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Q18GX3 (PSB_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene names
Name:psmB
Ordered Locus Names:HQ_2661A
OrganismHaloquadratum walsbyi (strain DSM 16790 / HBSQ001) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length243 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 – 4949Removed in mature form; by autocatalysis By similarity
PRO_0000397304
Chain50 – 243194Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397305

Sites

Active site501Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18GX3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 865B6717E5EEEB70

FASTA24326,023
        10         20         30         40         50         60 
MRTPMNNDIS GRPDSLNGDR SDVFSPELGE FPNADDRAND IGDMETKTGT TTVGLKTQDG 

        70         80         90        100        110        120 
TVLATDMRAS LGRMVSSKDV QKVEEIHPTG ALTIAGSVSA AQSLISSIRA EVRLYEARRG 

       130        140        150        160        170        180 
EDMSMEALST LLGNFLRSGG FFIVQPILGG VDDDGPHIYS IDPAGSIIEE EYTVTGSGSQ 

       190        200        210        220        230        240 
YALGVLEQQY NEDLSIEEAK TVAARSIESA VERDLASGNG INVCVVTEDG VEITQHEDFE 


ELV 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790 / HBSQ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ52772.1.
RefSeqYP_658378.1. NC_008212.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362976.HQ2661A.

Protein family/group databases

MEROPST01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ52772; CAJ52772; HQ_2661A.
GeneID4194516.
KEGGhwa:HQ2661A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091083.
KOK03433.
OMAGYYIAHR.

Enzyme and pathway databases

BioCycHWAL362976:GJSR-1762-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.
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.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB_HALWD
AccessionPrimary (citable) accession number: Q18GX3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: July 25, 2006
Last modified: June 11, 2014
This is version 62 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