Reviewed,
UniProtKB/Swiss-Prot P06874 (THER_BACST)
Last modified
June 16, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thermolysin EC=3.4.24.27 Alternative name(s): Thermostable neutral proteinase | ||
| Gene names |
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| Organism | Bacillus stearothermophilus (Geobacillus stearothermophilus) | ||
| Taxonomic identifier | 1422 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus |
Protein attributes
| Sequence length | 548 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 | Extracellular zinc metalloprotease. |
| Catalytic activity | Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe. |
| Cofactor | Binds 4 calcium ions per subunit. Binds 1 zinc ion per subunit. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase M4 family. |
| biophysicochemical properties | Temperature dependence: Thermostable. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | |||||||
| Propeptide | 26 – 229 | 204 | Activation peptide Ref.1 | PRO_0000028590 | |||||
| Chain | 230 – 548 | 319 | Thermolysin | PRO_0000028591 | |||||
Sites | |||||||||
| Active site | 375 | 1 | |||||||
| Active site | 463 | 1 | Proton donor | ||||||
| Metal binding | 289 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 291 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 293 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 370 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 374 | 1 | Zinc; catalytic | ||||||
| Metal binding | 378 | 1 | Zinc; catalytic | ||||||
| Metal binding | 398 | 1 | Zinc; catalytic | ||||||
| Metal binding | 409 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 409 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 415 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 417 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 417 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 419 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 422 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 422 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 425 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 426 | 1 | Calcium 4 By similarity | ||||||
| Metal binding | 429 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 432 | 1 | Calcium 4 By similarity | ||||||
Sequences
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References
| [1] | "Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus." Takagi M., Imanaka T., Aiba S. J. Bacteriol. 163:824-831(1985) [PubMed: 2993245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 230-243. |
Cross-references
Sequence databases | |
|---|---|
| M11446 Genomic DNA. Translation: AAA22621.1. | |
| PIR | HYBSS. A24924. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KJO based on UniProtKB P00800. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M04.001. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.27. 266715. |
Family and domain databases | |
| InterPro | IPR005075. Pept_M4_propep_PepSY. IPR006025. Pept_M_Zn_BS. IPR013856. Peptidase_M4. IPR001570. Peptidase_M4_C. IPR011096. Propep_M4_M36. [Graphical view] |
| Gene3D | G3DSA:3.10.170.10. Peptidase_M4. 1 hit. G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit. |
| Pfam | PF07504. FTP. 1 hit. PF03413. PepSY. 1 hit. PF01447. Peptidase_M4. 1 hit. PF02868. Peptidase_M4_C. 1 hit. [Graphical view] |
| PRINTS | PR00730. THERMOLYSIN. |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | THER_BACST | ||||||||
| Accession | Primary (citable) accession number: P06874 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


