ID   TKSU_THEKO              Reviewed;         422 AA.
AC   P58502; Q977F5;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Tk-subtilisin;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=TK1675;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=11375149; DOI=10.1128/aem.67.6.2445-2452.2001;
RA   Kannan Y., Koga Y., Inoue Y., Haruki M., Takagi M., Imanaka T.,
RA   Morikawa M., Kanaya S.;
RT   "Active subtilisin-like protease from a hyperthermophilic archaeon in a
RT   form with a putative prosequence.";
RL   Appl. Environ. Microbiol. 67:2445-2452(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Has a broad substrate specificity with a slight preference to
CC       large hydrophobic amino acid residues at the P1 position.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5.;
CC       Temperature dependence:
CC         Thermostable. Highly active at 80 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P58502; P58502: TK1675; NbExp=2; IntAct=EBI-7810114, EBI-7810114;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AB056701; BAB60701.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85864.1; -; Genomic_DNA.
DR   RefSeq; WP_011250626.1; NC_006624.1.
DR   PDB; 2E1P; X-ray; 2.30 A; A=25-422.
DR   PDB; 2Z2X; X-ray; 1.70 A; A=105-422.
DR   PDB; 2Z2Y; X-ray; 1.89 A; A/C=105-422, B/D=29-93.
DR   PDB; 2Z2Z; X-ray; 1.87 A; A=28-422.
DR   PDB; 2Z30; X-ray; 1.65 A; A=103-422, B=29-93.
DR   PDB; 2Z56; X-ray; 1.90 A; A=105-422, B=29-93.
DR   PDB; 2Z57; X-ray; 1.80 A; A=105-422, B=29-93.
DR   PDB; 2Z58; X-ray; 1.88 A; A=105-422, B=28-93.
DR   PDB; 2ZRQ; X-ray; 2.16 A; A=94-422.
DR   PDB; 2ZWO; X-ray; 2.07 A; A/B/C=25-422.
DR   PDB; 2ZWP; X-ray; 2.40 A; A/B=25-422.
DR   PDB; 3A3N; X-ray; 2.20 A; A=94-422, B=25-91.
DR   PDB; 3A3O; X-ray; 1.90 A; A=94-422, B=25-88.
DR   PDB; 3A3P; X-ray; 1.90 A; A=94-422, B=25-93.
DR   PDB; 3VHQ; X-ray; 2.15 A; A=25-422.
DR   PDB; 3VV2; X-ray; 1.83 A; A=94-422, B=25-93.
DR   PDB; 3WIU; X-ray; 1.80 A; A/B/C=25-422.
DR   PDB; 3WIV; X-ray; 1.90 A; A/B/C=25-422.
DR   PDB; 4JP8; X-ray; 2.21 A; A=25-422.
DR   PDBsum; 2E1P; -.
DR   PDBsum; 2Z2X; -.
DR   PDBsum; 2Z2Y; -.
DR   PDBsum; 2Z2Z; -.
DR   PDBsum; 2Z30; -.
DR   PDBsum; 2Z56; -.
DR   PDBsum; 2Z57; -.
DR   PDBsum; 2Z58; -.
DR   PDBsum; 2ZRQ; -.
DR   PDBsum; 2ZWO; -.
DR   PDBsum; 2ZWP; -.
DR   PDBsum; 3A3N; -.
DR   PDBsum; 3A3O; -.
DR   PDBsum; 3A3P; -.
DR   PDBsum; 3VHQ; -.
DR   PDBsum; 3VV2; -.
DR   PDBsum; 3WIU; -.
DR   PDBsum; 3WIV; -.
DR   PDBsum; 4JP8; -.
DR   AlphaFoldDB; P58502; -.
DR   SMR; P58502; -.
DR   MINT; P58502; -.
DR   STRING; 69014.TK1675; -.
DR   MEROPS; S08.129; -.
DR   EnsemblBacteria; BAD85864; BAD85864; TK1675.
DR   GeneID; 78448202; -.
DR   KEGG; tko:TK1675; -.
DR   PATRIC; fig|69014.16.peg.1633; -.
DR   eggNOG; arCOG00702; Archaea.
DR   HOGENOM; CLU_011263_15_0_2; -.
DR   InParanoid; P58502; -.
DR   OrthoDB; 341609at2157; -.
DR   PhylomeDB; P58502; -.
DR   BRENDA; 3.4.21.B57; 5246.
DR   EvolutionaryTrace; P58502; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..106
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027195"
FT   CHAIN           107..422
FT                   /note="Tk-subtilisin"
FT                   /id="PRO_0000027196"
FT   DOMAIN          111..417
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        139
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           43..49
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          58..67
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          95..98
FT                   /evidence="ECO:0007829|PDB:4JP8"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:3WIU"
FT   HELIX           112..116
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          213..216
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           217..229
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            230..233
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          253..257
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           266..277
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          303..309
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          330..336
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          340..344
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           347..369
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:2Z2X"
FT   HELIX           386..393
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   STRAND          398..403
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   TURN            404..406
FT                   /evidence="ECO:0007829|PDB:2Z30"
FT   HELIX           413..421
FT                   /evidence="ECO:0007829|PDB:2Z30"
SQ   SEQUENCE   422 AA;  43786 MW;  843255BCD806DB71 CRC64;
     MKKSIALVLS IVLLAALFAV PASAGEQNTI RVIVSVDKAK FNPHEVLGIG GHIVYQFKLI
     PAVVVDVPAN AVGKLKKMPG VEKVEFDHQA VLLGKPSWLG GGSTQPAQTI PWGIERVKAP
     SVWSITDGSV SVIQVAVLDT GVDYDHPDLA ANIAWCVSTL RGKVSTKLRD CADQNGHGTH
     VIGTIAALNN DIGVVGVAPG VQIYSVRVLD ARGSGSYSDI AIGIEQAILG PDGVADKDGD
     GIIAGDPDDD AAEVISMSLG GPADDSYLYD MIIQAYNAGI VIVAASGNEG APSPSYPAAY
     PEVIAVGAID SNDNIASFSN RQPEVSAPGV DILSTYPDDS YETLMGTSMA TPHVSGVVAL
     IQAAYYQKYG KILPVGTFDD ISKNTVRGIL HITADDLGPT GWDADYGYGV VRAALAVQAA
     LG
//