Reviewed,
UniProtKB/Swiss-Prot P84492 (LYSC_CHEMY)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme C EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C | ||
| Gene names |
| ||
| Organism | Chelonia mydas (Green sea-turtle) (Chelonia agassizi) | ||
| Taxonomic identifier | 8469 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines › Cryptodira › Chelonioidea › Cheloniidae › Chelonia |
Protein attributes
| Sequence length | 130 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents By similarity. |
| Catalytic activity | Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
| Subunit structure | Monomer By similarity. |
| Miscellaneous | Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | lysozyme activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 130 | 130 | Lysozyme C | PRO_0000247815 | |||||||
Sites | |||||||||||
| Active site | 35 | 1 | By similarity | ||||||||
| Active site | 53 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 6 ↔ 128 | By similarity | |||||||||
| Disulfide bond | 30 ↔ 116 | By similarity | |||||||||
| Disulfide bond | 65 ↔ 81 | By similarity | |||||||||
| Disulfide bond | 77 ↔ 95 | By similarity | |||||||||
Sequences
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References
| [1] | Araki T., Chijiiwa Y., Okabayashi K., Kawase M., Kamesaki M., Torikata T. Submitted (MAR-2003) to the PIR data bank Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | JC7918. |
3D structure databases | |
| SMR | P84492. Positions 1-130. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P84492. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 293409. |
Family and domain databases | |
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. [Graphical view] |
| Pfam | PF00062. Lys. 1 hit. [Graphical view] |
| PRINTS | PR00137. LYSOZYME. PR00135. LYZLACT. |
| SMART | SM00263. LYZ1. 1 hit. [Graphical view] |
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYSC_CHEMY | ||||||||
| Accession | Primary (citable) accession number: P84492 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


