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Q53079

- PSB1_RHOER

UniProt

Q53079 - PSB1_RHOER

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Protein

Proteasome subunit beta 1

Gene

prcB1

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 PublicationsUniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.2 PublicationsUniRule annotation

Enzyme regulationi

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.UniRule annotation

Kineticsi

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.

  1. KM=61.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype)1 Publication
  2. KM=66.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha2 proteasome subtype)1 Publication
  3. KM=71.2 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2 proteasome subtype)1 Publication
  4. KM=84.3 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1 proteasome subtype)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661NucleophileUniRule annotation

GO - Molecular functioni

  1. endopeptidase activity Source: UniProtKB
  2. threonine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. modification-dependent protein catabolic process Source: UniProtKB-HAMAP
  2. proteasomal protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

UniPathwayiUPA00997.

Protein family/group databases

MEROPSiT01.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta 1UniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome beta subunit 1UniRule annotation
Proteasome core protein PrcB 1UniRule annotation
Gene namesi
Name:prcB1UniRule annotation
OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifieri1833 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. proteasome core complex, beta-subunit complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101F → A: Prevents full assembly of proteasome. 1 Publication
Mutagenesisi216 – 2172KK → AA: Prevents full assembly of proteasome. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 6565Removed in mature form; by autocatalysis1 PublicationUniRule annotationPRO_0000397124Add
BLAST
Chaini66 – 294229Proteasome subunit beta 1PRO_0000397125Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
prcA1Q530802EBI-1037574,EBI-1037564

Protein-protein interaction databases

DIPiDIP-29144N.
IntActiQ53079. 1 interaction.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 305Combined sources
Turni31 – 333Combined sources
Helixi35 – 373Combined sources
Beta strandi68 – 725Combined sources
Beta strandi77 – 815Combined sources
Beta strandi85 – 873Combined sources
Beta strandi90 – 945Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi106 – 1127Combined sources
Helixi114 – 13522Combined sources
Helixi141 – 15313Combined sources
Helixi156 – 1594Combined sources
Turni160 – 1623Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi199 – 2057Combined sources
Helixi208 – 21811Combined sources
Helixi225 – 24218Combined sources
Turni244 – 2463Combined sources
Turni251 – 2544Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi266 – 2694Combined sources
Helixi272 – 28716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ53079.
SMRiQ53079. Positions 17-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53079.

Family & Domainsi

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_B. Proteasome_B_B.
InterProiIPR029055. Ntn_hydrolases_N.
IPR022483. Pept_T1A_Psome_suB_actinobac.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03690. 20S_bact_beta. 1 hit.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q53079-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTADRPALRT GDRDTRLSFG SNLSSFTDYL RGHAPELLPE NRIGHRSHST
60 70 80 90 100
RGGDGMESGD LAPHGTTIVA LTYKGGVLLA GDRRATQGNL IASRDVEKVY
110 120 130 140 150
VTDEYSAAGI AGTAGIAIEL VRLFAVELEH YEKIEGVPLT FDGKANRLAS
160 170 180 190 200
MVRGNLGAAM QGLAVVPLLV GYDLDADDES RAGRIVSYDV VGGRYEERAG
210 220 230 240 250
YHAVGSGSLF AKSALKKIYS PDSDEETALR AAIESLYDAA DDDSATGGPD
260 270 280 290
LTRGIYPTAV TITQAGAVHV SEETTSELAR RIVAERTEQG GSAR
Length:294
Mass (Da):31,161
Last modified:November 1, 1996 - v1
Checksum:i57914462BA4A05CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26421 Genomic DNA. Translation: AAC45740.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26421 Genomic DNA. Translation: AAC45740.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q5Q X-ray 2.60 H/I/J/K/L/M/N 66-294 [» ]
1Q5R X-ray 3.10 H/I/J/K/L/M/N 1-293 [» ]
2H6J X-ray 3.20 H/I/J/K/L/M/N 1-292 [» ]
ProteinModelPortali Q53079.
SMRi Q53079. Positions 17-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29144N.
IntActi Q53079. 1 interaction.

Protein family/group databases

MEROPSi T01.005.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00997 .

Miscellaneous databases

EvolutionaryTracei Q53079.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_02113_B. Proteasome_B_B.
InterProi IPR029055. Ntn_hydrolases_N.
IPR022483. Pept_T1A_Psome_suB_actinobac.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR03690. 20S_bact_beta. 1 hit.
PROSITEi PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiPSB1_RHOER
AccessioniPrimary (citable) accession number: Q53079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3