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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)DescriptionActionsGraphical viewLength
Binding sitei353ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 219ATP6

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)DescriptionActionsGraphical viewLength
Mutagenesisi113G → W: 7% of wild-type unfolding activity. 1 Publication1
Mutagenesisi153D → A: 2% of wild-type unfolding activity. 1 Publication1
Mutagenesisi156A → D: 1.5% of wild-type unfolding activity. 1 Publication1
Mutagenesisi157K → G: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi244F → A: 1% of wild-type unfolding activity. 1 Publication1
Mutagenesisi245I → A or W: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi246G → A: 5% of wild-type unfolding activity. 1 Publication1
Mutagenesisi250 – 251SL → AA: 4% of wild-type unfolding activity. 1 Publication2
Mutagenesisi271E → K: 9% of wild-type unfolding activity. 1 Publication1
Mutagenesisi285G → W: 1.6% of wild-type unfolding activity. 1 Publication1
Mutagenesisi286G → A: No effect on unfolding activity. 1 Publication1
Mutagenesisi286G → L or W: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi428L → A, V or F: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi428L → I, Y or W: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi428L → R, D, C or P: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1
Mutagenesisi429Y → 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 Publication1
Mutagenesisi430R → A or W: No effect on PAN's ability to stimulate gate opening. Still associates with the proteasome. 1 Publication1
Mutagenesisi430R → D: Loss of PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → G: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → L: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → RA: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1
Mutagenesisi430Missing : Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000847431 – 430Proteasome-activating nucleotidaseAdd BLAST430

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

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi75 – 88Combined sources14
Beta strandi92 – 102Combined sources11
Beta strandi105 – 110Combined sources6
Beta strandi113 – 120Combined sources8
Helixi126 – 128Combined sources3
Beta strandi134 – 137Combined sources4
Turni139 – 141Combined sources3
Beta strandi144 – 147Combined sources4
Beta strandi159 – 164Combined sources6
Helixi169 – 171Combined sources3
Helixi176 – 185Combined sources10
Helixi187 – 191Combined sources5
Helixi193 – 199Combined sources7
Beta strandi205 – 216Combined sources12
Helixi217 – 227Combined sources11
Beta strandi231 – 236Combined sources6
Helixi237 – 240Combined sources4
Helixi247 – 261Combined sources15
Beta strandi264 – 270Combined sources7
Helixi273 – 276Combined sources4
Beta strandi280 – 282Combined sources3
Helixi285 – 288Combined sources4
Helixi289 – 302Combined sources14
Beta strandi306 – 315Combined sources10
Helixi319 – 321Combined sources3
Helixi324 – 327Combined sources4
Beta strandi331 – 337Combined sources7
Helixi343 – 354Combined sources12
Helixi365 – 371Combined sources7
Helixi377 – 393Combined sources17
Beta strandi397 – 399Combined sources3
Helixi401 – 415Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58576.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni428 – 430Docks into pockets in the proteasome alpha-ring to cause gate opening3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili9 – 89UniRule annotationAdd BLAST81

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.
OMAiCTEAGMN.
PhylomeDBiQ58576.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00553. PAN. 1 hit.
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.
RefSeqiWP_010870689.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99179; AAB99179; MJ_1176.
GeneIDi1452074.
KEGGimja:MJ_1176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99179.1.
PIRiG64446.
RefSeqiWP_010870689.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
GeneIDi1452074.
KEGGimja:MJ_1176.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiQ58576.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00553. PAN. 1 hit.
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...

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: November 2, 2016
This is version 110 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.