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P96086

- TRI_THEAC

UniProt

P96086 - TRI_THEAC

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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

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 system2 Publications
Sitei936 – 9361Substrate specificity switch1 Publication
Active sitei965 – 9651Nucleophile2 Publications
Sitei966 – 9661Transition state stabilizer; via amide nitrogen2 Publications
Active sitei1023 – 10231Charge relay system1 Publication

GO - Molecular functioni

  1. serine-type peptidase activity Source: UniProtKB
Complete GO annotation...

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.-1 Publication)
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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1322RR → EE: Decreased catalytic activity towards protein substrates. Retains 10% of wild-type activity towards casein and about 30% towards oxidized insulin beta chain. However, there is no change in the activity for a tripeptide substrate. 2 Publications
Mutagenesisi184 – 1841L → C: Both peptidolytic and proteolytic activities doubled, probably due to the increase of the diameter of the channel for product exit. Retains less than 50% of wild-type activity after modification of the thiol group by maleimide, which decreases the diameter of the exit channel and impairs product exit from the catalytic chamber. 2 Publications
Mutagenesisi414 – 4141R → C: Retains 50% of wild-type activity after modification of the thiol group by maleimide, which decreases the diameter of the access channel and impairs substrate access to the active site. Decreased catalytic activity towards fluorogenic substrate and insulin beta chain prior to any modification or oxidation, probably due to the decrease of the diameter of the substrate access channel. Further decreased catalytic activity towards these substrates after modification with fluorescein-5-maleimide or oxidation by oxidized glutathione; when associated with C-643. 2 Publications
Mutagenesisi643 – 6431A → C: Decreased catalytic activity towards fluorogenic substrate and insulin beta chain prior to any modification or oxidation. Further decreased catalytic activity towards these substrates after modification with fluorescein-5-maleimide or oxidation by oxidized glutathione; when associated with C-414. 1 Publication
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.4 Publications

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 propeller1 PublicationAdd
BLAST
Regioni131 – 1322Binds the substrate's C-terminus2 Publications
Regioni326 – 675350Seven-bladed beta propeller1 PublicationAdd
BLAST
Regioni679 – 74567C-1; helical bundle1 PublicationAdd
BLAST
Regioni761 – 85595PDZ-like1 PublicationAdd
BLAST
Regioni856 – 1061206C-2; alpha-beta sandwich1 PublicationAdd
BLAST
Regioni916 – 9183Substrate binding2 Publications
Regioni993 – 9953Substrate binding1 Publication

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.3 Publications

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSLMSFGSC QWIDQGRFSR SLYRNFKTFK LHEMHGLCMP NLLLNPDIHG
60 70 80 90 100
DRIIFVCCDD LWEHDLKSGS TRKIVSNLGV INNARFFPDG RKIAIRVMRG
110 120 130 140 150
SSLNTADLYF YNGENGEIKR ITYFSGKSTG RRMFTDVAGF DPDGNLIIST
160 170 180 190 200
DAMQPFSSMT CLYRVENDGI NFVPLNLGPA THILFADGRR VIGRNTFELP
210 220 230 240 250
HWKGYRGGTR GKIWIEVNSG AFKKIVDMST HVSSPVIVGH RIYFITDIDG
260 270 280 290 300
FGQIYSTDLD GKDLRKHTSF TDYYPRHLNT DGRRILFSKG GSIYIFNPDT
310 320 330 340 350
EKIEKIEIGD LESPEDRIIS IPSKFAEDFS PLDGDLIAFV SRGQAFIQDV
360 370 380 390 400
SGTYVLKVPE PLRIRYVRRG GDTKVAFIHG TREGDFLGIY DYRTGKAEKF
410 420 430 440 450
EENLGNVFAM GVDRNGKFAV VANDRFEIMT VDLETGKPTV IERSREAMIT
460 470 480 490 500
DFTISDNSRF IAYGFPLKHG ETDGYVMQAI HVYDMEGRKI FAATTENSHD
510 520 530 540 550
YAPAFDADSK NLYYLSYRSL DPSPDRVVLN FSFEVVSKPF VIPLIPGSPN
560 570 580 590 600
PTKLVPRSMT SEAGEYDLND MYKRSSPINV DPGDYRMIIP LESSILIYSV
610 620 630 640 650
PVHGEFAAYY QGAPEKGVLL KYDVKTRKVT EVKNNLTDLR LSADRKTVMV
660 670 680 690 700
RKDDGKIYTF PLEKPEDERT VETDKRPLVS SIHEEFLQMY DEAWKLARDN
710 720 730 740 750
YWNEAVAKEI SERIYEKYRN LVPLCKTRYD LSNVIVEMQG EYRTSHSYEM
760 770 780 790 800
GGTFTDKDPF RSGRIACDFK LDGDHYVVAK AYAGDYSNEG EKSPIFEYGI
810 820 830 840 850
DPTGYLIEDI DGETVGAGSN IYRVLSEKAG TSARIRLSGK GGDKRDLMID
860 870 880 890 900
ILDDDRFIRY RSWVEANRRY VHERSKGTIG YIHIPDMGMM GLNEFYRLFI
910 920 930 940 950
NESSYQGLIV DVRFNGGGFV SQLIIEKLMN KRIGYDNPRR GTLSPYPTNS
960 970 980 990 1000
VRGKIIAITN EYAGSDGDIF SFSFKKLGLG KLIGTRTWGG VVGITPKRRL
1010 1020 1030 1040 1050
IDGTVLTQPE FAFWFRDAGF GVENYGVDPD VEIEYAPHDY LSGKDPQIDY
1060 1070
AIDALIEELR NWNEELPQRP S
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

« Hide 'large scale' publications
  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) OF 27-1071, SUBUNIT, DOMAIN, REGIONS, ACTIVE SITES, SITES, MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414; 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 (2.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, REGIONS, ACTIVE SITES, SITES, MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414 AND ALA-643.

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 29, 2014
This is version 114 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