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Protein

Proteinase K

Gene

PROK

Organism
Engyodontium album (Tritirachium album)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes keratin at aromatic and hydrophobic residues.

Catalytic activityi

Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211Calcium 2; via carbonyl oxygen
Active sitei144 – 1441Charge relay system
Active sitei174 – 1741Charge relay system
Metal bindingi280 – 2801Calcium 1; via carbonyl oxygen
Metal bindingi282 – 2821Calcium 1; via carbonyl oxygen
Metal bindingi305 – 3051Calcium 1
Active sitei329 – 3291Charge relay system
Metal bindingi365 – 3651Calcium 2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.64. 6510.

Protein family/group databases

MEROPSiS08.054.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase K (EC:3.4.21.64)
Alternative name(s):
Endopeptidase K
Tritirachium alkaline proteinase
Gene namesi
Name:PROK
OrganismiEngyodontium album (Tritirachium album)
Taxonomic identifieri37998 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotamitosporic AscomycotaEngyodontium

Pathology & Biotechi

Protein family/group databases

Allergomei8265. Tri al Proteinase K.

Chemistry

ChEMBLiCHEMBL1075070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Propeptidei16 – 105902 PublicationsPRO_0000027138Add
BLAST
Chaini106 – 384279Proteinase KPRO_0000027139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi139 ↔ 228
Disulfide bondi283 ↔ 354

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP06873.

Interactioni

Chemistry

BindingDBiP06873.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi107 – 1093Combined sources
Helixi113 – 1186Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi127 – 1293Combined sources
Turni132 – 1376Combined sources
Beta strandi138 – 1458Combined sources
Helixi152 – 1543Combined sources
Beta strandi158 – 1669Combined sources
Beta strandi171 – 1733Combined sources
Helixi174 – 18310Combined sources
Turni185 – 1873Combined sources
Beta strandi194 – 1996Combined sources
Helixi209 – 22214Combined sources
Helixi223 – 2253Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi238 – 2414Combined sources
Helixi244 – 25512Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi266 – 2705Combined sources
Helixi271 – 2733Combined sources
Turni276 – 2783Combined sources
Beta strandi282 – 2887Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi300 – 3034Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi311 – 3177Combined sources
Turni318 – 3203Combined sources
Beta strandi321 – 3255Combined sources
Helixi328 – 34417Combined sources
Turni350 – 3523Combined sources
Helixi353 – 3608Combined sources
Beta strandi361 – 3644Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJRX-ray2.44E106-384[»]
1CNMX-ray2.20A106-384[»]
1EGQX-ray1.55A106-384[»]
1HT3X-ray1.80A106-384[»]
1IC6X-ray0.98A106-384[»]
1OYOX-ray2.02A106-384[»]
1P7VX-ray1.08A106-384[»]
1P7WX-ray1.02A106-384[»]
1PEKX-ray2.20E106-384[»]
1PFGX-ray2.50A106-384[»]
1PJ8X-ray2.20A106-384[»]
1PTKX-ray2.40A106-384[»]
2DP4X-ray2.90E106-384[»]
2DQKX-ray1.93A106-384[»]
2DUJX-ray1.67A106-384[»]
2G4VX-ray2.14A106-384[»]
2HD4X-ray2.15A106-384[»]
2HPZX-ray1.69A106-384[»]
2ID8X-ray1.27A106-384[»]
2PKCX-ray1.50A106-384[»]
2PQ2X-ray1.82A106-384[»]
2PRKX-ray1.50A106-384[»]
2PWAX-ray0.83A106-384[»]
2PWBX-ray1.90A106-384[»]
2PYZX-ray1.79A106-384[»]
2V8BX-ray0.94A106-384[»]
3AJ8X-ray1.10A106-384[»]
3AJ9X-ray1.10A106-384[»]
3D9QX-ray1.43X106-384[»]
3DDZX-ray1.70X106-384[»]
3DE0X-ray1.90X106-384[»]
3DE1X-ray2.00X106-384[»]
3DE2X-ray2.10X106-384[»]
3DE3X-ray1.43X106-384[»]
3DE4X-ray1.80X106-384[»]
3DE5X-ray2.10X106-384[»]
3DE6X-ray2.20X106-384[»]
3DE7X-ray2.30X106-384[»]
3DVQX-ray1.02X106-384[»]
3DVRX-ray1.02X106-384[»]
3DVSX-ray1.02X106-384[»]
3DW1X-ray1.03X106-384[»]
3DW3X-ray0.99X106-384[»]
3DWEX-ray0.99X106-384[»]
3DYBX-ray1.32A106-384[»]
3GT3X-ray1.50A106-384[»]
3GT4X-ray1.76A106-384[»]
3I2YX-ray1.00X106-384[»]
3I30X-ray0.99X106-384[»]
3I34X-ray1.00X106-384[»]
3I37X-ray1.00X106-384[»]
3L1KX-ray1.55A106-384[»]
3OSZX-ray2.26A106-384[»]
3PRKX-ray2.20E106-384[»]
3PTLX-ray1.30A106-384[»]
3Q40X-ray1.80A106-384[»]
3Q5GX-ray1.77A106-384[»]
3QMPX-ray1.10A106-384[»]
4B5LX-ray1.60A106-384[»]
4DJ5X-ray1.80X106-384[»]
4FONX-ray1.05A106-384[»]
4WOBX-ray1.90A106-384[»]
4WOCX-ray1.60A106-384[»]
4ZARX-ray1.15A106-384[»]
5CW1X-ray1.45A106-384[»]
ProteinModelPortaliP06873.
SMRiP06873. Positions 106-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 365226Peptidase S8Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 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.

P06873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSVLLSLL PLALGAPAVE QRSEAAPLIE ARGEMVANKY IVKFKEGSAL
60 70 80 90 100
SALDAAMEKI SGKPDHVYKN VFSGFAATLD ENMVRVLRAH PDVEYIEQDA
110 120 130 140 150
VVTINAAQTN APWGLARISS TSPGTSTYYY DESAGQGSCV YVIDTGIEAS
160 170 180 190 200
HPEFEGRAQM VKTYYYSSRD GNGHGTHCAG TVGSRTYGVA KKTQLFGVKV
210 220 230 240 250
LDDNGSGQYS TIIAGMDFVA SDKNNRNCPK GVVASLSLGG GYSSSVNSAA
260 270 280 290 300
ARLQSSGVMV AVAAGNNNAD ARNYSPASEP SVCTVGASDR YDRRSSFSNY
310 320 330 340 350
GSVLDIFGPG TSILSTWIGG STRSISGTSM ATPHVAGLAA YLMTLGKTTA
360 370 380
ASACRYIADT ANKGDLSNIP FGTVNLLAYN NYQA
Length:384
Mass (Da):40,300
Last modified:January 1, 1990 - v2
Checksum:i00E1B111F0EFF5C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841S → SG AA sequence (Ref. 2) Curated
Sequence conflicti184 – 1841S → SG AA sequence (Ref. 3) Curated
Sequence conflicti312 – 3165SILST → DLS AA sequence (Ref. 2) Curated
Sequence conflicti312 – 3165SILST → DLS AA sequence (Ref. 3) Curated
Sequence conflicti312 – 3165SILST → DLS AA sequence (PubMed:3924077).Curated
Sequence conflicti374 – 3741V → F AA sequence (Ref. 2) Curated
Sequence conflicti377 – 3771Missing AA sequence (Ref. 2) Curated
Sequence conflicti377 – 3771Missing AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.
PIRiS02142. SUTIKA.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.
PIRiS02142. SUTIKA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJRX-ray2.44E106-384[»]
1CNMX-ray2.20A106-384[»]
1EGQX-ray1.55A106-384[»]
1HT3X-ray1.80A106-384[»]
1IC6X-ray0.98A106-384[»]
1OYOX-ray2.02A106-384[»]
1P7VX-ray1.08A106-384[»]
1P7WX-ray1.02A106-384[»]
1PEKX-ray2.20E106-384[»]
1PFGX-ray2.50A106-384[»]
1PJ8X-ray2.20A106-384[»]
1PTKX-ray2.40A106-384[»]
2DP4X-ray2.90E106-384[»]
2DQKX-ray1.93A106-384[»]
2DUJX-ray1.67A106-384[»]
2G4VX-ray2.14A106-384[»]
2HD4X-ray2.15A106-384[»]
2HPZX-ray1.69A106-384[»]
2ID8X-ray1.27A106-384[»]
2PKCX-ray1.50A106-384[»]
2PQ2X-ray1.82A106-384[»]
2PRKX-ray1.50A106-384[»]
2PWAX-ray0.83A106-384[»]
2PWBX-ray1.90A106-384[»]
2PYZX-ray1.79A106-384[»]
2V8BX-ray0.94A106-384[»]
3AJ8X-ray1.10A106-384[»]
3AJ9X-ray1.10A106-384[»]
3D9QX-ray1.43X106-384[»]
3DDZX-ray1.70X106-384[»]
3DE0X-ray1.90X106-384[»]
3DE1X-ray2.00X106-384[»]
3DE2X-ray2.10X106-384[»]
3DE3X-ray1.43X106-384[»]
3DE4X-ray1.80X106-384[»]
3DE5X-ray2.10X106-384[»]
3DE6X-ray2.20X106-384[»]
3DE7X-ray2.30X106-384[»]
3DVQX-ray1.02X106-384[»]
3DVRX-ray1.02X106-384[»]
3DVSX-ray1.02X106-384[»]
3DW1X-ray1.03X106-384[»]
3DW3X-ray0.99X106-384[»]
3DWEX-ray0.99X106-384[»]
3DYBX-ray1.32A106-384[»]
3GT3X-ray1.50A106-384[»]
3GT4X-ray1.76A106-384[»]
3I2YX-ray1.00X106-384[»]
3I30X-ray0.99X106-384[»]
3I34X-ray1.00X106-384[»]
3I37X-ray1.00X106-384[»]
3L1KX-ray1.55A106-384[»]
3OSZX-ray2.26A106-384[»]
3PRKX-ray2.20E106-384[»]
3PTLX-ray1.30A106-384[»]
3Q40X-ray1.80A106-384[»]
3Q5GX-ray1.77A106-384[»]
3QMPX-ray1.10A106-384[»]
4B5LX-ray1.60A106-384[»]
4DJ5X-ray1.80X106-384[»]
4FONX-ray1.05A106-384[»]
4WOBX-ray1.90A106-384[»]
4WOCX-ray1.60A106-384[»]
4ZARX-ray1.15A106-384[»]
5CW1X-ray1.45A106-384[»]
ProteinModelPortaliP06873.
SMRiP06873. Positions 106-384.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP06873.
ChEMBLiCHEMBL1075070.

Protein family/group databases

Allergomei8265. Tri al Proteinase K.
MEROPSiS08.054.

Proteomic databases

PRIDEiP06873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.64. 6510.

Miscellaneous databases

EvolutionaryTraceiP06873.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Proteinase K from Tritirachium album Limber. Characterization of the chromosomal gene and expression of the cDNA in Escherichia coli."
    Gunkel F.A., Gassen H.G.
    Eur. J. Biochem. 179:185-194(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: ATCC 22563 / Limber.
  2. "Proteinase K - a new subclass of the subtilisins. The amino acid sequence of the enzyme."
    Jany K.-D., Lederer G., Mayer B.
    Biol. Chem. Hoppe-Seyler 367:87-87(1986)
    Cited for: PROTEIN SEQUENCE OF 106-384.
  3. "Amino acid sequence of proteinase K from the mold Tritirachium album limber. Proteinase K - a subtilisin-related enzyme with disulfide bonds."
    Jany K.-D., Lederer G., Mayer B.
    FEBS Lett. 199:139-144(1986)
    Cited for: PROTEIN SEQUENCE OF 106-384.
  4. "Proteinase K from Tritirachium album limber. I. Molecular mass and sequence around the active site serine residue."
    Jany K.-D., Mayer B.
    Biol. Chem. Hoppe-Seyler 366:485-492(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 259-343.
  5. "Three-dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin."
    Paehler A., Banerjee A., Dattagupta J.K., Fujiwara T., Lindner K., Pal G.P., Suck D., Weber G., Saenger W.
    EMBO J. 3:1311-1314(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
  6. "Crystal structure of calcium-free proteinase K at 1.5-A resolution."
    Mueller A., Hinrichs W., Wolf W.M., Saenger W.
    J. Biol. Chem. 269:23108-23111(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  7. "Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K."
    Singh T.P., Sharma S., Karthikeyan S., Betzel C., Bhatia K.L.
    Proteins 33:30-38(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS).

Entry informationi

Entry nameiPRTK_ENGAL
AccessioniPrimary (citable) accession number: P06873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1990
Last modified: February 17, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.