Reviewed,
UniProtKB/Swiss-Prot Q00891 (NPRM_BACME)
Last modified
June 16, 2009.
Version 66.
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 | ||
| Gene names |
| ||
| Organism | Bacillus megaterium | ||
| Taxonomic identifier | 1404 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 562 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: 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 – 24 | 24 | Potential | ||||||
| Propeptide | 25 – 245 | 221 | Activation peptide Potential | PRO_0000028610 | |||||
| Chain | 246 – 562 | 317 | Bacillolysin | PRO_0000028611 | |||||
Sites | |||||||||
| Active site | 389 | 1 | By similarity | ||||||
| Active site | 477 | 1 | Proton donor By similarity | ||||||
| Metal binding | 303 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 305 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 384 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 388 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 392 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 412 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 423 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 423 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 429 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 431 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 431 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 433 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 436 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 436 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 439 | 1 | Calcium 4; via carbonyl oxygen By similarity | ||||||
| Metal binding | 440 | 1 | Calcium 4 By similarity | ||||||
| Metal binding | 446 | 1 | Calcium 4 By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 83 | 1 | S → N in CAA52964. Ref.2 | ||||||
| Sequence conflict | 186 | 1 | A → G in CAA52964. Ref.2 | ||||||
| Sequence conflict | 251 | 1 | T → A in CAA52964. Ref.2 | ||||||
| Sequence conflict | 302 | 1 | A → T in CAA52964. Ref.2 | ||||||
| Sequence conflict | 344 | 1 | R → A in CAA52964. Ref.2 | ||||||
| Sequence conflict | 394 | 1 | L → V in CAA52964. Ref.2 | ||||||
Sequences
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References
| [1] | "Molecular cloning and nucleotide sequence of the gene encoding a calcium-dependent exoproteinase from Bacillus megaterium ATCC 14581." Kuhn S., Fortnagel P. J. Gen. Microbiol. 139:39-47(1993) [PubMed: 8450307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14581 / DSM 32 / NCIB 9376 / NCTC 10342 / JCM 2506. |
| [2] | "Cloning and sequencing of the leu C and npr M genes and a putative spo IV gene from Bacillus megaterium DSM319." Meinhardt F., Busskamp M., Wittchen K.D. Appl. Microbiol. Biotechnol. 41:344-351(1994) [PubMed: 7764969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 319. |
Cross-references
Sequence databases | |
|---|---|
| X61380 Genomic DNA. Translation: CAA43654.1. X75070 Genomic DNA. Translation: CAA52964.1. | |
| PIR | A47710. I40227. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NPC based on UniProtKB P05806. |
| SMR | Q00891. Positions 246-561. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M04.001. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.28. 325. |
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 | NPRM_BACME | ||||||||
| Accession | Primary (citable) accession number: Q00891 | ||||||||
| Entry history |
| ||||||||
| 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


