ID   TRI_THEVO               Reviewed;        1030 AA.
AC   Q97A95;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Tricorn protease;
DE            EC=3.4.21.-;
GN   Name=tri; OrderedLocusNames=TV0915; ORFNames=TVG0940548;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Tricorn degrades oligopeptides in a sequential manner.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the tricorn proteolytic complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S41B family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000011; BAB60057.1; -; Genomic_DNA.
DR   RefSeq; WP_010917153.1; NC_002689.2.
DR   AlphaFoldDB; Q97A95; -.
DR   SMR; Q97A95; -.
DR   STRING; 273116.14325132; -.
DR   MEROPS; S41.005; -.
DR   PRIDE; Q97A95; -.
DR   EnsemblBacteria; BAB60057; BAB60057; BAB60057.
DR   GeneID; 1442001; -.
DR   KEGG; tvo:TVG0940548; -.
DR   eggNOG; arCOG03384; Archaea.
DR   HOGENOM; CLU_005503_1_0_2; -.
DR   OMA; YLHVPDM; -.
DR   OrthoDB; 456at2157; -.
DR   PhylomeDB; Q97A95; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   InterPro; IPR028204; Tricorn_C1.
DR   InterPro; IPR029414; Tricorn_PDZ.
DR   InterPro; IPR012393; Tricorn_protease.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43253; PTHR43253; 1.
DR   Pfam; PF07676; PD40; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   Pfam; PF14684; Tricorn_C1; 1.
DR   Pfam; PF14685; Tricorn_PDZ; 1.
DR   PIRSF; PIRSF036421; Tricorn_protease; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..1030
FT                   /note="Tricorn protease"
FT                   /id="PRO_0000207198"
FT   REGION          1..270
FT                   /note="Six-bladed beta propeller"
FT                   /evidence="ECO:0000250"
FT   REGION          93..94
FT                   /note="Binds the substrate's C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          286..635
FT                   /note="Seven-bladed beta propeller"
FT                   /evidence="ECO:0000250"
FT   REGION          641..712
FT                   /note="C-1"
FT                   /evidence="ECO:0000250"
FT   REGION          721..816
FT                   /note="PDZ-like"
FT   REGION          817..1022
FT                   /note="C-2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        706
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        926
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   ACT_SITE        984
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   BINDING         877..879
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         954..956
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   SITE            927
FT                   /note="Transition state stabilizer; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
SQ   SEQUENCE   1030 AA;  116998 MW;  410BE79E1117DB9D CRC64;
     MANLLQNPDI YGDRILFTCC DELWEYSLST GEKKRLTSHL GVVNNARYYD NGTKVVFRVM
     FGQSLDAADL FSIDLKSGEL KRLTFITGKS VGRRKFTDVA GFSKDGSIIV STDAFQPFSV
     PMLYKLGDDG SLDPLNLGPA VHYIEKNGRI YIGRDTYDLP HWKEYKGGTR GKIWSGTIEK
     GFKKIIDLEN HISCPVIVKD RIYFITDIDG AGNIYSTNLD GNDLKKHTDF HEYYPRHLNT
     DGKTIVFSMG GDIYTFDPTN DNVKSLDIGP VFDTDLNQSY APSKFLEDFS MSPGDMYSTV
     SRGKAFIFNE NVNYSIPVKS DGRVRYSRFL SKNEISLVIG DKDGDSIGVF DAGTGEMKRK
     IGPLGNIFSV KSSADGKYLV VGNDNFQILL IDVSNGTVKE IDQSREGLIV DFAISKDSRF
     IAYSFPVKSS DLASYVQRHI KLFDMLNDKH YDVTTETAND FAPAFDADTN YLYYLSNRSL
     DPSTDRFTFN FGYLNITRPF VVPLKKGYVS PARNMPQDIE PEKGEYDLER LKYISEPLPV
     DQADYRSITP LKDGVLLFSV PIHGEFSSYY SGQPEKGIIV KFEFKDKKVK EIKKEVVDFK
     ISTDGSKIMF SKQDGKLYTF RMEKPEEEKS LNIDAITIVS NVKEDFAEMY DEAWKLARDN
     YWDKEHALTI SEKIYERYRK LVERCVTRWD LSYLITEIQG EYRTSHSYEM GGYFTDIDMP
     RAGRIACDFK YSNGEYVISD ILYGDPSNEN EKSPFLLSTL DADIGDAVIE IDGIPIGKGK
     SIYEALVGKG NRSVLVKIRK KDNSVRSGFV DVLQDDRYIR YRAWVEKNKK FVHERTNGRI
     GYIHIPDMGI MGLNEFYRQY VTEASRNGLI VDVRFNGGGF VSQLILEKLY MKRLGYDNPR
     RGTLEPYPMN SIEGPMIAIT NEYAGSDGDI FSYSFKALHL GTLIGTRTWG GVVGISPRRK
     LIDGTVLSQP EYAFWFKGSG FSVENYGVDP DVVIEYPPEM YNVNVDPQLE RAIEMVLADL
     EKYKIELPKK