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C7NVQ4 (PSB_HALMD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 31. 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:Hmuk_0018
OrganismHalomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541) (Haloarcula mukohataei) [Complete proteome] [HAMAP]
Taxonomic identifier485914 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalomicrobium

Protein attributes

Sequence length237 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 – 4242Removed in mature form; by autocatalysis By similarity
PRO_0000397302
Chain43 – 237195Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397303

Sites

Active site431Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
C7NVQ4 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 44B1E4B09303DE57

FASTA23724,786
        10         20         30         40         50         60 
MSKFPDLPGM KNLDANPYEP ELASFDDMDA DAGDGDAVAK TGTTTIGITT DGGVVIATDM 

        70         80         90        100        110        120 
RASLGGRFVS NKSVQKVEQI HPSAALTLVG SVGGAQSFIR TLRSESDLYE VRRGEPMSIS 

       130        140        150        160        170        180 
ALATLAGNFA RGGPFFAINP ILGGVDEEGS HVYSIDPAGG VMEDDYTVTG SGMQVAHGKL 

       190        200        210        220        230 
EDRYHDDLSM EEAEELAVEA VYAATERDTG SGNGVYVATV TGDGVDITGY DDFEGAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001688 Genomic DNA. Translation: ACV46169.1.
RefSeqYP_003175876.1. NC_013202.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING485914.Hmuk_0018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV46169; ACV46169; Hmuk_0018.
GeneID8409514.
KEGGhmu:Hmuk_0018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091083.
KOK03433.
OMAMVDWLGT.

Enzyme and pathway databases

BioCycHMUK485914:GCKD-18-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_HALMD
AccessionPrimary (citable) accession number: C7NVQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: October 13, 2009
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