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P96086

- TRI_THEAC

UniProt

P96086 - TRI_THEAC

Protein

Tricorn protease

Gene

tri

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.

    pH dependencei

    Optimum pH is 8.5-8.8.

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei746 – 7461Charge relay system
    Sitei936 – 9361Substrate specificity switch
    Active sitei965 – 9651Charge relay system
    Active sitei966 – 9661Charge relay systemSequence Analysis

    GO - Molecular functioni

    1. serine-type peptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS41.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tricorn protease (EC:3.4.21.-)
    Gene namesi
    Name:tri
    Ordered Locus Names:Ta1490
    OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
    Taxonomic identifieri273075 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001024: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1322RR → EE: Retains 10% of wild-type activity.
    Mutagenesisi184 – 1841L → C: After modification of the thiol group by maleimide, retains less than 50% of wild-type activity. Blocks product exit from the catalytic chamber.
    Mutagenesisi414 – 4141R → C: After modification of thiol group by maleimide, retains 50% of wild-type activity. Blocks substrate access to active site.
    Mutagenesisi746 – 7461H → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi965 – 9651S → A: Loss of catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10711071Tricorn proteasePRO_0000207197Add
    BLAST

    Proteomic databases

    PRIDEiP96086.

    Interactioni

    Subunit structurei

    Part of the Tricorn proteolytic complex. Assembles to form a hexameric toroid, 20 copies of which may then assemble to form an icosahedral supermolecule of 14.6 MDa.

    Protein-protein interaction databases

    STRINGi273075.Ta1490.

    Structurei

    Secondary structure

    1
    1071
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 496
    Beta strandi52 – 576
    Beta strandi60 – 656
    Turni66 – 683
    Beta strandi71 – 755
    Beta strandi77 – 8610
    Beta strandi90 – 10011
    Beta strandi105 – 1128
    Turni113 – 1164
    Beta strandi117 – 1204
    Beta strandi126 – 1294
    Beta strandi135 – 1406
    Beta strandi146 – 1505
    Beta strandi154 – 1563
    Beta strandi161 – 1666
    Turni167 – 1704
    Beta strandi171 – 1744
    Beta strandi181 – 1866
    Beta strandi189 – 1957
    Beta strandi212 – 2187
    Beta strandi221 – 2266
    Beta strandi233 – 2386
    Beta strandi241 – 2466
    Beta strandi253 – 2586
    Beta strandi275 – 2839
    Beta strandi285 – 2895
    Beta strandi292 – 2965
    Turni298 – 3003
    Beta strandi303 – 3053
    Beta strandi316 – 3205
    Helixi322 – 3254
    Beta strandi326 – 3316
    Helixi333 – 3353
    Beta strandi337 – 3415
    Beta strandi344 – 3485
    Beta strandi352 – 3576
    Beta strandi364 – 3696
    Beta strandi371 – 38111
    Beta strandi384 – 3918
    Turni392 – 3943
    Beta strandi397 – 3993
    Beta strandi406 – 4127
    Beta strandi416 – 4238
    Beta strandi426 – 4327
    Turni433 – 4353
    Beta strandi438 – 4436
    Beta strandi445 – 4473
    Beta strandi452 – 4543
    Beta strandi460 – 4678
    Beta strandi477 – 4848
    Turni485 – 4884
    Beta strandi489 – 4924
    Beta strandi496 – 50510
    Beta strandi511 – 5177
    Beta strandi526 – 5294
    Beta strandi537 – 5459
    Helixi551 – 5533
    Helixi557 – 5593
    Helixi571 – 5744
    Beta strandi585 – 5906
    Beta strandi592 – 5998
    Helixi606 – 6116
    Beta strandi617 – 6237
    Turni624 – 6263
    Beta strandi629 – 64113
    Beta strandi643 – 6453
    Beta strandi647 – 6526
    Beta strandi657 – 6637
    Beta strandi678 – 6814
    Helixi682 – 70019
    Helixi704 – 71916
    Helixi720 – 7245
    Helixi728 – 74013
    Beta strandi766 – 7727
    Beta strandi775 – 7817
    Beta strandi788 – 7903
    Helixi794 – 7985
    Beta strandi806 – 8105
    Beta strandi816 – 8194
    Helixi821 – 8266
    Turni827 – 8304
    Beta strandi831 – 8388
    Beta strandi840 – 8423
    Beta strandi844 – 8507
    Helixi856 – 87419
    Turni875 – 8773
    Beta strandi878 – 8836
    Helixi889 – 90214
    Beta strandi905 – 9117
    Helixi921 – 9288
    Beta strandi934 – 9418
    Beta strandi944 – 9474
    Beta strandi953 – 9597
    Helixi966 – 97611
    Beta strandi979 – 9857
    Beta strandi992 – 9943
    Beta strandi1011 – 10155
    Turni1016 – 10183
    Turni1020 – 10256
    Beta strandi1030 – 10323
    Helixi1037 – 10415
    Helixi1046 – 105813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K32X-ray2.00A/B/C/D/E/F27-1071[»]
    1N6DX-ray2.80A/B/C/D/E/F1-1071[»]
    1N6EX-ray2.60A/C/E/G/I/K1-1071[»]
    1N6FX-ray2.70A/B/C/D/E/F1-1071[»]
    DisProtiDP00484.
    ProteinModelPortaliP96086.
    SMRiP96086. Positions 39-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96086.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 310272Six-bladed beta propellerAdd
    BLAST
    Regioni131 – 1322Binds the substrate's C-terminus
    Regioni326 – 675350Seven-bladed beta propellerAdd
    BLAST
    Regioni681 – 75272C-1Add
    BLAST
    Regioni761 – 85595PDZ-likeAdd
    BLAST
    Regioni856 – 1061206C-2Add
    BLAST
    Regioni916 – 9183Substrate binding

    Domaini

    It is thought that substrate reaches the active site through the seven-bladed beta propeller channel, while products exit via the six-bladed beta propeller channel.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase S41B family.Curated

    Phylogenomic databases

    eggNOGiCOG0793.
    HOGENOMiHOG000243096.
    KOiK08676.
    OMAiKSVYAIS.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.30.42.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR011659. PD40.
    IPR001478. PDZ.
    IPR005151. Tail-specific_protease.
    IPR028204. Tricorn_C1.
    IPR029414. Tricorn_PDZ.
    IPR012393. Tricorn_protease.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF07676. PD40. 1 hit.
    PF03572. Peptidase_S41. 1 hit.
    PF14684. Tricorn_C1. 1 hit.
    PF14685. Tricorn_PDZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036421. Tricorn_protease. 1 hit.
    SMARTiSM00245. TSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    SSF52096. SSF52096. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P96086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSLMSFGSC QWIDQGRFSR SLYRNFKTFK LHEMHGLCMP NLLLNPDIHG     50
    DRIIFVCCDD LWEHDLKSGS TRKIVSNLGV INNARFFPDG RKIAIRVMRG 100
    SSLNTADLYF YNGENGEIKR ITYFSGKSTG RRMFTDVAGF DPDGNLIIST 150
    DAMQPFSSMT CLYRVENDGI NFVPLNLGPA THILFADGRR VIGRNTFELP 200
    HWKGYRGGTR GKIWIEVNSG AFKKIVDMST HVSSPVIVGH RIYFITDIDG 250
    FGQIYSTDLD GKDLRKHTSF TDYYPRHLNT DGRRILFSKG GSIYIFNPDT 300
    EKIEKIEIGD LESPEDRIIS IPSKFAEDFS PLDGDLIAFV SRGQAFIQDV 350
    SGTYVLKVPE PLRIRYVRRG GDTKVAFIHG TREGDFLGIY DYRTGKAEKF 400
    EENLGNVFAM GVDRNGKFAV VANDRFEIMT VDLETGKPTV IERSREAMIT 450
    DFTISDNSRF IAYGFPLKHG ETDGYVMQAI HVYDMEGRKI FAATTENSHD 500
    YAPAFDADSK NLYYLSYRSL DPSPDRVVLN FSFEVVSKPF VIPLIPGSPN 550
    PTKLVPRSMT SEAGEYDLND MYKRSSPINV DPGDYRMIIP LESSILIYSV 600
    PVHGEFAAYY QGAPEKGVLL KYDVKTRKVT EVKNNLTDLR LSADRKTVMV 650
    RKDDGKIYTF PLEKPEDERT VETDKRPLVS SIHEEFLQMY DEAWKLARDN 700
    YWNEAVAKEI SERIYEKYRN LVPLCKTRYD LSNVIVEMQG EYRTSHSYEM 750
    GGTFTDKDPF RSGRIACDFK LDGDHYVVAK AYAGDYSNEG EKSPIFEYGI 800
    DPTGYLIEDI DGETVGAGSN IYRVLSEKAG TSARIRLSGK GGDKRDLMID 850
    ILDDDRFIRY RSWVEANRRY VHERSKGTIG YIHIPDMGMM GLNEFYRLFI 900
    NESSYQGLIV DVRFNGGGFV SQLIIEKLMN KRIGYDNPRR GTLSPYPTNS 950
    VRGKIIAITN EYAGSDGDIF SFSFKKLGLG KLIGTRTWGG VVGITPKRRL 1000
    IDGTVLTQPE FAFWFRDAGF GVENYGVDPD VEIEYAPHDY LSGKDPQIDY 1050
    AIDALIEELR NWNEELPQRP S 1071
    Length:1,071
    Mass (Da):121,623
    Last modified:May 1, 1997 - v1
    Checksum:iD8C5579436870710
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72850 Genomic DNA. Translation: AAC44621.1.
    AL445067 Genomic DNA. Translation: CAC12608.1.
    PIRiT43255.
    RefSeqiNP_394941.1. NC_002578.1.
    WP_010901890.1. NC_002578.1.

    Genome annotation databases

    EnsemblBacteriaiCAC12608; CAC12608; CAC12608.
    GeneIDi1456939.
    KEGGitac:Ta1490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72850 Genomic DNA. Translation: AAC44621.1 .
    AL445067 Genomic DNA. Translation: CAC12608.1 .
    PIRi T43255.
    RefSeqi NP_394941.1. NC_002578.1.
    WP_010901890.1. NC_002578.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K32 X-ray 2.00 A/B/C/D/E/F 27-1071 [» ]
    1N6D X-ray 2.80 A/B/C/D/E/F 1-1071 [» ]
    1N6E X-ray 2.60 A/C/E/G/I/K 1-1071 [» ]
    1N6F X-ray 2.70 A/B/C/D/E/F 1-1071 [» ]
    DisProti DP00484.
    ProteinModelPortali P96086.
    SMRi P96086. Positions 39-1061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273075.Ta1490.

    Protein family/group databases

    MEROPSi S41.005.

    Proteomic databases

    PRIDEi P96086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC12608 ; CAC12608 ; CAC12608 .
    GeneIDi 1456939.
    KEGGi tac:Ta1490.

    Phylogenomic databases

    eggNOGi COG0793.
    HOGENOMi HOG000243096.
    KOi K08676.
    OMAi KSVYAIS.

    Miscellaneous databases

    EvolutionaryTracei P96086.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.30.42.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR011659. PD40.
    IPR001478. PDZ.
    IPR005151. Tail-specific_protease.
    IPR028204. Tricorn_C1.
    IPR029414. Tricorn_PDZ.
    IPR012393. Tricorn_protease.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF07676. PD40. 1 hit.
    PF03572. Peptidase_S41. 1 hit.
    PF14684. Tricorn_C1. 1 hit.
    PF14685. Tricorn_PDZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036421. Tricorn_protease. 1 hit.
    SMARTi SM00245. TSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    SSF52096. SSF52096. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Tricorn protease -- the core of a modular proteolytic system."
      Tamura T., Tamura N., Cejka Z., Hegerl R., Lottspeich F., Baumeister W.
      Science 274:1385-1389(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 120-126; 290-304; 376-392; 490-506; 554-560; 634-638; 676-684; 696-708; 709-716 AND 932-946.
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    2. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
      Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
      Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    3. "The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation."
      Tamura N., Lottspeich F., Baumeister W., Tamura T.
      Cell 95:637-648(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF PROTEIN INTERACTION.
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    4. "Tricorn protease exists as an icosahedral supermolecule in vivo."
      Walz J., Tamura T., Tamura N., Grimm R., Baumeister W., Koster A.J.
      Mol. Cell 1:59-65(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: THREE-DIMENSIONAL RECONSTRUCTION FROM ELECTRON MICROGRAPHS.
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    5. "Capsids of Tricorn protease studied by electron cryomicroscopy."
      Walz J., Koster A.J., Tamura T., Baumeister W.
      J. Struct. Biol. 128:65-68(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: THREE-DIMENSIONAL RECONSTRUCTION (1.3 NM) BY ELECTRON CRYOMICROSCOPY.
    6. "Beta-propeller repeats and a PDZ domain in the Tricorn protease: predicted self-compartmentalisation and C-terminal polypeptide-binding strategies of substrate selection."
      Ponting C.P., Pallen M.J.
      FEMS Microbiol. Lett. 179:447-451(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    7. "Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum."
      Bosch J., Tamura T., Bourenkov G., Baumeister W., Essen L.-O.
      J. Struct. Biol. 134:83-87(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    8. "Crystal structure of the tricorn protease reveals a protein disassembly line."
      Brandstetter H., Kim J.-S., Groll M., Huber R.
      Nature 414:466-470(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF 131-ARG-ARG-132; HIS-746 AND SER-965.
    9. "Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum."
      Kim J.-S., Groll M., Musiol H.-J., Behrendt R., Kaiser M., Moroder L., Huber R., Brandstetter H.
      J. Mol. Biol. 324:1041-1050(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiTRI_THEAC
    AccessioniPrimary (citable) accession number: P96086
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 113 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3