Reviewed,
UniProtKB/Swiss-Prot P51782 (LYSC_TRIVU)
Last modified
June 16, 2009.
Version 55.
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 | Trichosurus vulpecula (Brush-tailed possum) | ||
| Taxonomic identifier | 9337 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Diprotodontia › Phalangeridae › Trichosurus |
Protein attributes
| Sequence length | 147 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 | 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. |
| 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. |
| Mass spectrometry | Molecular mass is 14896 Da from positions 19 - 147. Determined by MALDI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | |||||||||
| Chain | 19 – 147 | 129 | Lysozyme C | PRO_0000018493 | |||||||
Sites | |||||||||||
| Active site | 53 | 1 | By similarity | ||||||||
| Active site | 71 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 24 ↔ 145 | By similarity | |||||||||
| Disulfide bond | 48 ↔ 133 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 99 | By similarity | |||||||||
| Disulfide bond | 95 ↔ 113 | By similarity | |||||||||
Sequences
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References
| [1] | "Lysozyme and alpha-lactalbumin from the milk of a marsupial, the common brush-tailed possum (Trichosurus vulpecula)." Piotte C.P., Marshall C.J., Hubbard M.J., Collet C., Grigor M.R. Biochim. Biophys. Acta 1336:235-242(1997) [PubMed: 9305795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Mammary gland. |
Cross-references
Sequence databases | |
|---|---|
| U40664 Genomic DNA. Translation: AAB97109.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LZ6 based on UniProtKB P00695. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Phylogenomic databases | |
| HOVERGEN | P51782. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 270554. |
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_TRIVU | ||||||||
| Accession | Primary (citable) accession number: P51782 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


