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Q828I7 (PSA_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:SAV_6682
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation By similarity. HAMAP-Rule MF_00289

Catalytic activity

Cleavage of peptide bonds with very broad specificity. HAMAP-Rule MF_00289

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. HAMAP-Rule MF_00289

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 a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped by the proteasome-associated ATPase, ARC By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00289.

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000397176

Sequences

Sequence LengthMass (Da)Tools
Q828I7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CCB0A450F76965F4

FASTA25327,709
        10         20         30         40         50         60 
MSTPFYVSPQ QAMADRAEYA RKGIARGRSL VVLQFADGIV FVGENPSRAL HKFSEIYDRI 

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

       130        140        150        160        170        180 
VELVVAEVGE TPEGDQIYRL PHDGSIVDEH GSVAVGGNAE QISTYLDQRH QDGMTLAEAL 

       190        200        210        220        230        240 
KLAVQSLSRD TNGSEREIPA ERLEVAVLDR TRPQQRKFKR IVGRELSRLL EAAGASTAGE 

       250 
AGSAEDEGSD DEK 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC74393.1.
RefSeqNP_827858.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ828I7.
SMRQ828I7. Positions 8-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_6682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC74393; BAC74393; SAV_6682.
GeneID1211535.
KEGGsma:SAV_6682.
PATRIC23727474. VBIStrAve112782_7085.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245319.
KOK03432.
OMAGRYNEFE.
OrthoDBEOG6NKQZG.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6768-MONOMER.
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_STRAW
AccessionPrimary (citable) accession number: Q828I7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 70 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