Reviewed, UniProtKB/Swiss-Prot P06873 (PRTK_TRIAL)

Names and origin

Protein names

Recommended name:
    Proteinase K
    EC=3.4.21.64
Alternative name(s):
    Tritirachium alkaline proteinase
    Endopeptidase K

Gene names

Name:

PROK

Organism

Tritirachium album (Engyodontium album)

Taxonomic identifier

37998 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Engyodontium

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes keratin at aromatic and hydrophobic residues.
Catalytic activity	Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
Cofactor	Binds 2 calcium ions per subunit.
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Propeptide

16 – 105

90

Ref.2 Ref.3

PRO_0000027138

Chain

106 – 384

279

Proteinase K

PRO_0000027139

Sites

Active site

144

1

Charge relay system

Active site

174

1

Charge relay system

Active site

329

1

Charge relay system

Metal binding

121

1

Calcium 2; via carbonyl oxygen

Metal binding

280

1

Calcium 1; via carbonyl oxygen

Metal binding

282

1

Calcium 1; via carbonyl oxygen

Metal binding

305

1

Calcium 1

Metal binding

365

1

Calcium 2

Amino acid modifications

Disulfide bond

139 ↔ 228

Disulfide bond

283 ↔ 354

Experimental info

Sequence conflict

184

1

S → SG AA sequence Ref.2

Sequence conflict

184

1

S → SG AA sequence Ref.3

Sequence conflict

312 – 316

5

SILST → DLS AA sequence Ref.2

Sequence conflict

312 – 316

5

SILST → DLS AA sequence Ref.3

Sequence conflict

312 – 316

5

SILST → DLS AA sequence Ref.4

Sequence conflict

374

1

V → F AA sequence Ref.2

Sequence conflict

377

1

Missing AA sequence Ref.2

Sequence conflict

377

1

Missing AA sequence Ref.3

Secondary structure

1

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384

Helix Strand Turn

Details...

Helix

113 – 118

6

Turn

132 – 137

6

Beta strand

138 – 145

8

Helix

152 – 154

3

Beta strand

158 – 166

9

Beta strand

171 – 173

3

Helix

174 – 183

10

Turn

185 – 187

3

Beta strand

194 – 199

6

Helix

209 – 222

14

Helix

223 – 225

3

Beta strand

231 – 236

6

Helix

244 – 255

12

Beta strand

259 – 263

5

Beta strand

266 – 270

5

Helix

271 – 273

3

Turn

276 – 278

3

Beta strand

282 – 288

7

Beta strand

292 – 294

3

Beta strand

306 – 309

4

Beta strand

311 – 317

7

Turn

318 – 320

3

Beta strand

321 – 325

5

Helix

328 – 344

17

Turn

350 – 352

3

Helix

353 – 360

8

Beta strand

361 – 364

4

Sequences

	Sequence		Length	Mass (Da)
	P06873-1 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 00E1B111F0EFF5C4	FASTA	384	40,300
	10 20 30 40 50 60 MRLSVLLSLL PLALGAPAVE QRSEAAPLIE ARGEMVANKY IVKFKEGSAL SALDAAMEKI 70 80 90 100 110 120 SGKPDHVYKN VFSGFAATLD ENMVRVLRAH PDVEYIEQDA VVTINAAQTN APWGLARISS 130 140 150 160 170 180 TSPGTSTYYY DESAGQGSCV YVIDTGIEAS HPEFEGRAQM VKTYYYSSRD GNGHGTHCAG 190 200 210 220 230 240 TVGSRTYGVA KKTQLFGVKV LDDNGSGQYS TIIAGMDFVA SDKNNRNCPK GVVASLSLGG 250 260 270 280 290 300 GYSSSVNSAA ARLQSSGVMV AVAAGNNNAD ARNYSPASEP SVCTVGASDR YDRRSSFSNY 310 320 330 340 350 360 GSVLDIFGPG TSILSTWIGG STRSISGTSM ATPHVAGLAA YLMTLGKTTA ASACRYIADT 370 380 ANKGDLSNIP FGTVNLLAYN NYQA

References

[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: 2645134] [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: 3924077] [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: 6378621] [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: 8083213] [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: 9741842] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.

PIR

SUTIKA. S02142.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJR	X-ray	2.44	E	106-384	[»]
1CNM	X-ray	2.20	A	106-384	[»]
1EGQ	X-ray	1.55	A	106-384	[»]
1HT3	X-ray	1.80	A	106-384	[»]
1IC6	X-ray	0.98	A	106-384	[»]
1OYO	X-ray	2.02	A	106-384	[»]
1P7V	X-ray	1.08	A	106-384	[»]
1P7W	X-ray	1.02	A	106-384	[»]
1PEK	X-ray	2.20	E	106-384	[»]
1PFG	X-ray	2.50	A	106-384	[»]
1PJ8	X-ray	2.20	A	106-384	[»]
1PTK	X-ray	2.40	A	106-384	[»]
2DP4	X-ray	2.90	E	106-384	[»]
2DQK	X-ray	1.93	A	106-384	[»]
2DUJ	X-ray	1.67	A	106-384	[»]
2G4V	X-ray	2.14	A	106-384	[»]
2HD4	X-ray	2.15	A	106-384	[»]
2HPZ	X-ray	1.69	A	106-384	[»]
2ID8	X-ray	1.27	A	106-384	[»]
2PKC	X-ray	1.50	A	106-384	[»]
2PQ2	X-ray	1.82	A	106-384	[»]
2PRK	X-ray	1.50	A	106-384	[»]
2PWA	X-ray	0.83	A	106-384	[»]
2PWB	X-ray	1.90	A	106-384	[»]
2PYZ	X-ray	1.79	A	106-384	[»]
2V8B	X-ray	0.94	A	106-384	[»]
3DYB	X-ray	1.32	A	106-384	[»]
3GT3	X-ray	1.50	A	106-384	[»]
3GT4	X-ray	1.76	A	106-384	[»]
3PRK	X-ray	2.20	E	106-384	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S08.054.

Enzyme and pathway databases

BRENDA

3.4.21.64. 18581.

Family and domain databases

InterPro

IPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR010259. Prot_inh_S8A.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

PROSITE

PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRTK_TRIAL

Accession

Primary (citable) accession number: P06873

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)