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P96086 (TRI_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tricorn protease

EC=3.4.21.-
Gene names
Name:tri
Ordered Locus Names:Ta1490
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length1071 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasm.

Domain

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. Ref.6

Sequence similarities

Belongs to the peptidase S41B family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.5-8.8.

Temperature dependence:

Optimum temperature is 65 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Serine protease
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10711071Tricorn protease
PRO_0000207197

Regions

Region39 – 310272Six-bladed beta propeller
Region131 – 1322Binds the substrate's C-terminus
Region326 – 675350Seven-bladed beta propeller
Region681 – 75272C-1
Region761 – 85595PDZ-like
Region856 – 1061206C-2
Region916 – 9183Substrate binding

Sites

Active site7461Charge relay system
Active site9651Charge relay system
Active site9661Charge relay system Potential
Site9361Substrate specificity switch

Experimental info

Mutagenesis131 – 1322RR → EE: Retains 10% of wild-type activity.
Mutagenesis1841L → C: After modification of the thiol group by maleimide, retains less than 50% of wild-type activity. Blocks product exit from the catalytic chamber.
Mutagenesis4141R → C: After modification of thiol group by maleimide, retains 50% of wild-type activity. Blocks substrate access to active site.
Mutagenesis7461H → A: Loss of catalytic activity. Ref.8
Mutagenesis9651S → A: Loss of catalytic activity. Ref.8

Secondary structure

........................................................................................................................................................................................... 1071
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96086 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: D8C5579436870710

FASTA1,071121,623
        10         20         30         40         50         60 
MPSLMSFGSC QWIDQGRFSR SLYRNFKTFK LHEMHGLCMP NLLLNPDIHG DRIIFVCCDD 

        70         80         90        100        110        120 
LWEHDLKSGS TRKIVSNLGV INNARFFPDG RKIAIRVMRG SSLNTADLYF YNGENGEIKR 

       130        140        150        160        170        180 
ITYFSGKSTG RRMFTDVAGF DPDGNLIIST DAMQPFSSMT CLYRVENDGI NFVPLNLGPA 

       190        200        210        220        230        240 
THILFADGRR VIGRNTFELP HWKGYRGGTR GKIWIEVNSG AFKKIVDMST HVSSPVIVGH 

       250        260        270        280        290        300 
RIYFITDIDG FGQIYSTDLD GKDLRKHTSF TDYYPRHLNT DGRRILFSKG GSIYIFNPDT 

       310        320        330        340        350        360 
EKIEKIEIGD LESPEDRIIS IPSKFAEDFS PLDGDLIAFV SRGQAFIQDV SGTYVLKVPE 

       370        380        390        400        410        420 
PLRIRYVRRG GDTKVAFIHG TREGDFLGIY DYRTGKAEKF EENLGNVFAM GVDRNGKFAV 

       430        440        450        460        470        480 
VANDRFEIMT VDLETGKPTV IERSREAMIT DFTISDNSRF IAYGFPLKHG ETDGYVMQAI 

       490        500        510        520        530        540 
HVYDMEGRKI FAATTENSHD YAPAFDADSK NLYYLSYRSL DPSPDRVVLN FSFEVVSKPF 

       550        560        570        580        590        600 
VIPLIPGSPN PTKLVPRSMT SEAGEYDLND MYKRSSPINV DPGDYRMIIP LESSILIYSV 

       610        620        630        640        650        660 
PVHGEFAAYY QGAPEKGVLL KYDVKTRKVT EVKNNLTDLR LSADRKTVMV RKDDGKIYTF 

       670        680        690        700        710        720 
PLEKPEDERT VETDKRPLVS SIHEEFLQMY DEAWKLARDN YWNEAVAKEI SERIYEKYRN 

       730        740        750        760        770        780 
LVPLCKTRYD LSNVIVEMQG EYRTSHSYEM GGTFTDKDPF RSGRIACDFK LDGDHYVVAK 

       790        800        810        820        830        840 
AYAGDYSNEG EKSPIFEYGI DPTGYLIEDI DGETVGAGSN IYRVLSEKAG TSARIRLSGK 

       850        860        870        880        890        900 
GGDKRDLMID ILDDDRFIRY RSWVEANRRY VHERSKGTIG YIHIPDMGMM GLNEFYRLFI 

       910        920        930        940        950        960 
NESSYQGLIV DVRFNGGGFV SQLIIEKLMN KRIGYDNPRR GTLSPYPTNS VRGKIIAITN 

       970        980        990       1000       1010       1020 
EYAGSDGDIF SFSFKKLGLG KLIGTRTWGG VVGITPKRRL IDGTVLTQPE FAFWFRDAGF 

      1030       1040       1050       1060       1070 
GVENYGVDPD VEIEYAPHDY LSGKDPQIDY AIDALIEELR NWNEELPQRP S 

« Hide

References

« Hide 'large scale' references
[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72850 Genomic DNA. Translation: AAC44621.1.
AL445067 Genomic DNA. Translation: CAC12608.1.
PIRT43255.
RefSeqNP_394941.1. NC_002578.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00484.
ProteinModelPortalP96086.
SMRP96086. Positions 39-1061.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta1490.

Protein family/group databases

MEROPSS41.005.

Proteomic databases

PRIDEP96086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12608; CAC12608; CAC12608.
GeneID1456939.
KEGGtac:Ta1490.

Phylogenomic databases

eggNOGCOG0793.
HOGENOMHOG000243096.
KOK08676.
OMAKSVYAIS.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.30.42.10. 1 hit.
3.90.226.10. 1 hit.
InterProIPR029045. 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]
PfamPF07676. PD40. 1 hit.
PF03572. Peptidase_S41. 1 hit.
PF14684. Tricorn_C1. 1 hit.
PF14685. Tricorn_PDZ. 1 hit.
[Graphical view]
PIRSFPIRSF036421. Tricorn_protease. 1 hit.
SMARTSM00245. TSPc. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF52096. SSF52096. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP96086.

Entry information

Entry nameTRI_THEAC
AccessionPrimary (citable) accession number: P96086
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references