P04072 (THET_THEVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Thermitase EC=3.4.21.66
Organism	Thermoactinomyces vulgaris
Taxonomic identifier	2026 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Thermoactinomycetaceae › Thermoactinomyces

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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.
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Chain

1 – 279

279

Thermitase

PRO_0000076421

Sites

Active site

38

1

Active site

71

1

Active site

225

1

Metal binding

5

1

Calcium 1

Metal binding

47

1

Calcium 1

Metal binding

57

1

Calcium 2

Metal binding

60

1

Calcium 2

Metal binding

62

1

Calcium 2

Metal binding

64

1

Calcium 2

Metal binding

66

1

Calcium 2

Metal binding

82

1

Calcium 1; via carbonyl oxygen

Metal binding

85

1

Calcium 1

Metal binding

87

1

Calcium 1; via carbonyl oxygen

Metal binding

89

1

Calcium 1; via carbonyl oxygen

Secondary structure

1

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279

Helix Strand Turn

Details...

Helix

8 – 11

4

Helix

14 – 17

4

Helix

20 – 24

5

Beta strand

33 – 39

7

Turn

46 – 51

6

Beta strand

52 – 57

6

Turn

58 – 61

4

Beta strand

68 – 70

3

Helix

71 – 80

10

Beta strand

84 – 88

5

Beta strand

97 – 102

6

Helix

112 – 124

13

Beta strand

128 – 132

5

Beta strand

136 – 138

3

Helix

141 – 152

12

Beta strand

156 – 160

5

Beta strand

163 – 166

4

Turn

172 – 174

3

Beta strand

178 – 184

7

Beta strand

202 – 205

4

Beta strand

207 – 213

7

Turn

214 – 216

3

Beta strand

217 – 221

5

Helix

224 – 239

16

Turn

240 – 242

3

Helix

245 – 254

10

Turn

260 – 264

5

Beta strand

267 – 270

4

Helix

273 – 278

6

Sequences

	Sequence		Length	Mass (Da)
	P04072 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 8065049BC8927AC0	FASTA	279	28,366
	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

References

[1]	"Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases." Meloun B., Baudys M., Kostka V., Hausdorf G., Frommel C., Hohne W.E. FEBS Lett. 183:195-200(1985) Cited for: PROTEIN SEQUENCE.
[2]	"Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2-A resolution." Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Frommel C., Hohne W.E. FEBS Lett. 244:208-212(1989) [PubMed: 2647518] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]	"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." Gros P., Betzel C., Dauter Z., Wilson K.S., Hol W.G.J. J. Mol. Biol. 210:347-367(1989) [PubMed: 2689655] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
[4]	"Crystal structure of thermitase at 1.4-A resolution." Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Vainshtein B.K., Frommel C., Hohne W.E., Wilson K.S. J. Mol. Biol. 214:261-279(1990) [PubMed: 2196375] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[5]	"Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium." Gros P., Kalk K.H., Hol W.G.J. J. Biol. Chem. 266:2953-2961(1991) [PubMed: 1993669] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

SUMYTV. A00973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TEC	X-ray	2.20	E	1-279	[»]
1THM	X-ray	1.37	A	1-279	[»]
2TEC	X-ray	1.98	E	1-279	[»]
3TEC	X-ray	2.00	E	1-279	[»]

ProteinModelPortal

P04072.

SMR

P04072. Positions 1-279.

ModBase

Search...

Protein family/group databases

MEROPS

S08.007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

THET_THEVU

Accession

Primary (citable) accession number: P04072

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program