P23384 (NPRE_BACCL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 75.
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: Bacillolysin EC=3.4.24.28 Alternative name(s): Thermostable neutral protease | ||
| Gene names |
| ||
| Organism | Bacillus caldolyticus | ||
| Taxonomic identifier | 1394 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 544 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 | Similar, but not identical, to that of thermolysin. |
| Cofactor | Binds 4 calcium ions per subunit By similarity. Binds 1 zinc ion per subunit By similarity. |
| 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 | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred 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 | |||||||
| Propeptide | 26 – 225 | 200 | Activation peptide | PRO_0000028600 | |||||
| Chain | 226 – 544 | 319 | Bacillolysin | PRO_0000028601 | |||||
Sites | |||||||||
| Active site | 371 | 1 | By similarity | ||||||
| Active site | 459 | 1 | Proton donor By similarity | ||||||
| Metal binding | 285 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 287 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 289 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 366 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 370 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 374 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 394 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 405 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 405 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 411 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 413 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 413 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 415 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 418 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 418 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 421 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 422 | 1 | Calcium 4 By similarity | ||||||
| Metal binding | 425 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 428 | 1 | Calcium 4 By similarity | ||||||
Sequences
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References
| [1] | "A highly thermostable neutral protease from Bacillus caldolyticus: cloning and expression of the gene in Bacillus subtilis and characterization of the gene product." van den Burg B., Enequist H.G., van de Haar M.E., Eijsink V.G.H., Stulp B.K., Venema G. J. Bacteriol. 173:4107-4115(1991) [PubMed: 1905714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M63575 Genomic DNA. Translation: AAA22623.1. |
| PIR | A42464. |
3D structure databases | |
| ProteinModelPortal | P23384. |
| SMR | P23384. Positions 226-543. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR011096. FTP_domain. IPR005075. Pept_M4_propep_PepSY. IPR023612. Peptidase_M4. IPR001570. Peptidase_M4_C_domain. IPR013856. Peptidase_M4_domain. [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 | NPRE_BACCL | ||||||||
| Accession | Primary (citable) accession number: P23384 | ||||||||
| Entry history |
| ||||||||
| 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