDA; 3.1.3.31; 2561.
Proteomes; UP000008243; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
HAMAP; MF_00553; PAN; 1.
InterPro; IPR005937; 26S_Psome_P45-like.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR023501; Nucleotidase_PAN.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01242; 26Sp45; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
Nucleotide-binding; Proteasome; Reference proteome.
CHAIN 1 406 Proteasome-activating nucleotidase 1.
/FTId=PRO_0000397030.
NP_BIND 194 199 ATP. {ECO:0000255|HAMAP-Rule:MF_00553}.
REGION 404 406 Docks into pockets in the proteasome
alpha-ring to cause gate opening.
{ECO:0000255|HAMAP-Rule:MF_00553}.
COILED 13 72 {ECO:0000255|HAMAP-Rule:MF_00553}.
BINDING 333 333 ATP. {ECO:0000255|HAMAP-Rule:MF_00553}.
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


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