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Protein

Proteasome-activating nucleotidase

Gene

pan

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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-termini of the proteasomal ATPase function 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. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.UniRule annotation5 Publications

Enzyme regulationi

ATPase activity is inhibited by EDTA, N-ethylmaleimide (NEM) and p-chloromercuriphenyl-sulfonic acid (PCMS) in vitro.2 Publications

Kineticsi

  1. KM=497 µM for ATP1 Publication
  2. KM=307 µM for CTP1 Publication
  1. Vmax=3.5 µmol/min/mg enzyme for ATPase activity1 Publication
  2. Vmax=5.8 µmol/min/mg enzyme for CTPase activity1 Publication

pH dependencei

Optimum pH is 7-8 for ATPase activity. Is more active at pH 8 to 10 than at pH 5.5.1 Publication

Temperature dependencei

Optimum temperature is 80 degrees Celsius for ATPase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei353 – 3531ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2196ATP

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-HAMAP
  • CTPase activity Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome-activating nucleotidaseUniRule annotation
Short name:
PANUniRule annotation
Alternative name(s):
Proteasomal ATPaseUniRule annotation
Proteasome regulatory ATPaseUniRule annotation
Proteasome regulatory particleUniRule annotation
Gene namesi
Name:panUniRule annotation
Ordered Locus Names:MJ1176
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1131G → W: 7% of wild-type unfolding activity. 1 Publication
Mutagenesisi153 – 1531D → A: 2% of wild-type unfolding activity. 1 Publication
Mutagenesisi156 – 1561A → D: 1.5% of wild-type unfolding activity. 1 Publication
Mutagenesisi157 – 1571K → G: 4% of wild-type unfolding activity. 1 Publication
Mutagenesisi244 – 2441F → A: 1% of wild-type unfolding activity. 1 Publication
Mutagenesisi245 – 2451I → A or W: 4% of wild-type unfolding activity. 1 Publication
Mutagenesisi246 – 2461G → A: 5% of wild-type unfolding activity. 1 Publication
Mutagenesisi250 – 2512SL → AA: 4% of wild-type unfolding activity. 1 Publication
Mutagenesisi271 – 2711E → K: 9% of wild-type unfolding activity. 1 Publication
Mutagenesisi285 – 2851G → W: 1.6% of wild-type unfolding activity. 1 Publication
Mutagenesisi286 – 2861G → A: No effect on unfolding activity. 1 Publication
Mutagenesisi286 – 2861G → L or W: 4% of wild-type unfolding activity. 1 Publication
Mutagenesisi428 – 4281L → A, V or F: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi428 – 4281L → I, Y or W: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi428 – 4281L → R, D, C or P: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication
Mutagenesisi429 – 4291Y → A, V, I, L, F, W, R or D: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication
Mutagenesisi430 – 4301R → A or W: No effect on PAN's ability to stimulate gate opening. Still associates with the proteasome. 1 Publication
Mutagenesisi430 – 4301R → D: Loss of PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi430 – 4301R → G: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi430 – 4301R → L: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi430 – 4301R → RA: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication
Mutagenesisi430 – 4301Missing : Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Proteasome-activating nucleotidasePRO_0000084743Add
BLAST

Proteomic databases

PRIDEiQ58576.

Interactioni

Subunit structurei

Homohexamer. The hexameric complex has a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Alone, can form a complex composed of two stacked hexameric rings in vitro. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets.4 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi243232.MJ_1176.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 8814Combined sources
Beta strandi92 – 10211Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi113 – 1208Combined sources
Helixi126 – 1283Combined sources
Beta strandi134 – 1374Combined sources
Turni139 – 1413Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi159 – 1646Combined sources
Helixi169 – 1713Combined sources
Helixi176 – 18510Combined sources
Helixi187 – 1915Combined sources
Helixi193 – 1997Combined sources
Beta strandi205 – 21612Combined sources
Helixi217 – 22711Combined sources
Beta strandi231 – 2366Combined sources
Helixi237 – 2404Combined sources
Helixi247 – 26115Combined sources
Beta strandi264 – 2707Combined sources
Helixi273 – 2764Combined sources
Beta strandi280 – 2823Combined sources
Helixi285 – 2884Combined sources
Helixi289 – 30214Combined sources
Beta strandi306 – 31510Combined sources
Helixi319 – 3213Combined sources
Helixi324 – 3274Combined sources
Beta strandi331 – 3377Combined sources
Helixi343 – 35412Combined sources
Helixi365 – 3717Combined sources
Helixi377 – 39317Combined sources
Beta strandi397 – 3993Combined sources
Helixi401 – 41515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H43X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L74-150[»]
3H4MX-ray3.11A/B/C155-430[»]
3IPMX-ray4.00O/P/Q/R/S/T/U424-430[»]
ProteinModelPortaliQ58576.
SMRiQ58576. Positions 158-399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58576.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni428 – 4303Docks into pockets in the proteasome alpha-ring to cause gate opening

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili9 – 8981UniRule annotationAdd
BLAST

Domaini

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.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the AAA ATPase family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiarCOG01306. Archaea.
COG1222. LUCA.
InParanoidiQ58576.
KOiK03420.
OMAiCVGAELK.
PhylomeDBiQ58576.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00553. PAN.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR023501. Nucleotidase_PAN.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58576-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFEEFISTE LKKEKKAFTE EFKEEKEIND NSNLKNDLLK EELQEKARIA
60 70 80 90 100
ELESRILKLE LEKKELEREN LQLMKENEIL RRELDRMRVP PLIVGTVVDK
110 120 130 140 150
VGERKVVVKS STGPSFLVNV SHFVNPDDLA PGKRVCLNQQ TLTVVDVLPE
160 170 180 190 200
NKDYRAKAME VDERPNVRYE DIGGLEKQMQ EIREVVELPL KHPELFEKVG
210 220 230 240 250
IEPPKGILLY GPPGTGKTLL AKAVATETNA TFIRVVGSEL VKKFIGEGAS
260 270 280 290 300
LVKDIFKLAK EKAPSIIFID EIDAIAAKRT DALTGGDREV QRTLMQLLAE
310 320 330 340 350
MDGFDARGDV KIIGATNRPD ILDPAILRPG RFDRIIEVPA PDEKGRLEIL
360 370 380 390 400
KIHTRKMNLA EDVNLEEIAK MTEGCVGAEL KAICTEAGMN AIRELRDYVT
410 420 430
MDDFRKAVEK IMEKKKVKVK EPAHLDVLYR
Length:430
Mass (Da):48,690
Last modified:November 1, 1996 - v1
Checksum:i3FD2E94A68D483DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99179.1.
PIRiG64446.

Genome annotation databases

EnsemblBacteriaiAAB99179; AAB99179; MJ_1176.
KEGGimja:MJ_1176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99179.1.
PIRiG64446.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H43X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L74-150[»]
3H4MX-ray3.11A/B/C155-430[»]
3IPMX-ray4.00O/P/Q/R/S/T/U424-430[»]
ProteinModelPortaliQ58576.
SMRiQ58576. Positions 158-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1176.

Proteomic databases

PRIDEiQ58576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99179; AAB99179; MJ_1176.
KEGGimja:MJ_1176.

Phylogenomic databases

eggNOGiarCOG01306. Archaea.
COG1222. LUCA.
InParanoidiQ58576.
KOiK03420.
OMAiCVGAELK.
PhylomeDBiQ58576.

Miscellaneous databases

EvolutionaryTraceiQ58576.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00553. PAN.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR023501. Nucleotidase_PAN.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome."
    Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.
    J. Bacteriol. 182:1680-1692(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION AS AN ATPASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, INTERACTION WITH THE PROTEASOME.
  3. "An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes."
    Zwickl P., Ng D., Woo K.M., Klenk H.-P., Goldberg A.L.
    J. Biol. Chem. 274:26008-26014(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE PROTEASOME DEGRADATION PATHWAY, ATPASE ACTIVITY, NUCLEOTIDE SPECIFICITY, ENZYME REGULATION.
  4. "PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone."
    Benaroudj N., Goldberg A.L.
    Nat. Cell Biol. 2:833-839(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHAPERONE ACTIVITY.
  5. "ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins."
    Smith D.M., Kafri G., Cheng Y., Ng D., Walz T., Goldberg A.L.
    Mol. Cell 20:687-698(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THE PROTEASOME, SUBUNIT.
  6. "Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry."
    Smith D.M., Chang S.C., Park S., Finley D., Cheng Y., Goldberg A.L.
    Mol. Cell 27:731-744(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ROLE OF C-TERMINUS IN GATE OPENING, MUTAGENESIS OF LEU-428; TYR-429 AND ARG-430.
  7. "Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii."
    Zhang F., Wu Z., Zhang P., Tian G., Finley D., Shi Y.
    Mol. Cell 34:485-496(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UNFOLDING AND TRANSLOCATION MECHANISM, MUTAGENESIS OF GLY-113; ASP-153; ALA-156; LYS-157; PHE-244; ILE-245; GLY-246; 250-SER-LEU-251; GLU-271; GLY-285 AND GLY-286.
  8. "Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii."
    Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.
    Mol. Cell 34:473-484(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 74-430 IN COMPLEX WITH ADP, DOMAIN.
  9. "Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions."
    Yu Y., Smith D.M., Kim H.M., Rodriguez V., Goldberg A.L., Cheng Y.
    EMBO J. 29:692-702(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 424-430 IN COMPLEX WITH THE PROTEASOME OF T.ACIDOPHILUM.

Entry informationi

Entry nameiPAN_METJA
AccessioniPrimary (citable) accession number: Q58576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.