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Q53080

- PSA1_RHOER

UniProt

Q53080 - PSA1_RHOER

Protein

Proteasome subunit alpha 1

Gene

prcA1

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 72 (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

    GO - Molecular functioni

    1. endopeptidase activity Source: UniProtKB
    2. protein binding Source: IntAct
    3. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    UniPathwayiUPA00997.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha 1UniRule annotation (EC:3.4.25.1UniRule annotation)
    Alternative name(s):
    20S proteasome alpha subunit 1UniRule annotation
    Proteasome core protein PrcA 1UniRule annotation
    Gene namesi
    Name:prcA1UniRule 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, alpha-subunit complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 259259Proteasome subunit alpha 1PRO_0000397128Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    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
    prcB1Q530792EBI-1037564,EBI-1037574

    Protein-protein interaction databases

    DIPiDIP-29143N.
    IntActiQ53080. 1 interaction.

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2516
    Beta strandi30 – 345
    Beta strandi36 – 438
    Beta strandi48 – 503
    Beta strandi52 – 576
    Beta strandi60 – 667
    Helixi68 – 8821
    Helixi91 – 933
    Helixi96 – 11318
    Beta strandi114 – 1163
    Beta strandi120 – 1267
    Beta strandi130 – 1323
    Beta strandi137 – 1426
    Turni143 – 1453
    Beta strandi147 – 15913
    Helixi160 – 17011
    Helixi177 – 18812
    Beta strandi206 – 2127
    Beta strandi215 – 2173
    Beta strandi220 – 2223
    Helixi225 – 2295

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q5QX-ray2.60A/B/C/D/E/F/G1-259[»]
    1Q5RX-ray3.10A/B/C/D/E/F/G8-259[»]
    2H6JX-ray3.20A/B/C/D/E/F/G1-259[»]
    ProteinModelPortaliQ53080.
    SMRiQ53080. Positions 9-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53080.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.UniRule annotation

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00289_B. Proteasome_A_B.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR022296. Proteasome_asu_bac.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03691. 20S_bact_alpha. 1 hit.
    PROSITEiPS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q53080-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTFRDGVL FVAENPSTAL    50
    HKVSELYDRL GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA 100
    NAYAQTLGTI FTEQPKPYEV EICVAEVGRV GSPKAPQLYR ITYDGSIVDE 150
    QHFVVMGGTT EPIATAMRES YRADLDLEAA VGIAVNALRQ GGAGEGEKRN 200
    VDVASLEVAV LDQSRPRRAF RRIAGTALEQ LVPAEPAAAS ESAPEPKPDT 250
    ETKPADTQD 259
    Length:259
    Mass (Da):28,312
    Last modified:November 1, 1996 - v1
    Checksum:iC1A97CACA2D77050
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26421 Genomic DNA. Translation: AAC45741.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26421 Genomic DNA. Translation: AAC45741.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q5Q X-ray 2.60 A/B/C/D/E/F/G 1-259 [» ]
    1Q5R X-ray 3.10 A/B/C/D/E/F/G 8-259 [» ]
    2H6J X-ray 3.20 A/B/C/D/E/F/G 1-259 [» ]
    ProteinModelPortali Q53080.
    SMRi Q53080. Positions 9-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29143N.
    IntActi Q53080. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00997 .

    Miscellaneous databases

    EvolutionaryTracei Q53080.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_00289_B. Proteasome_A_B.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR022296. Proteasome_asu_bac.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03691. 20S_bact_alpha. 1 hit.
    PROSITEi PS51475. PROTEASOME_ALPHA_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], PARTIAL PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS, 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) IN COMPLEX WITH BETA 1 SUBUNIT, 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) IN COMPLEX WITH BETA 1 SUBUNIT, PROTEASOME ASSEMBLY PROCESS.

    Entry informationi

    Entry nameiPSA1_RHOER
    AccessioniPrimary (citable) accession number: Q53080
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 10, 2010
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 72 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