Reviewed,
UniProtKB/Swiss-Prot P68734 (NPRE_BACPU)
Last modified
June 16, 2009.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bacillolysin EC=3.4.24.28 Alternative name(s): Neutral protease MCP 76 | ||
| Gene names |
| ||
| Organism | Bacillus pumilus (Bacillus mesentericus) | ||
| Taxonomic identifier | 1408 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 300 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 Potential. Binds 1 zinc ion per subunit Potential. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase M4 family. |
| biophysicochemical properties | Temperature dependence: Thermolabile. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Ligand | Calcium Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 300 | 300 | Bacillolysin | PRO_0000078173 | |||||
Sites | |||||||||
| Active site | 144 | 1 | By similarity | ||||||
| Active site | 228 | 1 | Proton donor By similarity | ||||||
| Metal binding | 139 | 1 | Calcium 1 Potential | ||||||
| Metal binding | 143 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 147 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 167 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 178 | 1 | Calcium 1 Potential | ||||||
| Metal binding | 178 | 1 | Calcium 2 Potential | ||||||
| Metal binding | 181 | 1 | Calcium 1 Potential | ||||||
| Metal binding | 181 | 1 | Calcium 2 Potential | ||||||
| Metal binding | 183 | 1 | Calcium 1; via carbonyl oxygen Potential | ||||||
| Metal binding | 186 | 1 | Calcium 1 Potential | ||||||
| Metal binding | 186 | 1 | Calcium 2 Potential | ||||||
Sequences
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References
| [1] | "Primary structure of a zinc protease from Bacillus mesentericus strain 76." Stoeva S., Kleinschmidt T., Mesrob B., Braunitzer G. Biochemistry 29:527-534(1990) [PubMed: 2302386] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: 76. |
Cross-references
3D structure databases | |
|---|---|
| HSSP | HSSP built from PDB template 1BQB based on UniProtKB P81177. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M04.014. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.28. 1189. |
Family and domain databases | |
| InterPro | IPR006025. Pept_M_Zn_BS. IPR013856. Peptidase_M4. IPR001570. Peptidase_M4_C. [Graphical view] |
| Gene3D | G3DSA:3.10.170.10. Peptidase_M4. 1 hit. G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit. |
| Pfam | 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_BACPU | ||||||||
| Accession | Primary (citable) accession number: P68734 Secondary accession number(s): P06142, P25268 | ||||||||
| 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


