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Protein

Proteasome subunit beta 2

Gene

prcB2

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation2 Publications

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

    Pathway: proteasomal Pup-dependent pathway

    This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei60 – 601NucleophileUniRule annotation

    GO - Molecular functioni

    • endopeptidase activity Source: UniProtKB
    • threonine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    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 lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • 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 autocatalysisUniRule annotation1 PublicationPRO_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

    Protein-protein interaction databases

    STRINGi234621.RER_31740.

    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

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

    Protein-protein interaction databases

    STRINGi234621.RER_31740.

    Protein family/group databases

    MEROPSiT01.005.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00997.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 64 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.