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P25156 (PSA_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha

EC=3.4.25.1
Alternative name(s):
20S proteasome alpha subunit
Proteasome core protein PsmA
Gene names
Name:psmA
Ordered Locus Names:Ta1288
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.4

Enzyme regulation

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. Ref.8 Ref.14

Subunit structure

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. Ref.5 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00289.

Post-translational modification

The N-terminus is blocked. HAMAP-Rule MF_00289

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.

Sequence similarities

Belongs to the peptidase T1A family.

Biophysicochemical properties

Kinetic parameters:

KM=39 µM for Suc-LLVY-Amc (at 55 degrees Celsius) Ref.4

Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000124189

Experimental info

Mutagenesis1 – 1212Missing: Markedly increases peptidolytic activity. Designated open-gate mutant. Ref.7
Mutagenesis661K → A: Prevents PAN to associate with the proteasome and stimulate gate opening. Ref.8
Mutagenesis811L → A, E or G: Prevents PAN to stimulate gate opening. Ref.11
Mutagenesis821V → A: No effect on PAN's ability to stimulate gate opening. Ref.11
Mutagenesis821V → D or G: Prevents PAN to stimulate gate opening. Ref.11

Secondary structure

...................................... 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25156 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 141A48581DA0DFB5

FASTA23325,799
        10         20         30         40         50         60 
MQQGQMAYDR AITVFSPDGR LFQVEYAREA VKKGSTALGM KFANGVLLIS DKKVRSRLIE 

        70         80         90        100        110        120 
QNSIEKIQLI DDYVAAVTSG LVADARVLVD FARISAQQEK VTYGSLVNIE NLVKRVADQM 

       130        140        150        160        170        180 
QQYTQYGGVR PYGVSLIFAG IDQIGPRLFD CDPAGTINEY KATAIGSGKD AVVSFLEREY 

       190        200        210        220        230 
KENLPEKEAV TLGIKALKSS LEEGEELKAP EIASITVGNK YRIYDQEEVK KFL 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59507 Genomic DNA. Translation: CAA42094.1.
AL445067 Genomic DNA. Translation: CAC12411.1.
PIRS55350.
RefSeqNP_394744.1. NC_002578.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP25156.
SMRP25156. Positions 7-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta1288.

Proteomic databases

PRIDEP25156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12411; CAC12411; CAC12411.
GeneID1456771.
KEGGtac:Ta1288.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091085.
KOK03432.
OMAFQVNYAR.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_00289_A. Proteasome_A_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03633. arc_protsome_A. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25156.

Entry information

Entry namePSA_THEAC
AccessionPrimary (citable) accession number: P25156
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references