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Q9V2V6

- PSA1_HALVD

UniProt

Q9V2V6 - PSA1_HALVD

Protein

Proteasome subunit alpha 1

Gene

psmA1

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 87 (01 Oct 2014)
      Sequence version 2 (13 Jul 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

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciHVOL309800:GCOK-1095-MONOMER.

    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 PsmA 1UniRule annotation
    Cleaved into the following chain:
    Proteasome subunit alpha 1, N-terminally processedUniRule annotation
    Gene namesi
    Name:psmA1UniRule annotation
    Synonyms:psmA
    Ordered Locus Names:HVO_1091
    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, alpha-subunit complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    Pathology & Biotechi

    Disruption phenotypei

    Strains lacking psmA1 gene alone display relatively normal growth rate and overall cell yield, but they are more sensitive to growth on organic versus inorganic nitrogen sources and hypo-osmotic stress, and they show limited growth in the presence of L-canavanine. Abolition of alpha1 subunit synthesis also has a severe impact on the ability of cells to withstand thermal stress. Moreover, depletion of psmA1 and psmA2 together renders the cells inviable.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 1211Missing: Prevents acetylation of Met-1. Enhances peptidase activity of the proteasome. Renders the cells less tolerant of hypoosmotic stress than the wild-type. 1 PublicationAdd
    BLAST
    Mutagenesisi2 – 21Q → A: Enhances cleavage of PsmA1 by methionine aminopeptidase (MAP), resulting in acetylation of the N-terminal alanine. Enhances peptidase activity of the proteasome. Renders the cells less tolerant of hypoosmotic stress than the wild-type. 1 Publication
    Mutagenesisi2 – 21Q → D, P or T: Does not alter the prevalence of the alpha1 subunit in N-acetylated form in proteasomes. Renders the cells more tolerant of hypoosmotic and high-temperature stress than the wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Proteasome subunit alpha 1PRO_0000124171Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 252251Proteasome subunit alpha 1, N-terminally processedPRO_0000397604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; alternate2 Publications

    Post-translational modificationi

    Acetylated. The acetylated form at Met-1 was shown to be in 100-fold excess of the unacetylated form with the initiator methionine removed in whole cells and purified 20S proteasomes.2 Publications

    Keywords - PTMi

    Acetylation

    Expressioni

    Inductioni

    Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmA 1 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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000091085.
    KOiK03432.
    OMAiFQVNYAR.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00289_A. Proteasome_A_A.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR019982. Proteasome_asu_arc.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03633. arc_protsome_A. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9V2V6-1 [UniParc]FASTAAdd to Basket

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    MQGQAQQQAY DRGITIFSPD GRLYQVEYAR EAVKRGTASI GVRTPEGVVL    50
    AADKRSRSPL MEPTSVEKIH KADDHIGIAS AGHVADARQL IDFARRQSQV 100
    NRLRYGEPIG IETLTKEVTD HIQQYTQVGG ARPFGVALLI GGVENGTPRL 150
    YETDPSGTPY EWKAVSIGAD RGDHQEHLEE NFRDDLTLDE GIELALEAIA 200
    STSDEGTAPD GVDVATVSAE TERFVELSND EIESYLEAND LLATEDDEQT 250
    EE 252
    Length:252
    Mass (Da):27,613
    Last modified:July 13, 2010 - v2
    Checksum:i500A2DCCB0B71C71
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961R → H in AAD53404. (PubMed:10482525)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126260 Genomic DNA. Translation: AAD53404.1.
    CP001956 Genomic DNA. Translation: ADE04430.1.
    PIRiT48678.
    RefSeqiWP_004043847.1. NZ_AOHU01000092.1.
    YP_003535146.1. NC_013967.1.

    Genome annotation databases

    EnsemblBacteriaiADE04430; ADE04430; HVO_1091.
    GeneIDi8925549.
    KEGGihvo:HVO_1091.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126260 Genomic DNA. Translation: AAD53404.1 .
    CP001956 Genomic DNA. Translation: ADE04430.1 .
    PIRi T48678.
    RefSeqi WP_004043847.1. NZ_AOHU01000092.1.
    YP_003535146.1. NC_013967.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADE04430 ; ADE04430 ; HVO_1091 .
    GeneIDi 8925549.
    KEGGi hvo:HVO_1091.

    Phylogenomic databases

    HOGENOMi HOG000091085.
    KOi K03432.
    OMAi FQVNYAR.

    Enzyme and pathway databases

    BioCyci HVOL309800:GCOK-1095-MONOMER.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_00289_A. Proteasome_A_A.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR019982. Proteasome_asu_arc.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03633. arc_protsome_A. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_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 23-30; 89-95 AND 150-163, BLOCKAGE OF N-TERMINUS, 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: ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE.
    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.
    7. "The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii."
      Humbard M.A., Zhou G., Maupin-Furlow J.A.
      J. Bacteriol. 191:3794-3803(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, MUTAGENESIS OF GLN-2 AND 2-GLN--ARG-12.

    Entry informationi

    Entry nameiPSA1_HALVD
    AccessioniPrimary (citable) accession number: Q9V2V6
    Secondary accession number(s): D4GW11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 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