Q59193 (THER_BACCL) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thermolysin EC=3.4.24.27 Alternative name(s): Thermostable neutral proteinase | ||
| Gene names |
| ||
| Organism | Bacillus caldolyticus | ||
| Taxonomic identifier | 1394 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus![]() |
Protein attributes
| Sequence length | 546 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 |
| 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 metalloendopeptidase activityInferred 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 – 25 | 25 | Potential | ||||||
| Propeptide | 26 – 228 | 203 | Activation peptide | PRO_0000028586 | |||||
| Chain | 229 – 546 | 318 | Thermolysin | PRO_0000028587 | |||||
Sites | |||||||||
| Active site | 373 | 1 | By similarity | ||||||
| Active site | 461 | 1 | Proton donor By similarity | ||||||
| Metal binding | 287 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 289 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 291 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 368 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 372 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 376 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 396 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 413 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 415 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 415 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 417 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 420 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 420 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 423 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 424 | 1 | Calcium 4 By similarity | ||||||
| Metal binding | 427 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 430 | 1 | Calcium 4 By similarity | ||||||
Sequences
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References
| [1] | "Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. strain EA1: expression in Escherichia coli and characterisation." Saul D.J., Williams L.C., Toogood H.S., Daniel R.M., Bergquist P.L. Biochim. Biophys. Acta 1308:74-80(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 405 / NBRC 15313 / YP-T. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U25629 Genomic DNA. Translation: AAB18652.1. |
| PIR | S72176. |
3D structure databases | |
| ProteinModelPortal | Q59193. |
| SMR | Q59193. Positions 228-545. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M04.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.10.170.10. 1 hit. |
| InterPro | IPR011096. FTP_domain. IPR025711. PepSY. IPR023612. Peptidase_M4. IPR001570. Peptidase_M4_C_domain. IPR013856. Peptidase_M4_domain. [Graphical view] |
| 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_BACCL | ||||||||
| Accession | Primary (citable) accession number: Q59193 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
