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A4X744 (PSB2_SALTO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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 2

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit 2
Proteasome core protein PrcB 2
Gene names
Name:prcB2
Ordered Locus Names:Strop_2244
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length279 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 caution

The sequence ABP54694.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5353Removed in mature form; by autocatalysis By similarity
PRO_0000397578
Chain54 – 279226Proteasome subunit beta 2 HAMAP-Rule MF_02113
PRO_0000397579

Sites

Active site541Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A4X744 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: 93BE035FAAFE271B

FASTA27928,788
        10         20         30         40         50         60 
MAAAFDPSGR FPDLFTSVGT SSFSAFLSKA APELLPGRRP LPPGMATGLT PHATTIVAIA 

        70         80         90        100        110        120 
TAGGVVLAGD RRATMGNLIA QRDVEKVHPA DAYSLVGMAG AAGIGIELTR LFQVELEHYE 

       130        140        150        160        170        180 
KTEGAMLSLD GKANRLAAMV RGNLGAAMQG LAVVPLFAGF DLAATDPAKA GRIFSFDVTG 

       190        200        210        220        230        240 
GPYEETGYDA VGSGSVFAKS ALKKRFRLGL SVDDAVRLAV EALYDAADDD TATGGPDLTR 

       250        260        270 
RIYPVVMSAT AEGTHRLTEA ETAAIAESVV AGRMENPGG 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP54694.1. Different initiation.
RefSeqYP_001159072.1. NC_009380.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING369723.Strop_2244.

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP54694; ABP54694; Strop_2244.
GeneID5058707.
KEGGstp:Strop_2244.
PATRIC23443520. VBISalTro43511_2302.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245308.
KOK03433.
OrthoDBEOG6XM79W.

Enzyme and pathway databases

BioCycSTRO369723:GI49-2278-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 namePSB2_SALTO
AccessionPrimary (citable) accession number: A4X744
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: June 11, 2014
This is version 52 of the entry and version 2 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