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Subtilisin-like serine protease (EC 3.4.21.62) (Tk-SP)

 TKSP_THEKO              Reviewed;         663 AA.
Q5JIZ5;
26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
22-NOV-2017, entry version 88.
RecName: Full=Subtilisin-like serine protease {ECO:0000303|PubMed:20100702, ECO:0000303|PubMed:20595040, ECO:0000312|EMBL:BAD85878.1};
EC=3.4.21.62 {ECO:0000269|PubMed:20100702};
AltName: Full=Tk-SP {ECO:0000303|PubMed:20100702, ECO:0000303|PubMed:20595040};
Flags: Precursor;
OrderedLocusNames=TK1689 {ECO:0000312|EMBL:BAD85878.1};
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
(Pyrococcus kodakaraensis (strain KOD1)).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=69014 {ECO:0000312|Proteomes:UP000000536};
[1] {ECO:0000312|EMBL:BAD85878.1, ECO:0000312|Proteomes:UP000000536}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
{ECO:0000312|Proteomes:UP000000536};
PubMed=15710748; DOI=10.1101/gr.3003105;
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
"Complete genome sequence of the hyperthermophilic archaeon
Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
genomes.";
Genome Res. 15:352-363(2005).
[2]
PROTEIN SEQUENCE OF 24-26 AND 137-140, FUNCTION, CATALYTIC ACTIVITY,
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS
SPECTROMETRY, BIOTECHNOLOGY, MUTAGENESIS OF SER-382, AND MAGNETIC
CIRCULAR DICHROISM.
PubMed=20100702; DOI=10.1093/protein/gzp092;
Foophow T., Tanaka S., Koga Y., Takano K., Kanaya S.;
"Subtilisin-like serine protease from hyperthermophilic archaeon
Thermococcus kodakaraensis with N- and C-terminal propeptides.";
Protein Eng. Des. Sel. 23:347-355(2010).
[3] {ECO:0000312|PDB:3AFG}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 24-562 OF MUTANT ALA-382 IN
COMPLEX WITH CALCIUM, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN,
PRO-PEPTIDES, ACTIVE SITE, MUTAGENESIS OF SER-382, AND CIRCULAR
DICHROISM.
PubMed=20595040; DOI=10.1016/j.jmb.2010.05.064;
Foophow T., Tanaka S., Angkawidjaja C., Koga Y., Takano K., Kanaya S.;
"Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus
kodakaraensis: requirement of a C-terminal beta-jelly roll domain for
hyperstability.";
J. Mol. Biol. 400:865-877(2010).
-!- FUNCTION: Serine protease with a broad substrate specificity.
{ECO:0000269|PubMed:20100702}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity
for peptide bonds, and a preference for a large uncharged residue
in P1. Hydrolyzes peptide amides. {ECO:0000269|PubMed:20100702}.
-!- ENZYME REGULATION: Resistant to treatment with 5% SDS, 8 M urea,
10% Triton X-100 or 10% Tween-20. Fully active although less
stable in the presence of 10 mM EDTA. Activity not affected by the
absence or presence of 10 mM CaCl(2). Unstable in the presence of
2 M or over GdnHCl and loses 35% and 99% of its activity upon
incubation with 2 and 4 M GdnHCl, respectively, for 1 hour at 55
degrees Celsius. Nearly fully loses activity upon incubation at pH
2.0. {ECO:0000269|PubMed:20100702}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.11 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20
degrees Celsius and pH 7.5 {ECO:0000269|PubMed:20100702};
KM=0.41 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80
degrees Celsius and pH 7.5 {ECO:0000269|PubMed:20100702};
Vmax=510 umol/min/mg enzyme {ECO:0000269|PubMed:20100702};
Note=Kcat is 1.6 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-
nitroanilide at 20 degrees Celsius and pH 7.5(PubMed:20100702).
Kcat is 25 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
at 80 degrees Celsius and pH 7.5(PubMed:20100702).
{ECO:0000269|PubMed:20100702};
pH dependence:
High activity at a wide pH range between 7.0-11.5 at 20 degrees
Celsius and pH 7.5. It is not fully stable at pH 6 or under and
at pH 12 or over. It loses over 85% of its activity at pH 3 or
under and at pH 13. {ECO:0000269|PubMed:20100702};
Temperature dependence:
Optimum temperature is about 100 degrees Celsius. Highly
thermostable. Stable at 80 degrees Celsius for at least 3 hours.
Half-life at 100 degrees Celsius is 100 minutes and at 90
degrees Celsius more than 3 hours.
{ECO:0000269|PubMed:20100702};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20100702,
ECO:0000269|PubMed:20595040}.
-!- DOMAIN: The C-terminal calcium-binding beta-jelly roll domain
(445-562) of the mature domain is not required for folding or
activity, but it is required for the hyperstabilization of the
protein and possibly for its adaptation to high-temperature
environment. {ECO:0000269|PubMed:20595040}.
-!- MASS SPECTROMETRY: Mass=68600; Method=MALDI; Range=24-663;
Evidence={ECO:0000269|PubMed:20100702};
-!- MASS SPECTROMETRY: Mass=44187; Mass_error=202; Method=MALDI;
Range=137-562; Evidence={ECO:0000269|PubMed:20100702};
-!- BIOTECHNOLOGY: Has potential for application in biotechnology
fields due to its high resistance to heat, denaturants, detergents
and chelating agents. {ECO:0000303|PubMed:20100702}.
-!- SIMILARITY: Belongs to the peptidase S8 family.
{ECO:0000255|RuleBase:RU003355}.
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EMBL; AP006878; BAD85878.1; -; Genomic_DNA.
RefSeq; WP_011250640.1; NC_006624.1.
PDB; 3AFG; X-ray; 2.00 A; A/B=24-562.
PDBsum; 3AFG; -.
ProteinModelPortal; Q5JIZ5; -.
SMR; Q5JIZ5; -.
STRING; 69014.TK1689; -.
EnsemblBacteria; BAD85878; BAD85878; TK1689.
GeneID; 3234995; -.
KEGG; tko:TK1689; -.
PATRIC; fig|69014.16.peg.1647; -.
eggNOG; arCOG00702; Archaea.
eggNOG; COG1404; LUCA.
HOGENOM; HOG000199176; -.
KO; K17734; -.
OMA; VTATLYW; -.
OrthoDB; POG093Z01QC; -.
BioCyc; TKOD69014:GH72-1724-MONOMER; -.
EvolutionaryTrace; Q5JIZ5; -.
Proteomes; UP000000536; Chromosome.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR007280; Peptidase_C_arc/bac.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
InterPro; IPR017319; Subtilisin_TK1689.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF04151; PPC; 2.
PIRSF; PIRSF037907; Subtilisin_rel_TK1689; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Hydrolase; Metal-binding; Protease; Reference proteome;
Serine protease; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:20595040}.
PROPEP 24 136 Removed in mature form.
{ECO:0000269|PubMed:20100702,
ECO:0000269|PubMed:20595040}.
/FTId=PRO_0000431236.
CHAIN 137 562 Subtilisin-like serine protease.
{ECO:0000269|PubMed:20100702,
ECO:0000269|PubMed:20595040}.
/FTId=PRO_0000431237.
PROPEP 563 663 Removed in mature form.
{ECO:0000269|PubMed:20100702,
ECO:0000269|PubMed:20595040}.
/FTId=PRO_0000431238.
DOMAIN 165 439 Peptidase S8. {ECO:0000255}.
ACT_SITE 170 170 Charge relay system.
{ECO:0000269|PubMed:20595040}.
ACT_SITE 203 203 Charge relay system.
{ECO:0000269|PubMed:20595040}.
ACT_SITE 382 382 Nucleophile.
{ECO:0000269|PubMed:20595040}.
METAL 420 420 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:20595040}.
METAL 423 423 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:20595040}.
METAL 483 483 Calcium 2. {ECO:0000269|PubMed:20595040}.
METAL 484 484 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:20595040}.
METAL 485 485 Calcium 2. {ECO:0000269|PubMed:20595040}.
METAL 497 497 Calcium 1. {ECO:0000269|PubMed:20595040}.
METAL 498 498 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:20595040}.
METAL 501 501 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:20595040}.
METAL 507 507 Calcium 2. {ECO:0000269|PubMed:20595040}.
SITE 303 303 Important for catalytic activity.
{ECO:0000303|PubMed:20100702}.
MUTAGEN 382 382 S->A: Loss of activity. Greatly
destabilized; when associated with the
deletion of the calcium-binding form of
the beta-jelly roll domain of the mature
domain. {ECO:0000269|PubMed:20595040}.
MUTAGEN 382 382 S->C: Greatly reduced enzymatic activity.
Greatly reduced enzymatic activity; when
associated with the deletion of the beta-
jelly roll domain of the mature domain.
{ECO:0000269|PubMed:20595040}.
HELIX 44 51 {ECO:0000244|PDB:3AFG}.
STRAND 58 67 {ECO:0000244|PDB:3AFG}.
HELIX 68 81 {ECO:0000244|PDB:3AFG}.
STRAND 84 88 {ECO:0000244|PDB:3AFG}.
STRAND 90 100 {ECO:0000244|PDB:3AFG}.
HELIX 101 107 {ECO:0000244|PDB:3AFG}.
STRAND 124 129 {ECO:0000244|PDB:3AFG}.
STRAND 132 134 {ECO:0000244|PDB:3AFG}.
STRAND 165 172 {ECO:0000244|PDB:3AFG}.
HELIX 178 180 {ECO:0000244|PDB:3AFG}.
TURN 181 183 {ECO:0000244|PDB:3AFG}.
STRAND 184 189 {ECO:0000244|PDB:3AFG}.
TURN 190 192 {ECO:0000244|PDB:3AFG}.
STRAND 199 202 {ECO:0000244|PDB:3AFG}.
HELIX 203 212 {ECO:0000244|PDB:3AFG}.
HELIX 216 218 {ECO:0000244|PDB:3AFG}.
TURN 219 222 {ECO:0000244|PDB:3AFG}.
STRAND 230 235 {ECO:0000244|PDB:3AFG}.
STRAND 241 244 {ECO:0000244|PDB:3AFG}.
HELIX 245 257 {ECO:0000244|PDB:3AFG}.
HELIX 259 262 {ECO:0000244|PDB:3AFG}.
STRAND 264 269 {ECO:0000244|PDB:3AFG}.
HELIX 282 292 {ECO:0000244|PDB:3AFG}.
STRAND 296 300 {ECO:0000244|PDB:3AFG}.
STRAND 306 309 {ECO:0000244|PDB:3AFG}.
TURN 313 316 {ECO:0000244|PDB:3AFG}.
STRAND 318 326 {ECO:0000244|PDB:3AFG}.
STRAND 334 336 {ECO:0000244|PDB:3AFG}.
STRAND 349 353 {ECO:0000244|PDB:3AFG}.
STRAND 355 360 {ECO:0000244|PDB:3AFG}.
STRAND 368 370 {ECO:0000244|PDB:3AFG}.
STRAND 372 378 {ECO:0000244|PDB:3AFG}.
HELIX 381 398 {ECO:0000244|PDB:3AFG}.
HELIX 404 414 {ECO:0000244|PDB:3AFG}.
HELIX 420 422 {ECO:0000244|PDB:3AFG}.
TURN 426 428 {ECO:0000244|PDB:3AFG}.
HELIX 435 439 {ECO:0000244|PDB:3AFG}.
HELIX 441 443 {ECO:0000244|PDB:3AFG}.
STRAND 444 453 {ECO:0000244|PDB:3AFG}.
STRAND 458 467 {ECO:0000244|PDB:3AFG}.
STRAND 469 478 {ECO:0000244|PDB:3AFG}.
STRAND 483 489 {ECO:0000244|PDB:3AFG}.
STRAND 495 499 {ECO:0000244|PDB:3AFG}.
STRAND 502 505 {ECO:0000244|PDB:3AFG}.
STRAND 507 513 {ECO:0000244|PDB:3AFG}.
STRAND 516 528 {ECO:0000244|PDB:3AFG}.
STRAND 530 543 {ECO:0000244|PDB:3AFG}.
SEQUENCE 663 AA; 70955 MW; 2CE68ACD3888E90E CRC64;
MKKFGAVVLA LFLVGLMAGS VLAAPQKPAV RNVSQQKNYG LLTPGLFKKV QRMSWDQEVS
TIIMFDNQAD KEKAVEILDF LGAKIKYNYH IIPALAVKIK VKDLLIIAGL MDTGYFGNAQ
LSGVQFIQED YVVKVAVETE GLDESAAQVM ATNMWNLGYD GSGITIGIID TGIDASHPDL
QGKVIGWVDF VNGKTTPYDD NGHGTHVASI AAGTGAASNG KYKGMAPGAK LVGIKVLNGQ
GSGSISDIIN GVDWAVQNKD KYGIKVINLS LGSSQSSDGT DSLSQAVNNA WDAGLVVVVA
AGNSGPNKYT VGSPAAASKV ITVGAVDKYD VITDFSSRGP TADNRLKPEV VAPGNWIIAA
RASGTSMGQP INDYYTAAPG TSMATPHVAG IAALLLQAHP SWTPDKVKTA LIETADIVKP
DEIADIAYGA GRVNAYKAAY YDNYAKLTFT GYVSNKGSQS HQFTISGAGF VTATLYWDNS
GSDLDLYLYD PNGNQVDYSY TAYYGFEKVG YYNPTAGTWT IKVVSYSGSA NYQVDVVSDG
SLGQPSGGGS EPSPSPSPEP TVDEKTFTGT VHDYYDKSDT FTMTVNSGAT KITGDLYFDT
SYHDLDLYLY DPNQNLVDRS ESSNSYEHVE YNNPAPGTWY FLVYAYDTYG YADYQLDAKV
YYG


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