UniProtKB - P25156 (PSA_THEAC)
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Protein
Proteasome subunit alpha
Gene
psmA
Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Functioni
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.UniRule annotation1 Publication
Miscellaneous
The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.
Catalytic activityi
Cleavage of peptide bonds with very broad specificity.UniRule annotation1 Publication
Enzyme regulationi
The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.UniRule annotation2 Publications
Kineticsi
- KM=39 µM for Suc-LLVY-Amc (at 55 degrees Celsius)1 Publication
- Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius)1 Publication
GO - Molecular functioni
- endopeptidase activity Source: UniProtKB
- threonine-type endopeptidase activity Source: UniProtKB-KW
GO - Biological processi
- proteasomal protein catabolic process Source: UniProtKB
- ubiquitin-dependent protein catabolic process Source: InterPro
Keywordsi
Molecular function | Hydrolase, Protease, Threonine protease |
Enzyme and pathway databases
BioCyci | TACI273075:G1GT7-1408-MONOMER. |
Protein family/group databases
MEROPSi | T01.970. |
Names & Taxonomyi
Protein namesi | Recommended name: Proteasome subunit alphaUniRule annotation (EC:3.4.25.1UniRule annotation)Alternative name(s): 20S proteasome alpha subunitUniRule annotation Proteasome core protein PsmAUniRule annotation |
Gene namesi | Name:psmAUniRule annotation Ordered Locus Names:Ta1288 |
Organismi | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
Taxonomic identifieri | 273075 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
- proteasome core complex, alpha-subunit complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, ProteasomePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1 – 12 | Missing : Markedly increases peptidolytic activity. Designated open-gate mutant. 1 PublicationAdd BLAST | 12 | |
Mutagenesisi | 66 | K → A: Prevents PAN to associate with the proteasome and stimulate gate opening. 1 Publication | 1 | |
Mutagenesisi | 81 | L → A, E or G: Prevents PAN to stimulate gate opening. 1 Publication | 1 | |
Mutagenesisi | 82 | V → A: No effect on PAN's ability to stimulate gate opening. 1 Publication | 1 | |
Mutagenesisi | 82 | V → D or G: Prevents PAN to stimulate gate opening. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000124189 | 1 – 233 | Proteasome subunit alphaAdd BLAST | 233 |
Post-translational modificationi
The N-terminus is blocked.
Proteomic databases
PRIDEi | P25156. |
Interactioni
Subunit structurei
The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.UniRule annotation6 Publications
Protein-protein interaction databases
STRINGi | 273075.Ta1288. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 13 – 15 | Combined sources | 3 | |
Helixi | 22 – 31 | Combined sources | 10 | |
Beta strandi | 37 – 42 | Combined sources | 6 | |
Beta strandi | 45 – 50 | Combined sources | 6 | |
Beta strandi | 57 – 59 | Combined sources | 3 | |
Beta strandi | 61 – 63 | Combined sources | 3 | |
Beta strandi | 66 – 71 | Combined sources | 6 | |
Beta strandi | 74 – 81 | Combined sources | 8 | |
Helixi | 82 – 103 | Combined sources | 22 | |
Helixi | 109 – 122 | Combined sources | 14 | |
Turni | 123 – 125 | Combined sources | 3 | |
Beta strandi | 126 – 129 | Combined sources | 4 | |
Beta strandi | 134 – 141 | Combined sources | 8 | |
Beta strandi | 146 – 151 | Combined sources | 6 | |
Turni | 153 – 155 | Combined sources | 3 | |
Beta strandi | 157 – 166 | Combined sources | 10 | |
Helixi | 169 – 179 | Combined sources | 11 | |
Helixi | 186 – 199 | Combined sources | 14 | |
Helixi | 202 – 204 | Combined sources | 3 | |
Beta strandi | 211 – 216 | Combined sources | 6 | |
Beta strandi | 222 – 224 | Combined sources | 3 | |
Helixi | 226 – 230 | Combined sources | 5 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1PMA | X-ray | 3.40 | A/C/D/E/F/G/H/I/J/K/L/M/N/O | 1-233 | [»] | |
1YA7 | X-ray | 2.30 | A/B/C/D/E/F/G | 1-233 | [»] | |
1YAR | X-ray | 1.90 | A/B/C/D/E/F/G | 1-233 | [»] | |
1YAU | X-ray | 2.40 | A/B/C/D/E/F/G | 1-233 | [»] | |
2KU1 | NMR | - | A/B/C/D/E/F/G | 1-233 | [»] | |
2KU2 | NMR | - | A/B/C/D/E/F/G | 1-233 | [»] | |
3C91 | electron microscopy | 6.80 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 1-233 | [»] | |
3C92 | electron microscopy | 6.80 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 1-233 | [»] | |
3IPM | X-ray | 4.00 | A/B/C/D/E/F/G | 1-233 | [»] | |
3J9I | electron microscopy | 3.30 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-233 | [»] | |
3JRM | X-ray | 2.90 | A/B/C/D/E/F/G | 7-233 | [»] | |
3JSE | X-ray | 2.90 | A/B/C/D/E/F/G | 7-233 | [»] | |
3JTL | X-ray | 3.20 | A/B/C/D/E/F/G | 7-233 | [»] | |
5VY3 | electron microscopy | 3.10 | 0/A/C/E/G/I/K/M/O/Q/S/U/W/Y | 10-233 | [»] | |
5VY4 | electron microscopy | 3.30 | 0/A/C/E/G/I/K/M/O/Q/S/U/W/Y | 10-233 | [»] | |
6BDF | electron microscopy | 2.80 | 0/A/C/E/G/I/K/M/O/Q/S/U/W/Y | 1-233 | [»] | |
ProteinModelPortali | P25156. | |||||
SMRi | P25156. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P25156. |
Family & Domainsi
Sequence similaritiesi
Belongs to the peptidase T1A family.UniRule annotation
Phylogenomic databases
eggNOGi | arCOG00971. Archaea. COG0638. LUCA. |
HOGENOMi | HOG000091085. |
KOi | K03432. |
OMAi | FQVEYAR. |
OrthoDBi | POG093Z086S. |
Family and domain databases
CDDi | cd03756. proteasome_alpha_archeal. 1 hit. |
Gene3Di | 3.60.20.10. 1 hit. |
HAMAPi | MF_00289_A. Proteasome_A_A. 1 hit. |
InterProi | View protein in InterPro IPR029055. Ntn_hydrolases_N. IPR023332. Proteasome_alpha-type. IPR019982. Proteasome_asu_arc. IPR000426. Proteasome_asu_N. IPR001353. Proteasome_sua/b. |
Pfami | View protein in Pfam PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. |
SMARTi | View protein in SMART SM00948. Proteasome_A_N. 1 hit. |
SUPFAMi | SSF56235. SSF56235. 1 hit. |
TIGRFAMsi | TIGR03633. arc_protsome_A. 1 hit. |
PROSITEi | View protein in PROSITE PS00388. PROTEASOME_ALPHA_1. 1 hit. PS51475. PROTEASOME_ALPHA_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
P25156-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQQGQMAYDR AITVFSPDGR LFQVEYAREA VKKGSTALGM KFANGVLLIS
60 70 80 90 100
DKKVRSRLIE QNSIEKIQLI DDYVAAVTSG LVADARVLVD FARISAQQEK
110 120 130 140 150
VTYGSLVNIE NLVKRVADQM QQYTQYGGVR PYGVSLIFAG IDQIGPRLFD
160 170 180 190 200
CDPAGTINEY KATAIGSGKD AVVSFLEREY KENLPEKEAV TLGIKALKSS
210 220 230
LEEGEELKAP EIASITVGNK YRIYDQEEVK KFL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X59507 Genomic DNA. Translation: CAA42094.1. AL445067 Genomic DNA. Translation: CAC12411.1. |
PIRi | S55350. |
RefSeqi | WP_010901695.1. NC_002578.1. |
Genome annotation databases
EnsemblBacteriai | CAC12411; CAC12411; CAC12411. |
GeneIDi | 1456771. |
KEGGi | tac:Ta1288. |
Similar proteinsi
Entry informationi
Entry namei | PSA_THEAC | |
Accessioni | P25156Primary (citable) accession number: P25156 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | October 1, 1994 | |
Last modified: | March 28, 2018 | |
This is version 144 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |