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Q53083

- PSB2_RHOER

UniProt

Q53083 - PSB2_RHOER

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Protein

Proteasome subunit beta 2

Gene

prcB2

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 sitei60 – 601NucleophileUniRule 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 2UniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome beta subunit 2UniRule annotation
Proteasome core protein PrcB 2UniRule annotation
Gene namesi
Name:prcB2UniRule 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5959Removed in mature form; by autocatalysis1 PublicationUniRule annotationPRO_0000397126Add
BLAST
Chaini60 – 292233Proteasome subunit beta 2PRO_0000397127Add
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.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ53083.
SMRiQ53083. Positions 16-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.

Q53083-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVDRAPRIT DGDTRLSFGS NLSSFSEYLR VHAPEHLPQN RFADTGGVVM
60 70 80 90 100
GGGDVAPHGT TIVAISYAGG VLLAGDRRAT MGNLIASRDV QKVYVTDDYS
110 120 130 140 150
AAGIAGTAGI AIELVRLFAV ELEHYEKIEG VPLTFDGKAN RLSSMVRGNL
160 170 180 190 200
GAAMQGLAVV PLLVGYDLDA VDPSRAGRIV SYDVVGGRYE ERAGYHAVGS
210 220 230 240 250
GSLFAKSALK KLYSPGIDED TALRFAVEAL YDAADDDSAT GGPDLTRGIY
260 270 280 290
PTAVTITSAG AVELSTAKAA EIAREIVAAR TATASPEGES AL
Length:292
Mass (Da):30,398
Last modified:November 1, 1996 - v1
Checksum:i759E364233C73FBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26422 Genomic DNA. Translation: AAC45736.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26422 Genomic DNA. Translation: AAC45736.1 .

3D structure databases

ProteinModelPortali Q53083.
SMRi Q53083. Positions 16-278.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi T01.005.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00997 .

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 60-92; 139-156; 211-228 AND 269-292, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT.
    Strain: NI86/21.
  2. Cited for: SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
    Strain: NI86/21.

Entry informationi

Entry nameiPSB2_RHOER
AccessioniPrimary (citable) accession number: Q53083
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 62 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3