Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A0LU51 (PSA_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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:Acel_1189
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length234 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 – 234234Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000397131

Sequences

Sequence LengthMass (Da)Tools
A0LU51 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: FD21E92AF2B05FA6

FASTA23425,863
        10         20         30         40         50         60 
MSTPFYVSPE QIMKDRAEFA RKGIARGRSN VVLQYADGIL FVAENTSKAL HKISEVYDRI 

        70         80         90        100        110        120 
AFAAVGRYNE FENLRVAGVR LADLTGYTYD RRDVTGRTIA NAYAQTLGAI FSGATEKPYE 

       130        140        150        160        170        180 
VEIVVAEVGD TPDGDSMYRL TYDGSVAEEH GYVAMGGQAE QITAQLKDRY VENLPLGEAL 

       190        200        210        220        230 
RLAVDVLSRA SDGGEPRTLT PDQLEVAALD RTRGRRAFRR FIGAQLQELL RPTS 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK52961.1.
RefSeqYP_872947.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LU51.
SMRA0LU51. Positions 8-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351607.Acel_1189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK52961; ABK52961; Acel_1189.
GeneID4485511.
KEGGace:Acel_1189.
PATRIC20672850. VBIAciCel132453_1261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245319.
KOK03432.
OMAGRYNEFE.
OrthoDBEOG6NKQZG.

Enzyme and pathway databases

BioCycACEL351607:GIXW-1215-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_ACIC1
AccessionPrimary (citable) accession number: A0LU51
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: December 12, 2006
Last modified: June 11, 2014
This is version 51 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