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D1A2S9 (PSB1_THECD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 31. 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 1

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit 1
Proteasome core protein PrcB 1
Gene names
Name:prcB1
Ordered Locus Names:Tcur_2311
OrganismThermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081) [Complete proteome] [HAMAP]
Taxonomic identifier471852 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeThermomonosporaceaeThermomonospora

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_0000397596
Chain57 – 284228Proteasome subunit beta 1 HAMAP-Rule MF_02113
PRO_0000397597

Sites

Active site571Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
D1A2S9 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: 8F0B5BD4B7311B59

FASTA28430,317
        10         20         30         40         50         60 
MASHDSYTGR LPGAFMNPGT SSFTEFLASY NPDLLPGRHM TALAGGMPGN VEAPHATTIV 

        70         80         90        100        110        120 
AVTFPGGVVM AGDRRATAGN MIAQRDVEKV FRADEFSAVA IAGTAGIGME IVRLFQVEIE 

       130        140        150        160        170        180 
HYEKMEGRTL SLEGKANRLA TMIRANLGMA MQGLVAVPLF AGYDTEREVG RIFSYDPAGG 

       190        200        210        220        230        240 
RYEEHEHHSI GSGSVFARGA LKKLWRPDLS AQDAALVCVQ ALYDAADDDS ATGGPDLIRK 

       250        260        270        280 
IYPVVATVTA DGFRRLPEEE VGELARIVVD GRHDSPGGPT APLR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001738 Genomic DNA. Translation: ACY97877.1.
RefSeqYP_003299915.1. NC_013510.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACY97877; ACY97877; Tcur_2311.
GeneID8603648.
KEGGtcu:Tcur_2311.
PATRIC32514290. VBITheCur33965_2364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000245308.
KOK03433.
OMAFQVELEH.
OrthoDBEOG6XM79W.

Enzyme and pathway databases

BioCycTCUR471852:GHHD-2358-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.
IPR000243. Pept_T1A_subB.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03690. 20S_bact_beta. 1 hit.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB1_THECD
AccessionPrimary (citable) accession number: D1A2S9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 19, 2010
Last modified: June 11, 2014
This is version 31 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