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Protein

Tk-subtilisin

Gene

TK1675

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position.

Cofactori

pH dependencei

Optimum pH is 9.5.

Temperature dependencei

Thermostable. Highly active at 80 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Charge relay systemBy similarity
Active sitei177 – 1771Charge relay systemBy similarity
Active sitei348 – 3481Charge relay systemBy similarity

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1707-MONOMER.

Protein family/group databases

MEROPSiS08.129.

Names & Taxonomyi

Protein namesi
Recommended name:
Tk-subtilisin (EC:3.4.21.-)
Gene namesi
Ordered Locus Names:TK1675
OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Taxonomic identifieri69014 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000000536: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 10682Sequence AnalysisPRO_0000027195Add
BLAST
Chaini107 – 422316Tk-subtilisinPRO_0000027196Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7810114,EBI-7810114

Protein-protein interaction databases

MINTiMINT-8404006.
STRINGi69014.TK1675.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 367Combined sources
Helixi38 – 403Combined sources
Helixi43 – 497Combined sources
Beta strandi52 – 565Combined sources
Beta strandi58 – 6710Combined sources
Helixi69 – 713Combined sources
Helixi72 – 765Combined sources
Beta strandi81 – 866Combined sources
Beta strandi89 – 924Combined sources
Beta strandi95 – 984Combined sources
Beta strandi105 – 1073Combined sources
Helixi112 – 1165Combined sources
Helixi120 – 1223Combined sources
Turni123 – 1253Combined sources
Beta strandi134 – 1407Combined sources
Turni147 – 1493Combined sources
Helixi150 – 1523Combined sources
Beta strandi153 – 1586Combined sources
Helixi160 – 1623Combined sources
Helixi168 – 1714Combined sources
Beta strandi174 – 1763Combined sources
Helixi177 – 18610Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi213 – 2164Combined sources
Helixi217 – 22913Combined sources
Turni230 – 2334Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi259 – 2624Combined sources
Helixi266 – 27712Combined sources
Beta strandi281 – 2855Combined sources
Turni297 – 2993Combined sources
Beta strandi303 – 3097Combined sources
Beta strandi324 – 3285Combined sources
Beta strandi330 – 3367Combined sources
Turni337 – 3393Combined sources
Beta strandi340 – 3445Combined sources
Helixi347 – 36923Combined sources
Beta strandi382 – 3854Combined sources
Helixi386 – 3938Combined sources
Beta strandi398 – 4036Combined sources
Turni404 – 4063Combined sources
Helixi413 – 4219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E1PX-ray2.30A25-422[»]
2Z2XX-ray1.70A105-422[»]
2Z2YX-ray1.89A/C105-422[»]
B/D29-93[»]
2Z2ZX-ray1.87A28-422[»]
2Z30X-ray1.65A103-422[»]
B29-93[»]
2Z56X-ray1.90A105-422[»]
B29-93[»]
2Z57X-ray1.80A105-422[»]
B29-93[»]
2Z58X-ray1.88A105-422[»]
B28-93[»]
2ZRQX-ray2.16A94-422[»]
2ZWOX-ray2.07A/B/C25-422[»]
2ZWPX-ray2.40A/B25-422[»]
3A3NX-ray2.20A94-422[»]
B25-91[»]
3A3OX-ray1.90A94-422[»]
B25-88[»]
3A3PX-ray1.90A94-422[»]
B25-93[»]
3VHQX-ray2.15A25-422[»]
3VV2X-ray1.83A94-422[»]
B25-93[»]
3WIUX-ray1.80A/B/C25-422[»]
3WIVX-ray1.90A/B/C25-422[»]
4JP8X-ray2.21A25-422[»]
ProteinModelPortaliP58502.
SMRiP58502. Positions 28-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58502.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 417283Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1404.
HOGENOMiHOG000199176.
InParanoidiP58502.
KOiK01362.
OMAiDACDEAY.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 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.

P58502-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKSIALVLS IVLLAALFAV PASAGEQNTI RVIVSVDKAK FNPHEVLGIG
60 70 80 90 100
GHIVYQFKLI PAVVVDVPAN AVGKLKKMPG VEKVEFDHQA VLLGKPSWLG
110 120 130 140 150
GGSTQPAQTI PWGIERVKAP SVWSITDGSV SVIQVAVLDT GVDYDHPDLA
160 170 180 190 200
ANIAWCVSTL RGKVSTKLRD CADQNGHGTH VIGTIAALNN DIGVVGVAPG
210 220 230 240 250
VQIYSVRVLD ARGSGSYSDI AIGIEQAILG PDGVADKDGD GIIAGDPDDD
260 270 280 290 300
AAEVISMSLG GPADDSYLYD MIIQAYNAGI VIVAASGNEG APSPSYPAAY
310 320 330 340 350
PEVIAVGAID SNDNIASFSN RQPEVSAPGV DILSTYPDDS YETLMGTSMA
360 370 380 390 400
TPHVSGVVAL IQAAYYQKYG KILPVGTFDD ISKNTVRGIL HITADDLGPT
410 420
GWDADYGYGV VRAALAVQAA LG
Length:422
Mass (Da):43,786
Last modified:December 19, 2001 - v1
Checksum:i843255BCD806DB71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056701 Genomic DNA. Translation: BAB60701.1.
AP006878 Genomic DNA. Translation: BAD85864.1.
RefSeqiWP_011250626.1. NC_006624.1.
YP_184088.1. NC_006624.1.

Genome annotation databases

EnsemblBacteriaiBAD85864; BAD85864; TK1675.
GeneIDi3234572.
KEGGitko:TK1675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056701 Genomic DNA. Translation: BAB60701.1.
AP006878 Genomic DNA. Translation: BAD85864.1.
RefSeqiWP_011250626.1. NC_006624.1.
YP_184088.1. NC_006624.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E1PX-ray2.30A25-422[»]
2Z2XX-ray1.70A105-422[»]
2Z2YX-ray1.89A/C105-422[»]
B/D29-93[»]
2Z2ZX-ray1.87A28-422[»]
2Z30X-ray1.65A103-422[»]
B29-93[»]
2Z56X-ray1.90A105-422[»]
B29-93[»]
2Z57X-ray1.80A105-422[»]
B29-93[»]
2Z58X-ray1.88A105-422[»]
B28-93[»]
2ZRQX-ray2.16A94-422[»]
2ZWOX-ray2.07A/B/C25-422[»]
2ZWPX-ray2.40A/B25-422[»]
3A3NX-ray2.20A94-422[»]
B25-91[»]
3A3OX-ray1.90A94-422[»]
B25-88[»]
3A3PX-ray1.90A94-422[»]
B25-93[»]
3VHQX-ray2.15A25-422[»]
3VV2X-ray1.83A94-422[»]
B25-93[»]
3WIUX-ray1.80A/B/C25-422[»]
3WIVX-ray1.90A/B/C25-422[»]
4JP8X-ray2.21A25-422[»]
ProteinModelPortaliP58502.
SMRiP58502. Positions 28-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8404006.
STRINGi69014.TK1675.

Protein family/group databases

MEROPSiS08.129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD85864; BAD85864; TK1675.
GeneIDi3234572.
KEGGitko:TK1675.

Phylogenomic databases

eggNOGiCOG1404.
HOGENOMiHOG000199176.
InParanoidiP58502.
KOiK01362.
OMAiDACDEAY.

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1707-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP58502.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence."
    Kannan Y., Koga Y., Inoue Y., Haruki M., Takagi M., Imanaka T., Morikawa M., Kanaya S.
    Appl. Environ. Microbiol. 67:2445-2452(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.
  2. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
    Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
    Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Entry informationi

Entry nameiTKSU_THEKO
AccessioniPrimary (citable) accession number: P58502
Secondary accession number(s): Q977F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 19, 2001
Last sequence update: December 19, 2001
Last modified: January 7, 2015
This is version 99 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, 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

External Data

Dasty 3

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 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.