[1]	PROTEIN SEQUENCE. Meloun B., Baudys M., Kostka V., Hausdorf G., Frommel C., Hohne W.E.; "Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases."; FEBS Lett. 183:195-200(1985).
[2]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1016/0014-5793(89)81194-9; PubMed=2647518 [NCBI, ExPASy, EBI, Israel, Japan] Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Frommel C., Hohne W.E.; "Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2-A resolution."; FEBS Lett. 244:208-212(1989).
[3]	X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS). DOI=10.1016/0022-2836(89)90336-7; PubMed=2689655 [NCBI, ExPASy, EBI, Israel, Japan] Gros P., Betzel C., Dauter Z., Wilson K.S., Hol W.G.J.; "Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98-A resolution and comparison of two crystal forms that differ in calcium content."; J. Mol. Biol. 210:347-367(1989).
[4]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). DOI=10.1016/0022-2836(90)90160-N; PubMed=2196375 [NCBI, ExPASy, EBI, Israel, Japan] Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Vainshtein B.K., Frommel C., Hohne W.E., Wilson K.S.; "Crystal structure of thermitase at 1.4-A resolution."; J. Mol. Biol. 214:261-279(1990).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=1993669 [NCBI, ExPASy, EBI, Israel, Japan] Gros P., Kalk K.H., Hol W.G.J.; "Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium."; J. Biol. Chem. 266:2953-2961(1991).

Comments

CATALYTIC ACTIVITY: Hydrolysis of proteins, including collagen.
COFACTOR: Binds 3 calcium ions or 2 calcium ions and 1 sodium ion per subunit. The sodium ion is bound at calcium concentrations up to 5 mM. At 100 mM calcium 3 calcium ions are bound.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peptidase S8 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00973; SUMYTV.

3D structure databases

PDB

1TEC; X-ray; 2.20 A; E=1-279.	[ExPASy / RCSB / EBI]
1THM; X-ray; 1.37 A; A=1-279.	[ExPASy / RCSB / EBI]
2TEC; X-ray; 1.98 A; E=1-279.	[ExPASy / RCSB / EBI]
3TEC; X-ray; 2.00 A; E=1-279.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1TEC; -.
1THM; -.
2TEC; -.
3TEC; -.

ModBase

P04072.

Protein family/group databases

MEROPS

S08.007; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.200; Pept_S8_S53; 1.

PANTHER

PTHR10795; SubtilSerProt; 1.

Pfam

PF00082; Peptidase_S8; 1.
Pfam graphical view of domain structure.

PRINTS

PR00723; SUBTILISIN.

PROSITE

PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.

Other

P04072; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 279`	`279`	`Thermitase.`	`PRO_0000076421`
`ACT_SITE`	`38 38`
`ACT_SITE`	`71 71`
`ACT_SITE`	`225 225`
`METAL`	`5 5`		`Calcium 1.`
`METAL`	`47 47`		`Calcium 1.`
`METAL`	`57 57`		`Calcium 2.`
`METAL`	`60 60`		`Calcium 2.`
`METAL`	`62 62`		`Calcium 2.`
`METAL`	`64 64`		`Calcium 2.`
`METAL`	`66 66`		`Calcium 2.`
`METAL`	`82 82`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`85 85`		`Calcium 1.`
`METAL`	`87 87`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`89 89`		`Calcium 1; via carbonyl oxygen.`
`HELIX`	`8 11`	`4`
`HELIX`	`14 17`	`4`
`HELIX`	`20 24`	`5`
`STRAND`	`33 39`	`7`
`TURN`	`46 51`	`6`
`STRAND`	`52 57`	`6`
`TURN`	`58 61`	`4`
`STRAND`	`68 70`	`3`
`HELIX`	`71 80`	`10`
`STRAND`	`84 88`	`5`
`STRAND`	`97 102`	`6`
`HELIX`	`112 124`	`13`
`STRAND`	`128 132`	`5`
`STRAND`	`136 138`	`3`
`HELIX`	`141 152`	`12`
`STRAND`	`156 160`	`5`
`STRAND`	`163 166`	`4`
`TURN`	`172 174`	`3`
`STRAND`	`178 184`	`7`
`STRAND`	`202 205`	`4`
`STRAND`	`207 213`	`7`
`TURN`	`214 216`	`3`
`STRAND`	`217 221`	`5`
`HELIX`	`224 239`	`16`
`TURN`	`240 242`	`3`
`HELIX`	`245 254`	`10`
`TURN`	`260 264`	`5`
`STRAND`	`267 270`	`4`
`HELIX`	`273 278`	`6`

Sequence information

Length: 279 AA [This is the length of the unprocessed precursor]

Molecular weight: 28366 Da [This is the MW of the unprocessed precursor]

CRC64: 8065049BC8927AC0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
YTPNDPYFSS RQYGPQKIQA PQAWDIAEGS GAKIAIVDTG VQSNHPDLAG KVVGGWDFVD 

        70         80         90        100        110        120 
NDSTPQNGNG HGTHCAGIAA AVTNNSTGIA GTAPKASILA VRVLDNSGSG TWTAVANGIT 

       130        140        150        160        170        180 
YAADQGAKVI SLSLGGTVGN SGLQQAVNYA WNKGSVVVAA AGNAGNTAPN YPAYYSNAIA 

       190        200        210        220        230        240 
VASTDQNDNK SSFSTYGSVV DVAAPGSWIY STYPTSTYAS LSGTSMATPH VAGVAGLLAS 

       250        260        270 
QGRSASNIRA AIENTADKIS GTGTYWAKGR VNAYKAVQY

P04072 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools