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

A4FBY1 (PSB_SACEN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. 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 beta

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PrcB
Gene names
Name:prcB
Ordered Locus Names:SACE_2251
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_02113

Catalytic activity

Cleavage of peptide bonds with very broad specificity. HAMAP-Rule MF_02113

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_02113

Pathway

Protein degradation; proteasomal Pup-dependent pathway. HAMAP-Rule MF_02113

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_02113.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5656Removed in mature form; by autocatalysis By similarity
PRO_0000397572
Chain57 – 284228Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397573

Sites

Active site571Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A4FBY1 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 13A121F4FA79D892

FASTA28429,828
        10         20         30         40         50         60 
MSPMESSSTR FPGQALPAAY LTPGSSSFTD FLRVAAPELM PGSRPVPDGA VEAPHGTTIV 

        70         80         90        100        110        120 
ALTFRGGVLL AGDRRATMGN LIAQRDMEKL YVTDDYSAVG IAGTAGIALE MVRLYAIELE 

       130        140        150        160        170        180 
HYEKLEGVSL SLDGKANKLA TMLRGNLQGA MAGLAVLPLF AGFDVDADDP DRAGRIVSYD 

       190        200        210        220        230        240 
ITGGRYNELG GYYAVGSGSL FAKSALKKRF DPDADVDTAV RAAVEALYDA ADDDTATGGP 

       250        260        270        280 
DLSRRIYPSI ITITGTDGAT RVPEERAAEI ATEVVNGRMQ NPGG 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAM01556.1.
RefSeqYP_001104481.1. NC_009142.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405948.SACE_2251.

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM01556; CAM01556; SACE_2251.
GeneID4942104.
KEGGsen:SACE_2251.
PATRIC23411930. VBISacEry28377_2260.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245308.
KOK03433.
OMAFQVELEH.
OrthoDBEOG6XM79W.

Enzyme and pathway databases

UniPathwayUPA00997.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_02113_B. Proteasome_B_B.
InterProIPR029055. Ntn_hydrolases_N.
IPR022483. Pept_T1A_Psome_suB_actinobac.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03690. 20S_bact_beta. 1 hit.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB_SACEN
AccessionPrimary (citable) accession number: A4FBY1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: April 17, 2007
Last modified: June 11, 2014
This is version 53 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