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Protein

Proteasome subunit beta 1

Gene

prcB1

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

    Pathwayi

    Sites

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

    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 autocatalysisUniRule annotation1 PublicationPRO_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
    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...

    Protein-protein interaction databases

    DIPiDIP-29144N.
    IntActiQ53079. 1 interaction.

    Protein family/group databases

    MEROPSiT01.005.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00997.

    Miscellaneous databases

    EvolutionaryTraceiQ53079.

    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 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: May 27, 2015
    This is version 76 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

    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.