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A0PQT3 (PSB_MYCUA) 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:MUL_2331
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length289 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 – 5555Removed in mature form; by autocatalysis By similarity
PRO_0000397552
Chain56 – 289234Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397553

Sites

Active site561Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PQT3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: EAA3931ABA342C6B

FASTA28930,302
        10         20         30         40         50         60 
MTWPLPDRLS INSAISGSAV DLSSFAEFLR RQAPELLPAS IKHGGGAVGD QLPHATTIVA 

        70         80         90        100        110        120 
LKYPGGVLIA GDRRSTQGNM IAGRDVRKVY ITDDYTATGI AGTAAIAVEF ARLYAVELEH 

       130        140        150        160        170        180 
YEKLEGVPLT FAGKVNRLAI MVRGNLAAAM QGLVALPLLA SYDIHASDPR SAGRIVSFDA 

       190        200        210        220        230        240 
AGGWNIEEEG YQAVGSGSIF AKSSIKKLYA QVTDADSALR VAVEALYDAA DDDSATGGPD 

       250        260        270        280 
LVRGIYPTAV TINADGAVDV PEVRIAELAR EVIGSRSRAD TFGPDGGEK 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL04702.1.
RefSeqYP_906173.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PQT3.
SMRA0PQT3. Positions 21-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_2331.

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL04702; ABL04702; MUL_2331.
GeneID4550476.
KEGGmul:MUL_2331.
PATRIC18171810. VBIMycUlc37413_2747.

Organism-specific databases

GenoListMUL_2331.
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_MYCUA
AccessionPrimary (citable) accession number: A0PQT3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 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