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P28061

- PSB_THEAC

UniProt

P28061 - PSB_THEAC

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Protein
Proteasome subunit beta
Gene
psmB, Ta0612
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

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 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 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.2 Publications

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)

Sites

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

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene namesi
Name:psmB
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 By similarity UniRule annotation

GO - Cellular componenti

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

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 autocatalysisUniRule annotation
PRO_0000026675
Chaini9 – 211203Proteasome subunit betaUniRule annotation
PRO_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 Publications

Protein-protein interaction databases

STRINGi273075.Ta0612.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP28061.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

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