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Q7AKQ6 (PSA_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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 PrcA
Gene names
Name:prcA
Ordered Locus Names:SCO1643
ORF Names:SCI41.26
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length254 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 S.coelicolor proteasome is able to cleave oligopeptides after hydrophobic residues, but not after basic or acidic residues, thus displaying chymotrypsin-like activity but not trypsin-like activity. Ref.1

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.1

Enzyme regulation

The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger 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 By similarity. Peptidolytic activity is completely inhibited by lactacystin, and to a lesser extent, by N-acetyl-Leu-Leu-norleucinal (Ac-LLnL) and benzoyloxycarbonyl-Leu-Leu-Leu-vinylsulfone (Z-LLL-VS) in vitro. Ref.1

Pathway

Protein degradation; proteasomal Pup-dependent pathway. HAMAP-Rule MF_00289

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 probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped by the proteasome-associated ATPase, ARC. Ref.1

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00289.

Post-translational modification

The N-terminus is blocked. HAMAP-Rule MF_00289

Sequence similarities

Belongs to the peptidase T1A family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 55 degrees Celsius. HAMAP-Rule MF_00289

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000383484

Sequences

Sequence LengthMass (Da)Tools
Q7AKQ6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 97460DA9883C33D8

FASTA25427,883
        10         20         30         40         50         60 
MSTPFYVSPQ QAMADRAEYA RKGIARGRSL VVLQYADGIV FVGENPSRAL HKFSEIYDRI 

        70         80         90        100        110        120 
GFAAAGKYNE YENLRIGGVR YADLRGYTYD RDDVTARGLA NVYAQTLGTI FSSQAEKPYE 

       130        140        150        160        170        180 
VELVVAEVGD SPENDQIYRL PHDGSIVDEH GSVAVGGNAE QISGYLDQRH RDGMTLAEAL 

       190        200        210        220        230        240 
KLAVQALSRD TNGTEREIPA ERLEVAVLDR TRPQQRKFKR IVGGQLSRLL ESGAASADGE 

       250 
AETEAETDSG SDEE 

« Hide

References

« Hide 'large scale' references
[1]"The 20S proteasome of Streptomyces coelicolor."
Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R.
J. Bacteriol. 180:5448-5453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, ENZYME REGULATION, TEMPERATURE DEPENDENCE, BLOCKAGE OF N-TERMINUS.
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF086832 Genomic DNA. Translation: AAC64278.1.
AL939109 Genomic DNA. Translation: CAB59496.1.
RefSeqNP_625918.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ7AKQ6.
SMRQ7AKQ6. Positions 8-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO1643.

Protein family/group databases

MEROPST01.011.

PTM databases

PhosSiteP12011285.

Proteomic databases

PRIDEQ7AKQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB59496; CAB59496; CAB59496.
GeneID1097074.
KEGGsco:SCO1643.
PATRIC23732888. VBIStrCoe124346_1658.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245319.
KOK03432.
OMAGRYNEFE.
OrthoDBEOG6NKQZG.
PhylomeDBQ7AKQ6.

Enzyme and pathway databases

UniPathwayUPA00997.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_00289_B. Proteasome_A_B.
InterProIPR029055. Ntn_hydrolases_N.
IPR022296. Proteasome_asu_bac.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03691. 20S_bact_alpha. 1 hit.
PROSITEPS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSA_STRCO
AccessionPrimary (citable) accession number: Q7AKQ6
Secondary accession number(s): O87599
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 72 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways