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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: 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)DescriptionActionsGraphical viewLength
    Active sitei66NucleophileUniRule annotation1

    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 lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi210F → A: Prevents full assembly of proteasome. 1 Publication1
    Mutagenesisi216 – 217KK → AA: Prevents full assembly of proteasome. 1 Publication2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    PropeptideiPRO_00003971241 – 65Removed in mature form; by autocatalysisUniRule annotation1 PublicationAdd BLAST65
    ChainiPRO_000039712566 – 294Proteasome subunit beta 1Add BLAST229

    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 interactor.

    Structurei

    Secondary structure

    1294
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi26 – 30Combined sources5
    Turni31 – 33Combined sources3
    Helixi35 – 37Combined sources3
    Beta strandi68 – 72Combined sources5
    Beta strandi77 – 81Combined sources5
    Beta strandi85 – 87Combined sources3
    Beta strandi90 – 94Combined sources5
    Beta strandi99 – 103Combined sources5
    Beta strandi106 – 112Combined sources7
    Helixi114 – 135Combined sources22
    Helixi141 – 153Combined sources13
    Helixi156 – 159Combined sources4
    Turni160 – 162Combined sources3
    Beta strandi165 – 172Combined sources8
    Beta strandi183 – 188Combined sources6
    Beta strandi190 – 192Combined sources3
    Beta strandi194 – 196Combined sources3
    Beta strandi199 – 205Combined sources7
    Helixi208 – 218Combined sources11
    Helixi225 – 242Combined sources18
    Turni244 – 246Combined sources3
    Turni251 – 254Combined sources4
    Beta strandi258 – 263Combined sources6
    Beta strandi266 – 269Combined sources4
    Helixi272 – 287Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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. 1 hit.
    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-29144N.
    IntActiQ53079. 1 interactor.

    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. 1 hit.
    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...

    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 2, 2016
    This is version 81 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

    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 one 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.