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P28061

- PSB_THEAC

UniProt

P28061 - PSB_THEAC

Protein

Proteasome subunit beta

Gene

psmB

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 114 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei9 – 91Nucleophile1 PublicationUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Protein family/group databases

    MEROPSiT01.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit betaUniRule annotation (EC:3.4.25.1UniRule annotation)
    Alternative name(s):
    20S proteasome beta subunitUniRule annotation
    Proteasome core protein PsmBUniRule annotation
    Gene namesi
    Name:psmBUniRule annotation
    Ordered Locus Names:Ta0612
    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, beta-subunit complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91T → S: No effect on catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 88Removed in mature form; by autocatalysis1 PublicationUniRule annotationPRO_0000026675
    Chaini9 – 211203Proteasome subunit betaPRO_0000026676Add
    BLAST

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Proteomic databases

    PRIDEiP28061.

    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.Ta0612.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 166
    Beta strandi19 – 246
    Beta strandi28 – 303
    Beta strandi33 – 375
    Beta strandi42 – 465
    Beta strandi49 – 557
    Helixi57 – 7822
    Helixi84 – 9714
    Turni98 – 1003
    Beta strandi105 – 12117
    Beta strandi127 – 13610
    Helixi139 – 14911
    Helixi156 – 17318
    Beta strandi182 – 1876
    Turni188 – 1903
    Beta strandi191 – 1944
    Helixi197 – 20711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PMAX-ray3.401/2/B/P/Q/R/S/T/U/V/W/X/Y/Z1-211[»]
    1YA7X-ray2.30H/I/J/K/L/M/N1-211[»]
    1YARX-ray1.90H/I/J/K/L/M/N1-211[»]
    1YAUX-ray2.40H/I/J/K/L/M/N1-211[»]
    3C91electron microscopy6.801/2/H/I/J/K/L/M/N/V/W/X/Y/Z9-211[»]
    3C92electron microscopy6.801/2/H/I/J/K/L/M/N/V/W/X/Y/Z9-211[»]
    3IPMX-ray4.00H/I/J/K/L/M/N1-211[»]
    3JRMX-ray2.90H/I/J/K/L/M/N9-211[»]
    3JSEX-ray2.90H/I/J/K/L/M/N9-211[»]
    3JTLX-ray3.20H/I/J/K/L/M/N9-211[»]
    ProteinModelPortaliP28061.
    SMRiP28061. Positions 9-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28061.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091083.
    KOiK03433.
    OMAiGYYIAHR.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_02113_A. Proteasome_B_A.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQTLETGTT TVGITLKDAV IMATERRVTM ENFIMHKNGK KLFQIDTYTG    50
    MTIAGLVGDA QVLVRYMKAE LELYRLQRRV NMPIEAVATL LSNMLNQVKY 100
    MPYMVQLLVG GIDTAPHVFS IDAAGGSVED IYASTGSGSP FVYGVLESQY 150
    SEKMTVDEGV DLVIRAISAA KQRDSASGGM IDVAVITRKD GYVQLPTDQI 200
    ESRIRKLGLI L 211
    Length:211
    Mass (Da):23,147
    Last modified:August 1, 1992 - v1
    Checksum:iF81B9360641873DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83674 Genomic DNA. Translation: AAA72102.1.
    AL445064 Genomic DNA. Translation: CAC11751.1.
    PIRiA42068.
    RefSeqiNP_394085.1. NC_002578.1.
    WP_010901036.1. NC_002578.1.

    Genome annotation databases

    EnsemblBacteriaiCAC11751; CAC11751; CAC11751.
    GeneIDi1456195.
    KEGGitac:Ta0612.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83674 Genomic DNA. Translation: AAA72102.1 .
    AL445064 Genomic DNA. Translation: CAC11751.1 .
    PIRi A42068.
    RefSeqi NP_394085.1. NC_002578.1.
    WP_010901036.1. 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 1/2/B/P/Q/R/S/T/U/V/W/X/Y/Z 1-211 [» ]
    1YA7 X-ray 2.30 H/I/J/K/L/M/N 1-211 [» ]
    1YAR X-ray 1.90 H/I/J/K/L/M/N 1-211 [» ]
    1YAU X-ray 2.40 H/I/J/K/L/M/N 1-211 [» ]
    3C91 electron microscopy 6.80 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z 9-211 [» ]
    3C92 electron microscopy 6.80 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z 9-211 [» ]
    3IPM X-ray 4.00 H/I/J/K/L/M/N 1-211 [» ]
    3JRM X-ray 2.90 H/I/J/K/L/M/N 9-211 [» ]
    3JSE X-ray 2.90 H/I/J/K/L/M/N 9-211 [» ]
    3JTL X-ray 3.20 H/I/J/K/L/M/N 9-211 [» ]
    ProteinModelPortali P28061.
    SMRi P28061. Positions 9-211.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273075.Ta0612.

    Protein family/group databases

    MEROPSi T01.002.

    Proteomic databases

    PRIDEi P28061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC11751 ; CAC11751 ; CAC11751 .
    GeneIDi 1456195.
    KEGGi tac:Ta0612.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091083.
    KOi K03433.
    OMAi GYYIAHR.

    Miscellaneous databases

    EvolutionaryTracei P28061.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_02113_A. Proteasome_B_A.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03634. arc_protsome_B. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase."
      Zwickl P., Grziwa A., Puehler G., Dahlmann B., Lottspeich F., Baumeister W.
      Biochemistry 31:964-972(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "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.
    3. "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.
    4. "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.
    5. "Proteasome from Thermoplasma acidophilum: a threonine protease."
      Seemuller E., Lupas A., Stock D., Lowe J., Huber R., Baumeister W.
      Science 268:579-582(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, CATALYTIC MECHANISM, MUTAGENESIS OF THR-9.
    6. "Autocatalytic processing of the 20S proteasome."
      Seemuller E., Lupas A., Baumeister W.
      Nature 382:468-471(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOCATALYTIC PROCESSING.
    7. "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.
    8. "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.
    9. "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.
    10. "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 ALPHA SUBUNIT, SUBUNIT.
    11. "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 ALPHA SUBUNIT AND T.BRUCEI PA26.
    12. "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.
    13. "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 ALPHA SUBUNIT AND THE C-TERMINUS OF PAN FROM M.JANNASCHII.
    14. "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 ALPHA SUBUNIT AND CHIMERIC PA26 CONSTRUCTS.
    15. "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: ENZYME REGULATION.

    Entry informationi

    Entry nameiPSB_THEAC
    AccessioniPrimary (citable) accession number: P28061
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 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