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

B1YDJ0 (PSB2_PYRNV) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit 2
Proteasome core protein PsmB 2
Gene names
Name:psmB2
Ordered Locus Names:Tneu_0916
OrganismPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus) [Complete proteome] [HAMAP]
Taxonomic identifier444157 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length203 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 PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers 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

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 at one or both ends by the proteasome regulatory ATPase, PAN By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02113.

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Cellular componentCytoplasm
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteasomal protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex, beta-subunit complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 99Removed in mature form; by autocatalysis Potential
PRO_0000397484
Chain10 – 203194Proteasome subunit beta 2 HAMAP-Rule MF_02113
PRO_0000397485

Sites

Active site101Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
B1YDJ0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 879BE899429C0A17

FASTA20321,556
        10         20         30         40         50         60 
MGEEFQVGAT AVGIRAKDGV VLAAEKRVSY GFYTLSTAGK KVFIVNDKLA IASAGIIADM 

        70         80         90        100        110        120 
QALAKILKLN ARSYELEVKK KPTVKAMAKL LSVVMFSRRF MPFYAEVLVG GVDEEGPHLI 

       130        140        150        160        170        180 
VMDPLGSLIE DNYAALGTGA KLAVSLLDAS YRPDMTVEEA KKLAVQAVKA AIERDPVSGG 

       190        200 
GIDLVVVDGG GAREEEVKVQ VVI 

« Hide

References

[1]"Complete sequence of Thermoproteus neutrophilus V24Sta."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001014 Genomic DNA. Translation: ACB39853.1.
RefSeqYP_001794299.1. NC_010525.1.

3D structure databases

ProteinModelPortalB1YDJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444157.Tneu_0916.

Protein family/group databases

MEROPST01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB39853; ACB39853; Tneu_0916.
GeneID6164563.
KEGGtne:Tneu_0916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091083.
KOK03433.
OMAYSYKLAP.

Enzyme and pathway databases

BioCycTNEU444157:GHL2-929-MONOMER.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_02113_A. Proteasome_B_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03634. arc_protsome_B. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB2_PYRNV
AccessionPrimary (citable) accession number: B1YDJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 40 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