Reviewed,
UniProtKB/Swiss-Prot Q7M135 (LYSC_LYSEN)
Last modified
June 16, 2009.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Lysyl endopeptidase EC=3.4.21.50 Alternative name(s): Lys-C |
| Organism | Lysobacter enzymogenes |
| Taxonomic identifier | 69 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter |
Protein attributes
| Sequence length | 269 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Highly specific endopeptidase that hydrolyzes lysyl bonds including the Lys-Pro bond. |
| Catalytic activity | Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. |
| Subcellular location | |
| Biotechnological use | Sold under the name 'Endoproteinase Lys-C' by Roche. |
| Sequence similarities | Belongs to the peptidase S1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type peptidase activity Inferred 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 – 269 | 269 | Lysyl endopeptidase | PRO_0000093854 | |||||||
Sites | |||||||||||
| Active site | 57 | 1 | Charge relay system By similarity | ||||||||
| Active site | 113 | 1 | Charge relay system By similarity | ||||||||
| Active site | 194 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 6 ↔ 216 | By similarity | |||||||||
| Disulfide bond | 12 ↔ 80 | By similarity | |||||||||
| Disulfide bond | 36 ↔ 58 | By similarity | |||||||||
Sequences
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References
| [1] | Mentele R., Eckerskorn C., Kellermann J., Strupat K., Hagmann J., Lottspeich F. Submitted (JUN-1997) to the PIR data bank Cited for: PROTEIN SEQUENCE. |
Cross-references
Entry information
| Entry name | LYSC_LYSEN | ||||||||
| Accession | Primary (citable) accession number: Q7M135 | ||||||||
| 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 |

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