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Protein

Subtilisin-like serine protease

Gene

TK1689

Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease with a broad substrate specificity.1 Publication

Catalytic activityi

Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.1 Publication

Enzyme regulationi

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 CaCl2. 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 2.0.1 Publication

Kineticsi

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).1 Publication

Manual assertion based on experiment ini

  1. KM=0.11 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.51 Publication
  2. KM=0.41 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.51 Publication
  1. Vmax=510 µmol/min/mg enzyme1 Publication

pH dependencei

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 13.1 Publication

Temperature dependencei

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei170Charge relay system1 Publication1
Active sitei203Charge relay system1 Publication1
Sitei303Important for catalytic activity1 Publication1
Active sitei382Nucleophile1 Publication1
Metal bindingi420Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi423Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi483Calcium 21 Publication1
Metal bindingi484Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi485Calcium 21 Publication1
Metal bindingi497Calcium 11 Publication1
Metal bindingi498Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi501Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi507Calcium 21 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1724-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin-like serine protease2 PublicationsImported (EC:3.4.21.621 Publication)
Alternative name(s):
Tk-SP2 Publications
Gene namesi
Ordered Locus Names:TK1689Imported
OrganismiThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))Imported
Taxonomic identifieri69014 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000000536 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

Has potential for application in biotechnology fields due to its high resistance to heat, denaturants, detergents and chelating agents.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi382S → 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. 1 Publication1
Mutagenesisi382S → C: Greatly reduced enzymatic activity. Greatly reduced enzymatic activity; when associated with the deletion of the beta-jelly roll domain of the mature domain. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
PropeptideiPRO_000043123624 – 136Removed in mature form2 PublicationsAdd BLAST113
ChainiPRO_0000431237137 – 562Subtilisin-like serine protease2 PublicationsAdd BLAST426
PropeptideiPRO_0000431238563 – 663Removed in mature form2 PublicationsAdd BLAST101

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi69014.TK1689.

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 51Combined sources8
Beta strandi58 – 67Combined sources10
Helixi68 – 81Combined sources14
Beta strandi84 – 88Combined sources5
Beta strandi90 – 100Combined sources11
Helixi101 – 107Combined sources7
Beta strandi124 – 129Combined sources6
Beta strandi132 – 134Combined sources3
Beta strandi165 – 172Combined sources8
Helixi178 – 180Combined sources3
Turni181 – 183Combined sources3
Beta strandi184 – 189Combined sources6
Turni190 – 192Combined sources3
Beta strandi199 – 202Combined sources4
Helixi203 – 212Combined sources10
Helixi216 – 218Combined sources3
Turni219 – 222Combined sources4
Beta strandi230 – 235Combined sources6
Beta strandi241 – 244Combined sources4
Helixi245 – 257Combined sources13
Helixi259 – 262Combined sources4
Beta strandi264 – 269Combined sources6
Helixi282 – 292Combined sources11
Beta strandi296 – 300Combined sources5
Beta strandi306 – 309Combined sources4
Turni313 – 316Combined sources4
Beta strandi318 – 326Combined sources9
Beta strandi334 – 336Combined sources3
Beta strandi349 – 353Combined sources5
Beta strandi355 – 360Combined sources6
Beta strandi368 – 370Combined sources3
Beta strandi372 – 378Combined sources7
Helixi381 – 398Combined sources18
Helixi404 – 414Combined sources11
Helixi420 – 422Combined sources3
Turni426 – 428Combined sources3
Helixi435 – 439Combined sources5
Helixi441 – 443Combined sources3
Beta strandi444 – 453Combined sources10
Beta strandi458 – 467Combined sources10
Beta strandi469 – 478Combined sources10
Beta strandi483 – 489Combined sources7
Beta strandi495 – 499Combined sources5
Beta strandi502 – 505Combined sources4
Beta strandi507 – 513Combined sources7
Beta strandi516 – 528Combined sources13
Beta strandi530 – 543Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AFGX-ray2.00A/B24-562[»]
ProteinModelPortaliQ5JIZ5.
SMRiQ5JIZ5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5JIZ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini165 – 439Peptidase S8Sequence analysisAdd BLAST275

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the peptidase S8 family.UniRule annotation
Contains 1 peptidase S8 domain.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiarCOG00702. Archaea.
COG1404. LUCA.
HOGENOMiHOG000199176.
KOiK17734.
OMAiVTATLYW.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR007280. Peptidase_C_arc/bac.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR017319. Subtilisin_TK1689.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 4 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
PF04151. PPC. 2 hits.
[Graphical view]
PIRSFiPIRSF037907. Subtilisin_rel_TK1689. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5JIZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFGAVVLA LFLVGLMAGS VLAAPQKPAV RNVSQQKNYG LLTPGLFKKV
60 70 80 90 100
QRMSWDQEVS TIIMFDNQAD KEKAVEILDF LGAKIKYNYH IIPALAVKIK
110 120 130 140 150
VKDLLIIAGL MDTGYFGNAQ LSGVQFIQED YVVKVAVETE GLDESAAQVM
160 170 180 190 200
ATNMWNLGYD GSGITIGIID TGIDASHPDL QGKVIGWVDF VNGKTTPYDD
210 220 230 240 250
NGHGTHVASI AAGTGAASNG KYKGMAPGAK LVGIKVLNGQ GSGSISDIIN
260 270 280 290 300
GVDWAVQNKD KYGIKVINLS LGSSQSSDGT DSLSQAVNNA WDAGLVVVVA
310 320 330 340 350
AGNSGPNKYT VGSPAAASKV ITVGAVDKYD VITDFSSRGP TADNRLKPEV
360 370 380 390 400
VAPGNWIIAA RASGTSMGQP INDYYTAAPG TSMATPHVAG IAALLLQAHP
410 420 430 440 450
SWTPDKVKTA LIETADIVKP DEIADIAYGA GRVNAYKAAY YDNYAKLTFT
460 470 480 490 500
GYVSNKGSQS HQFTISGAGF VTATLYWDNS GSDLDLYLYD PNGNQVDYSY
510 520 530 540 550
TAYYGFEKVG YYNPTAGTWT IKVVSYSGSA NYQVDVVSDG SLGQPSGGGS
560 570 580 590 600
EPSPSPSPEP TVDEKTFTGT VHDYYDKSDT FTMTVNSGAT KITGDLYFDT
610 620 630 640 650
SYHDLDLYLY DPNQNLVDRS ESSNSYEHVE YNNPAPGTWY FLVYAYDTYG
660
YADYQLDAKV YYG
Length:663
Mass (Da):70,955
Last modified:February 15, 2005 - v1
Checksum:i2CE68ACD3888E90E
GO

Mass spectrometryi

Molecular mass is 68600 Da from positions 24 - 663. Determined by MALDI. 1 Publication
Molecular mass is 44187±202 Da from positions 137 - 562. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85878.1.
RefSeqiWP_011250640.1. NC_006624.1.

Genome annotation databases

EnsemblBacteriaiBAD85878; BAD85878; TK1689.
GeneIDi3234995.
KEGGitko:TK1689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85878.1.
RefSeqiWP_011250640.1. NC_006624.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AFGX-ray2.00A/B24-562[»]
ProteinModelPortaliQ5JIZ5.
SMRiQ5JIZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi69014.TK1689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD85878; BAD85878; TK1689.
GeneIDi3234995.
KEGGitko:TK1689.

Phylogenomic databases

eggNOGiarCOG00702. Archaea.
COG1404. LUCA.
HOGENOMiHOG000199176.
KOiK17734.
OMAiVTATLYW.

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1724-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5JIZ5.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR007280. Peptidase_C_arc/bac.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR017319. Subtilisin_TK1689.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 4 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
PF04151. PPC. 2 hits.
[Graphical view]
PIRSFiPIRSF037907. Subtilisin_rel_TK1689. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTKSP_THEKO
AccessioniPrimary (citable) accession number: Q5JIZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.