Proteasome subunit alpha - psmA - Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

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P25156 (PSA_THEAC) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]

Taxonomic identifier

273075 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma ›

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=39 µM for Suc-LLVY-Amc (at 55 degrees Celsius) Ref.4 V_max=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius)

Ontologies

Keywords
Cellular component	Cytoplasm Proteasome
Molecular function	Hydrolase Protease Threonine protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteasomal protein catabolic process Inferred from direct assay Ref.4. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complex Inferred from direct assay Ref.12 Ref.9 Ref.4. Source: UniProtKB
Molecular_function	endopeptidase activity Inferred from direct assay Ref.4. Source: UniProtKB threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 233

233

Proteasome subunit alpha HAMAP-Rule MF_00289

PRO_0000124189

Experimental info

Mutagenesis

1 – 12

Missing: Markedly increases peptidolytic activity. Designated open-gate mutant. Ref.7

Mutagenesis

K → A: Prevents PAN to associate with the proteasome and stimulate gate opening. Ref.8

Mutagenesis

L → A, E or G: Prevents PAN to stimulate gate opening. Ref.11

Mutagenesis

V → A: No effect on PAN's ability to stimulate gate opening. Ref.11

Mutagenesis

V → D or G: Prevents PAN to stimulate gate opening. Ref.11

Secondary structure

233

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P25156 [UniParc].

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

FASTA

233

25,799

        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' referencesShow '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.

PIR

S55350.

RefSeq

NP_394744.1. NC_002578.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]

ProteinModelPortal

P25156.

SMR

P25156. Positions 7-233.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

STRING

273075.Ta1288.

Proteomic databases

PRIDE

P25156.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAC12411; CAC12411; CAC12411.

GeneID

1456771.

KEGG

tac:Ta1288.

Phylogenomic databases

eggNOG

COG0638.

HOGENOM

HOG000091085.

K03432.

OMA

FQVNYAR.

Family and domain databases

Gene3D

3.60.20.10. 1 hit.

HAMAP

MF_00289_A. Proteasome_A_A.

InterPro

IPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]

Pfam

PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]

SMART

SM00948. Proteasome_A_N. 1 hit.
[Graphical view]

SUPFAM

SSF56235. SSF56235. 1 hit.

TIGRFAMs

TIGR03633. arc_protsome_A. 1 hit.

PROSITE

PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25156.

Entry information

Entry name

PSA_THEAC

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents