Reviewed,
UniProtKB/Swiss-Prot P37155 (LYSC_FELCA)
Last modified
July 28, 2009.
Version 51.
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 | Felis catus (Cat) (Felis silvestris catus) | ||
| Taxonomic identifier | 9685 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis |
Protein attributes
| Sequence length | 20 AA. |
| Sequence status | Fragment. |
| 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. |
| 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. |
| 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 Milk protein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | lysozyme activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Feline whey proteins: identification, isolation and initial characterization of alpha-lactalbumin, beta-lactoglobulin and lysozyme." Halliday J.A., Bell K., McKenzie H.A., Shaw D.C. Comp. Biochem. Physiol. 95B:773-779(1990) [PubMed: 2344734] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Milk. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A60525. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EL1 based on UniProtKB P81708. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Phylogenomic databases | |
| HOVERGEN | P37155. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 273949. |
Family and domain databases | |
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. [Graphical view] |
| Pfam | PF00062. Lys. 1 hit. [Graphical view] |
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYSC_FELCA | ||||||||
| Accession | Primary (citable) accession number: P37155 | ||||||||
| Entry history |
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| 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


