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Q53079 (PSB1_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity. Ref.1 Ref.2

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.1 Ref.2

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. All four combinations of alpha- and beta-subunits (beta2-alpha1, beta2-alpha2, beta1-alpha2 and beta1-alpha1) yield fully assembled and proteolytically active proteasomes. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped by the proteasome-associated ATPase, ARC. Ref.1 Ref.2 Ref.3 Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02113.

Domain

In contrast to M.tuberculosis, the propeptide is required for correct proteasome folding and assembly. The propeptide is positioned strategically at the region where it can act as an assembly-promoting factor by linking its own beta-subunit to two adjacent alpha-subunits at the same time. Ref.3

Sequence similarities

Belongs to the peptidase T1B family.

Biophysicochemical properties

Kinetic parameters:

The Vmax observed with the beta2-alpha1 proteasome subtype is 2.2-fold, 1.2-fold and 4-fold higher than that with the beta2-alpha2, beta1-alpha2 and beta1-alpha1 subtypes, respectively.

KM=61.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype) Ref.2

KM=66.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha2 proteasome subtype)

KM=71.2 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2 proteasome subtype)

KM=84.3 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1 proteasome subtype)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

prcA1Q530802EBI-1037574,EBI-1037564

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 6565Removed in mature form; by autocatalysis HAMAP-Rule MF_02113
PRO_0000397124
Chain66 – 294229Proteasome subunit beta 1 HAMAP-Rule MF_02113
PRO_0000397125

Sites

Active site661Nucleophile By similarity

Experimental info

Mutagenesis2101F → A: Prevents full assembly of proteasome. Ref.4
Mutagenesis216 – 2172KK → AA: Prevents full assembly of proteasome.

Secondary structure

................................................. 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q53079 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 57914462BA4A05CD

FASTA29431,161
        10         20         30         40         50         60 
MTADRPALRT GDRDTRLSFG SNLSSFTDYL RGHAPELLPE NRIGHRSHST RGGDGMESGD 

        70         80         90        100        110        120 
LAPHGTTIVA LTYKGGVLLA GDRRATQGNL IASRDVEKVY VTDEYSAAGI AGTAGIAIEL 

       130        140        150        160        170        180 
VRLFAVELEH YEKIEGVPLT FDGKANRLAS MVRGNLGAAM QGLAVVPLLV GYDLDADDES 

       190        200        210        220        230        240 
RAGRIVSYDV VGGRYEERAG YHAVGSGSLF AKSALKKIYS PDSDEETALR AAIESLYDAA 

       250        260        270        280        290 
DDDSATGGPD LTRGIYPTAV TITQAGAVHV SEETTSELAR RIVAERTEQG GSAR 

« Hide

References

[1]"The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus."
Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., de Mot R., Baumeister W.
Curr. Biol. 5:766-774(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 66-75, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: NI86/21.
[2]"Subunit topology of the Rhodococcus proteasome."
Zuhl F., Tamura T., Dolenc I., Cejka Z., Nagy I., De Mot R., Baumeister W.
FEBS Lett. 400:83-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
Strain: NI86/21.
[3]"Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly."
Kwon Y.D., Nagy I., Adams P.D., Baumeister W., Jap B.K.
J. Mol. Biol. 335:233-245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF PROCESSED AND UNPROCESSED FORMS IN COMPLEX WITH ALPHA 1 SUBUNIT, SUBUNIT, DOMAIN, PROTEASOME ASSEMBLY PROCESS.
[4]"Proteasome assembly triggers a switch required for active-site maturation."
Witt S., Kwon Y.D., Sharon M., Felderer K., Beuttler M., Robinson C.V., Baumeister W., Jap B.K.
Structure 14:1179-1188(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF MUTANT ALA-210 IN COMPLEX WITH ALPHA 1 SUBUNIT, PROTEASOME ASSEMBLY PROCESS, SUBUNIT, MUTAGENESIS OF PHE-210 AND 216-LYS-LYS-217, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26421 Genomic DNA. Translation: AAC45740.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q5QX-ray2.60H/I/J/K/L/M/N66-294[»]
1Q5RX-ray3.10H/I/J/K/L/M/N1-293[»]
2H6JX-ray3.20H/I/J/K/L/M/N1-292[»]
ProteinModelPortalQ53079.
SMRQ53079. Positions 17-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29144N.
IntActQ53079. 1 interaction.

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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...

Other

EvolutionaryTraceQ53079.

Entry information

Entry namePSB1_RHOER
AccessionPrimary (citable) accession number: Q53079
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 70 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways