ID   TRIC_SULTO              Reviewed;         854 AA.
AC   Q972G5;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative Tricorn-like protease C-terminal subunit;
DE            EC=3.4.21.-;
GN   Name=triC; OrderedLocusNames=STK_11680;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Degrades oligopeptides in a sequential manner. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S41B family. {ECO:0000305}.
CC   -!- CAUTION: Tricorn seems to be split into two ORFs in S.tokodaii, encoded
CC       on opposite strands and separated by approximately 279 kb.
CC       {ECO:0000305}.
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DR   EMBL; BA000023; BAB66203.1; -; Genomic_DNA.
DR   RefSeq; WP_010979182.1; NC_003106.2.
DR   AlphaFoldDB; Q972G5; -.
DR   SMR; Q972G5; -.
DR   STRING; 273063.STK_11680; -.
DR   EnsemblBacteria; BAB66203; BAB66203; STK_11680.
DR   GeneID; 1459157; -.
DR   KEGG; sto:STK_11680; -.
DR   PATRIC; fig|273063.9.peg.1319; -.
DR   eggNOG; arCOG03384; Archaea.
DR   OMA; YLHVPDM; -.
DR   OrthoDB; 456at2157; -.
DR   Proteomes; UP000001015; 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   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..854
FT                   /note="Putative Tricorn-like protease C-terminal subunit"
FT                   /id="PRO_0000207196"
FT   REGION          554..646
FT                   /note="PDZ-like"
FT   ACT_SITE        539
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        756
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   ACT_SITE        814
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   BINDING         709
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
FT   SITE            757
FT                   /note="Transition state stabilizer; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P96086"
SQ   SEQUENCE   854 AA;  98910 MW;  9D86E77DA84A84D4 CRC64;
     MFYNFLLYLV IHVNYALDAL TFNKFLSLDG IVSWPMIIKD RVYFLSDHEG ISNLYSVNLE
     GKDLTKHTNF TEYYCRNASS DGRRIVFQNS GDIYLYDPEK QELKLLDIDL PTDRKKKQGK
     FVEVLDYTTE AIANDKYLSL ISRGKVFLMR HWDGPAVQLG EKQGVRYKQI QLLPNGDTVV
     LDTNDDKLTF LSKDGSIKKL NVDLGRIERI KVSPDGKKIL ISNNRLELWL YEVDTTNLRL
     IDKSEYDVIS QMDWHPDNEW FAYTFPESYS TQSIKLAHIS GKVIRITSPY GYDFSPSFDP
     DGRYLYFLSA RHLDPTNDKV IFNMSFQRVI KPYLVVLSNT YSPFNQSLEE TTSDKKVEIE
     GIEDRVIPFP VDEDYYIRIE GAKNNKVFLF SLPIKGYRYP GETLGKLEVF DLDSKTKELY
     ADNVKSFSLT IDKGKILILF KDSIRLFDVN TKPDLNATGK KGGIVDLSRI KVYVDPEREW
     KQMFREAWKL MQQNYWKPDG LKDWESVLLK YEKLIDRIST RYELSDLIQE MQGETKTSHS
     YEMPYDYDTA EPLPIGGLGA DYEYDKENKC YKIARIYVGD PTNENERSPL RDPGVQLNIG
     DCIKAVDGEE VKYNILSYLV NKDQVVLDVI TKGKTKRVTV KLLKDEKFLI YRYWVEKNRQ
     YVHEKSKGKL GYVHIPDMMY QGFAEFYRLF LSEFHREGLI VDVRFNRGGF ISGLILEKLL
     LKRMGYVVRR NGKELPHPFF SSPGVIVAIT NQYAGSDGDI FSYLFKKYKL GILIGRRTWG
     GVIGINVRDR LADNSAVSQP EFAVHFHDIG LKIENYGVDP DIEVDIKPED YANGRDPQLD
     TAIELALKQL EEKS