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D4GYZ1

- PSB_HALVD

UniProt

D4GYZ1 - PSB_HALVD

Protein

Proteasome subunit beta

Gene

psmB

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (18 May 2010)
      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 H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity.1 PublicationUniRule annotation

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.1 PublicationUniRule annotation

    Enzyme regulationi

    The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers 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 By similarity. In vitro, the chymotrypsin-like activity of the alpha1-beta proteasome is potently inhibited by carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I).1 PublicationUniRule annotation

    pH dependencei

    Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype).1 Publication

    Temperature dependencei

    Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501NucleophileUniRule annotation

    GO - Molecular functioni

    1. endopeptidase activity Source: UniProtKB
    2. threonine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciHVOL309800:GCOK-1565-MONOMER.

    Protein family/group databases

    MEROPSiT01.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit betaUniRule annotation (EC:3.4.25.1UniRule annotation)
    Alternative name(s):
    20S proteasome beta subunitUniRule annotation
    Proteasome core protein PsmBUniRule annotation
    Gene namesi
    Name:psmBUniRule annotation
    Ordered Locus Names:HVO_1562
    OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
    Taxonomic identifieri309800 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
    ProteomesiUP000008243: Chromosome

    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

    Pathology & Biotechi

    Disruption phenotypei

    Strains lacking psmB gene are inviable.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 4949Removed in mature form; by autocatalysis1 PublicationUniRule annotationPRO_0000397605Add
    BLAST
    Chaini50 – 243194Proteasome subunit betaPRO_0000397606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei129 – 1291Phosphoserine1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Phosphoprotein, Zymogen

    PTM databases

    PhosSiteiP0611175.

    Expressioni

    Inductioni

    Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmB is expressed at a high and relatively constant level throughout growth.1 Publication

    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. H.volcanii produces at least 2 types of 20S proteasomes: an alpha1-beta proteasome and a proteasome containing all three subunits (alpha1, alpha2, and beta) that appears to be asymmetrical with homo-oligomeric alpha1 and alpha2 rings positioned on separate ends. 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 at one or both ends by the proteasome regulatory ATPase, PAN.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliD4GYZ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000091083.
    KOiK03433.
    OMAiMVDWLGT.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_02113_A. Proteasome_B_A.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03634. arc_protsome_B. 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.

    D4GYZ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTPTHDEFS GRLDSLNGDR SNVFGPELGE FSNADRRADE LGDKETKTGT    50
    TTVGIKTEEG VVLATDMRAS MGYMVSSKDV QKVEEIHPTG ALTIAGSVSA 100
    AQSLISSLRA EVRLYEARRG EDMSMQALST LVGNFLRSGG FYVVQPILGG 150
    VDETGPHIYS IDPAGSILEE EYTVTGSGSQ YALGVLEQEF EDGLSIEEAK 200
    GVATKAIRSA VERDLASGNG INIAVVTEDG VDIQRHQNFE GLE 243
    Length:243
    Mass (Da):25,994
    Last modified:May 18, 2010 - v1
    Checksum:i6253E28ADDA40E61
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126262 Genomic DNA. Translation: AAD53406.1.
    CP001956 Genomic DNA. Translation: ADE03141.1.
    PIRiT48677.
    RefSeqiYP_003535609.1. NC_013967.1.

    Genome annotation databases

    EnsemblBacteriaiADE03141; ADE03141; HVO_1562.
    GeneIDi8923965.
    KEGGihvo:HVO_1562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126262 Genomic DNA. Translation: AAD53406.1 .
    CP001956 Genomic DNA. Translation: ADE03141.1 .
    PIRi T48677.
    RefSeqi YP_003535609.1. NC_013967.1.

    3D structure databases

    ProteinModelPortali D4GYZ1.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi T01.002.

    PTM databases

    PhosSitei P0611175.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADE03141 ; ADE03141 ; HVO_1562 .
    GeneIDi 8923965.
    KEGGi hvo:HVO_1562.

    Phylogenomic databases

    HOGENOMi HOG000091083.
    KOi K03433.
    OMAi MVDWLGT.

    Enzyme and pathway databases

    BioCyci HVOL309800:GCOK-1565-MONOMER.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_02113_A. Proteasome_B_A.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03634. arc_protsome_B. 1 hit.
    PROSITEi PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis."
      Wilson H.L., Aldrich H.C., Maupin-Furlow J.
      J. Bacteriol. 181:5814-5824(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-79, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SALT REQUIREMENT, SUBUNIT.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
    3. "Subunit topology of two 20S proteasomes from Haloferax volcanii."
      Kaczowka S.J., Maupin-Furlow J.A.
      J. Bacteriol. 185:165-174(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    4. "Differential regulation of the PanA and PanB proteasome-activating nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax volcanii."
      Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.
      J. Bacteriol. 186:7763-7772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii."
      Humbard M.A., Stevens S.M. Jr., Maupin-Furlow J.A.
      J. Bacteriol. 188:7521-7530(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-129.
    6. "Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii."
      Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.
      J. Bacteriol. 190:8096-8105(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPSB_HALVD
    AccessioniPrimary (citable) accession number: D4GYZ1
    Secondary accession number(s): Q9V2V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    H.volcanii proteasome requires high concentrations of salt, similar to the extracellular environment and cytoplasm of this organism, for complex stability and optimal activity.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3