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P25156

- PSA_THEAC

UniProt

P25156 - PSA_THEAC

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    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

    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 lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001024: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

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

    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. 2 Publications
    Mutagenesisi81 – 811L → A, E or G: Prevents PAN to stimulate gate opening. 2 Publications
    Mutagenesisi82 – 821V → A: No effect on PAN's ability to stimulate gate opening. 2 Publications
    Mutagenesisi82 – 821V → D or G: Prevents PAN to stimulate gate opening. 2 Publications

    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 – 3110
    Beta strandi37 – 426
    Beta strandi45 – 506
    Beta strandi57 – 593
    Beta strandi61 – 633
    Beta strandi66 – 716
    Beta strandi74 – 818
    Helixi82 – 10322
    Helixi109 – 12214
    Turni123 – 1253
    Beta strandi126 – 1294
    Beta strandi134 – 1418
    Beta strandi146 – 1516
    Beta strandi157 – 16610
    Helixi169 – 17911
    Helixi186 – 19914
    Helixi202 – 2043
    Beta strandi211 – 2166
    Beta strandi222 – 2243
    Helixi226 – 2305

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiFQVNYAR.

    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

    MQQGQMAYDR AITVFSPDGR LFQVEYAREA VKKGSTALGM KFANGVLLIS    50
    DKKVRSRLIE QNSIEKIQLI DDYVAAVTSG LVADARVLVD FARISAQQEK 100
    VTYGSLVNIE NLVKRVADQM QQYTQYGGVR PYGVSLIFAG IDQIGPRLFD 150
    CDPAGTINEY KATAIGSGKD AVVSFLEREY KENLPEKEAV TLGIKALKSS 200
    LEEGEELKAP EIASITVGNK YRIYDQEEVK KFL 233
    Length:233
    Mass (Da):25,799
    Last modified:October 1, 1994 - v2
    Checksum:i141A48581DA0DFB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 FQVNYAR.

    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

    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: October 1, 2014
    This is version 124 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