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Q53083

- PSB2_RHOER

UniProt

Q53083 - PSB2_RHOER

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
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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-SubCell
    2. proteasome core complex, beta-subunit complex Source: UniProtKB

    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

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    MTVDRAPRIT DGDTRLSFGS NLSSFSEYLR VHAPEHLPQN RFADTGGVVM    50
    GGGDVAPHGT TIVAISYAGG VLLAGDRRAT MGNLIASRDV QKVYVTDDYS 100
    AAGIAGTAGI AIELVRLFAV ELEHYEKIEG VPLTFDGKAN RLSSMVRGNL 150
    GAAMQGLAVV PLLVGYDLDA VDPSRAGRIV SYDVVGGRYE ERAGYHAVGS 200
    GSLFAKSALK KLYSPGIDED TALRFAVEAL YDAADDDSAT GGPDLTRGIY 250
    PTAVTITSAG AVELSTAKAA EIAREIVAAR TATASPEGES AL 292
    Length:292
    Mass (Da):30,398
    Last modified:November 1, 1996 - v1
    Checksum:i759E364233C73FBE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26422 Genomic DNA. Translation: AAC45736.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 61 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