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D2Q4H5 (PSA_KRIFD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 27. 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:Kfla_3227
OrganismKribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399) [Complete proteome] [HAMAP]
Taxonomic identifier479435 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeKribbella

Protein attributes

Sequence length283 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 – 283283Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000397144

Sequences

Sequence LengthMass (Da)Tools
D2Q4H5 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 21E3FE4D188C5C62

FASTA28330,692
        10         20         30         40         50         60 
MSTPFYVSPE QLMRDRADFA RKGIAKGRSA IALQYADGIL FVAENRSPAL HKVAEIYDRM 

        70         80         90        100        110        120 
AFAAVGRYNE FENLRIAGVR LADMRGYSYD RRDVTGRALA NAYAQTLGAI FSSGGEKPLE 

       130        140        150        160        170        180 
VEILVAEVGT TAADDQIYRL TYDGSIADVR GYAVMGGPAE QVADYVGEHY QEGISLAGAL 

       190        200        210        220        230        240 
RLAVDALGHD SSEVRQLEPD QIEVAVLDRT RTQVRKFKRI SDQTLARILS ESRPDTAPSP 

       250        260        270        280 
ESSAHTEETE TVDGGSYESA AGTSAADDAP IAPPEDPDDN RPL 

« Hide

References

[1]"The complete genome of Kribbella flavida DSM 17836."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M. expand/collapse author list , Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17836 / JCM 10339 / NBRC 14399.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001736 Genomic DNA. Translation: ADB32289.1.
RefSeqYP_003381088.1. NC_013729.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB32289; ADB32289; Kfla_3227.
GeneID8719833.
KEGGkfl:Kfla_3227.
PATRIC32236898. VBIKriFla67707_3220.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000245319.
KOK03432.
OMAGRYNEFE.

Enzyme and pathway databases

BioCycKFLA479435:GI0F-3256-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_KRIFD
AccessionPrimary (citable) accession number: D2Q4H5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: March 2, 2010
Last modified: June 11, 2014
This is version 27 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