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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: 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)DescriptionActionsGraphical viewLength
Active sitei746Charge relay system2 Publications1
Sitei936Substrate specificity switch1 Publication1
Active sitei965Nucleophile2 Publications1
Sitei966Transition state stabilizer; via amide nitrogen2 Publications1
Active sitei1023Charge relay system1 Publication1

GO - Molecular functioni

  • serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.B34. 6324.

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
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi131 – 132RR → 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 Publications2
Mutagenesisi184L → 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 Publications1
Mutagenesisi414R → 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 Publications1
Mutagenesisi643A → 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 Publication1
Mutagenesisi746H → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi965S → A: Loss of catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002071971 – 1071Tricorn proteaseAdd BLAST1071

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

11071
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 49Combined sources6
Beta strandi52 – 57Combined sources6
Beta strandi60 – 65Combined sources6
Turni66 – 68Combined sources3
Beta strandi71 – 75Combined sources5
Beta strandi77 – 86Combined sources10
Beta strandi90 – 100Combined sources11
Beta strandi105 – 112Combined sources8
Turni113 – 116Combined sources4
Beta strandi117 – 120Combined sources4
Beta strandi126 – 129Combined sources4
Beta strandi135 – 140Combined sources6
Beta strandi146 – 150Combined sources5
Beta strandi154 – 156Combined sources3
Beta strandi161 – 166Combined sources6
Turni167 – 170Combined sources4
Beta strandi171 – 174Combined sources4
Beta strandi181 – 186Combined sources6
Beta strandi189 – 195Combined sources7
Beta strandi212 – 218Combined sources7
Beta strandi221 – 226Combined sources6
Beta strandi233 – 238Combined sources6
Beta strandi241 – 246Combined sources6
Beta strandi253 – 258Combined sources6
Beta strandi275 – 283Combined sources9
Beta strandi285 – 289Combined sources5
Beta strandi292 – 296Combined sources5
Turni298 – 300Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi316 – 320Combined sources5
Helixi322 – 325Combined sources4
Beta strandi326 – 331Combined sources6
Helixi333 – 335Combined sources3
Beta strandi337 – 341Combined sources5
Beta strandi344 – 348Combined sources5
Beta strandi352 – 357Combined sources6
Beta strandi364 – 369Combined sources6
Beta strandi371 – 381Combined sources11
Beta strandi384 – 391Combined sources8
Turni392 – 394Combined sources3
Beta strandi397 – 399Combined sources3
Beta strandi406 – 412Combined sources7
Beta strandi416 – 423Combined sources8
Beta strandi426 – 432Combined sources7
Turni433 – 435Combined sources3
Beta strandi438 – 443Combined sources6
Beta strandi445 – 447Combined sources3
Beta strandi452 – 454Combined sources3
Beta strandi460 – 467Combined sources8
Beta strandi477 – 484Combined sources8
Turni485 – 488Combined sources4
Beta strandi489 – 492Combined sources4
Beta strandi496 – 505Combined sources10
Beta strandi511 – 517Combined sources7
Beta strandi526 – 529Combined sources4
Beta strandi537 – 545Combined sources9
Helixi551 – 553Combined sources3
Helixi557 – 559Combined sources3
Helixi571 – 574Combined sources4
Beta strandi585 – 590Combined sources6
Beta strandi592 – 599Combined sources8
Helixi606 – 611Combined sources6
Beta strandi617 – 623Combined sources7
Turni624 – 626Combined sources3
Beta strandi629 – 641Combined sources13
Beta strandi643 – 645Combined sources3
Beta strandi647 – 652Combined sources6
Beta strandi657 – 663Combined sources7
Beta strandi678 – 681Combined sources4
Helixi682 – 700Combined sources19
Helixi704 – 719Combined sources16
Helixi720 – 724Combined sources5
Helixi728 – 740Combined sources13
Beta strandi766 – 772Combined sources7
Beta strandi775 – 781Combined sources7
Beta strandi788 – 790Combined sources3
Helixi794 – 798Combined sources5
Beta strandi806 – 810Combined sources5
Beta strandi816 – 819Combined sources4
Helixi821 – 826Combined sources6
Turni827 – 830Combined sources4
Beta strandi831 – 838Combined sources8
Beta strandi840 – 842Combined sources3
Beta strandi844 – 850Combined sources7
Helixi856 – 874Combined sources19
Turni875 – 877Combined sources3
Beta strandi878 – 883Combined sources6
Helixi889 – 902Combined sources14
Beta strandi905 – 911Combined sources7
Helixi921 – 928Combined sources8
Beta strandi934 – 941Combined sources8
Beta strandi944 – 947Combined sources4
Beta strandi953 – 959Combined sources7
Helixi966 – 976Combined sources11
Beta strandi979 – 985Combined sources7
Beta strandi992 – 994Combined sources3
Beta strandi1011 – 1015Combined sources5
Turni1016 – 1018Combined sources3
Turni1020 – 1025Combined sources6
Beta strandi1030 – 1032Combined sources3
Helixi1037 – 1041Combined sources5
Helixi1046 – 1058Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96086.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 310Six-bladed beta propeller1 PublicationAdd BLAST272
Regioni131 – 132Binds the substrate's C-terminus2 Publications2
Regioni326 – 675Seven-bladed beta propeller1 PublicationAdd BLAST350
Regioni679 – 745C-1; helical bundle1 PublicationAdd BLAST67
Regioni761 – 855PDZ-like1 PublicationAdd BLAST95
Regioni856 – 1061C-2; alpha-beta sandwich1 PublicationAdd BLAST206
Regioni916 – 918Substrate binding2 Publications3
Regioni993 – 995Substrate binding1 Publication3

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

eggNOGiarCOG03384. Archaea.
ENOG4102TDY. Archaea.
COG0793. LUCA.
COG4946. LUCA.
HOGENOMiHOG000243096.
KOiK08676.
OMAiGNLYSVD.

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

        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:
EMBLi
GenBanki
DDBJi
Links Updated
U72850 Genomic DNA. Translation: AAC44621.1.
AL445067 Genomic DNA. Translation: CAC12608.1.
PIRiT43255.
RefSeqiWP_010901890.1. NC_002578.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72850 Genomic DNA. Translation: AAC44621.1.
AL445067 Genomic DNA. Translation: CAC12608.1.
PIRiT43255.
RefSeqiWP_010901890.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta1490.

Protein family/group databases

MEROPSiS41.005.

Proteomic databases

PRIDEiP96086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG03384. Archaea.
ENOG4102TDY. Archaea.
COG0793. LUCA.
COG4946. LUCA.
HOGENOMiHOG000243096.
KOiK08676.
OMAiGNLYSVD.

Enzyme and pathway databases

BRENDAi3.4.21.B34. 6324.

Miscellaneous databases

EvolutionaryTraceiP96086.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.