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D2S6E2 (PSB_GEOOG) 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 beta

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PrcB
Gene names
Name:prcB
Ordered Locus Names:Gobs_2682
OrganismGeodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / G-20) [Complete proteome] [HAMAP]
Taxonomic identifier526225 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeGeodermatophilaceaeGeodermatophilus

Protein attributes

Sequence length280 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 – 5353Removed in mature form; by autocatalysis By similarity
PRO_0000397510
Chain54 – 280227Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397511

Sites

Active site541Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
D2S6E2 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: D3F1DEB8112F9BE3

FASTA28029,436
        10         20         30         40         50         60 
MSEYSAGRSG FSPAYLDRVG SSFTDFLAAA APHLLPGSRP VPQIPVGNVT PHGTTIVSVT 

        70         80         90        100        110        120 
YDGGVLMGGD RRATMGNLIS SREIEKVYPA DAWSVIGIAG AAGIAIEMVR LYQVELEHYE 

       130        140        150        160        170        180 
KIEGLTLSLD GKANRLAQMI RGNLGAALQG LAVVPLFAGF DLDAAPGAAP GRIFSYDVTG 

       190        200        210        220        230        240 
GNYEERGYSA VGSGSLFARN SLKKTWRPNL DGDAATRSLV EALYDAADDD SATGGPDPVR 

       250        260        270        280 
RLYPIVYRVD AEGAVRVPDD EIAAVATRIT DERSAADGQG 

« Hide

References

[1]"The complete genome of Geodermatophilus obscurus DSM 43160."
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., Munk A.C., 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., Jando M., Schneider S., Klenk H.-P., Eisen J.A.
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25078 / DSM 43160 / JCM 3152 / G-20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001867 Genomic DNA. Translation: ADB75316.1.
RefSeqYP_003409687.1. NC_013757.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB75316; ADB75316; Gobs_2682.
GeneID8754354.
KEGGgob:Gobs_2682.
PATRIC32174490. VBIGeoObs49253_2658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000245308.
KOK03433.
OMAFQVELEH.

Enzyme and pathway databases

BioCycGOBS526225:GI00-2711-MONOMER.
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_GEOOG
AccessionPrimary (citable) accession number: D2S6E2
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