TKSU_THEKO
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 03-AUG-2022, entry version 133.
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}.
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; 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; 3234572; -.
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 OMA; FSTRRWY; -.
DR OrthoDB; 53822at2157; -.
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; -; 1.
DR Gene3D; 3.40.50.200; -; 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 Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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
