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P25156

- PSA_THEAC

UniProt

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
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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.1 PublicationUniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 PublicationUniRule annotation

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.2 PublicationsUniRule annotation

Kineticsi

  1. 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

  1. endopeptidase activity Source: UniProtKB
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal protein catabolic process Source: UniProtKB
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

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
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma ›
ProteomesiUP000001024: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. proteasome core complex, alpha-subunit complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1212Missing: Markedly increases peptidolytic activity. Designated open-gate mutant. 1 PublicationAdd
BLAST
Mutagenesisi66 – 661K → A: Prevents PAN to associate with the proteasome and stimulate gate opening. 1 Publication
Mutagenesisi81 – 811L → A, E or G: Prevents PAN to stimulate gate opening. 1 Publication
Mutagenesisi82 – 821V → A: No effect on PAN's ability to stimulate gate opening. 1 Publication
Mutagenesisi82 – 821V → D or G: Prevents PAN to stimulate gate opening. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Proteasome subunit alphaPRO_0000124189Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP25156.

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.6 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi273075.Ta1288.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3110Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 506Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 716Combined sources
Beta strandi74 – 818Combined sources
Helixi82 – 10322Combined sources
Helixi109 – 12214Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi157 – 16610Combined sources
Helixi169 – 17911Combined sources
Helixi186 – 19914Combined sources
Helixi202 – 2043Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi222 – 2243Combined sources
Helixi226 – 2305Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMAX-ray3.40A/C/D/E/F/G/H/I/J/K/L/M/N/O1-233[»]
1YA7X-ray2.30A/B/C/D/E/F/G1-233[»]
1YARX-ray1.90A/B/C/D/E/F/G1-233[»]
1YAUX-ray2.40A/B/C/D/E/F/G1-233[»]
2KU1NMR-A/B/C/D/E/F/G1-233[»]
2KU2NMR-A/B/C/D/E/F/G1-233[»]
3C91electron microscopy6.80A/B/C/D/E/F/G/O/P/Q/R/S/T/U1-233[»]
3C92electron microscopy6.80A/B/C/D/E/F/G/O/P/Q/R/S/T/U1-233[»]
3IPMX-ray4.00A/B/C/D/E/F/G1-233[»]
3JRMX-ray2.90A/B/C/D/E/F/G7-233[»]
3JSEX-ray2.90A/B/C/D/E/F/G7-233[»]
3JTLX-ray3.20A/B/C/D/E/F/G7-233[»]
ProteinModelPortaliP25156.
SMRiP25156. Positions 7-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25156.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
KOiK03432.
OMAiEKNYKYD.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00289_A. Proteasome_A_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03633. arc_protsome_A. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25156-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:233
Mass (Da):25,799
Last modified:October 1, 1994 - v2
Checksum:i141A48581DA0DFB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59507 Genomic DNA. Translation: CAA42094.1.
AL445067 Genomic DNA. Translation: CAC12411.1.
PIRiS55350.
RefSeqiNP_394744.1. NC_002578.1.
WP_010901695.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC12411; CAC12411; CAC12411.
GeneIDi1456771.
KEGGitac:Ta1288.

Cross-referencesi

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 NP_394744.1. NC_002578.1.
WP_010901695.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
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 [» ]
ProteinModelPortali P25156.
SMRi P25156. Positions 7-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273075.Ta1288.

Proteomic databases

PRIDEi P25156.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC12411 ; CAC12411 ; CAC12411 .
GeneIDi 1456771.
KEGGi tac:Ta1288.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091085.
KOi K03432.
OMAi EKNYKYD.

Miscellaneous databases

EvolutionaryTracei P25156.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_00289_A. Proteasome_A_A.
InterProi IPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR03633. arc_protsome_A. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the gene encoding the large (alpha-) subunit of the proteasome from Thermoplasma acidophilum."
    Zwickl P., Lottspeich F., Dahlmann B., Baumeister W.
    FEBS Lett. 278:217-221(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-28; 41-54 AND 88-93.
  2. Zwickl P.
    Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 66-69.
  3. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  4. "Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum."
    Akopian T.N., Kisselev A.F., Goldberg A.L.
    J. Biol. Chem. 272:1791-1798(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
  5. "Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum."
    Puehler G., Weinkauf S., Bachmann L., Mueller S., Engel E., Hegerl R., Baumeister W.
    EMBO J. 11:1607-1616(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes."
    Kisselev A.F., Akopian T.N., Goldberg A.L.
    J. Biol. Chem. 273:1982-1989(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "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: INTERACTION WITH PAN, SUBUNIT, GATED STRUCTURE, MUTAGENESIS OF 1-MET--ILE-12.
  8. "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: GATE OPENING MECHANISM, ENZYME REGULATION, MUTAGENESIS OF LYS-66.
  9. "Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4-A resolution."
    Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R.
    Science 268:533-539(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, SUBUNIT.
  10. "The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions."
    Forster A., Masters E.I., Whitby F.G., Robinson H., Hill C.P.
    Mol. Cell 18:589-599(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND T.BRUCEI PA26.
  11. "Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases."
    Rabl J., Smith D.M., Yu Y., Chang S.C., Goldberg A.L., Cheng Y.
    Mol. Cell 30:360-368(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.8 ANGSTROMS) OF THE OPEN-GATE AND CLOSED-GATE CONFORMATIONS, GATE OPENING MECHANISM, MUTAGENESIS OF LEU-81 AND VAL-82.
  12. "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) IN COMPLEX WITH THE BETA SUBUNIT AND THE C-TERMINUS OF PAN FROM M.JANNASCHII.
  13. "Structural models for interactions between the 20S proteasome and its PAN/19S activators."
    Stadtmueller B.M., Ferrell K., Whitby F.G., Heroux A., Robinson H., Myszka D.G., Hill C.P.
    J. Biol. Chem. 285:13-17(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND CHIMERIC PA26 CONSTRUCTS.
  14. "Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR."
    Religa T.L., Sprangers R., Kay L.E.
    Science 328:98-102(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, ENZYME REGULATION.

Entry informationi

Entry nameiPSA_THEAC
AccessioniPrimary (citable) accession number: P25156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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