P11375 (LYSC_EQUAS) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 76.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Equus asinus (Donkey) | ||
| Taxonomic identifier | 9793 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › ![]() |
Protein attributes
| Sequence length | 129 AA. |
| Sequence status | Complete. |
| 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. |
| Cofactor | Binds 1 calcium ion per subunit Probable. |
| 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 | |
|---|---|
| Ligand | Calcium Metal-binding |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase Milk protein |
| 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 metal 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 129 | 129 | Lysozyme C | PRO_0000208849 | |||||||
Regions | |||||||||||
| Calcium binding | 81 – 92 | 12 | By similarity | ||||||||
Sites | |||||||||||
| Active site | 35 | 1 | By similarity | ||||||||
| Active site | 53 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 6 ↔ 127 | By similarity | |||||||||
| Disulfide bond | 30 ↔ 115 | By similarity | |||||||||
| Disulfide bond | 65 ↔ 80 | By similarity | |||||||||
| Disulfide bond | 76 ↔ 94 | By similarity | |||||||||
Sequences
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References
| [1] | "The primary structure of donkey (Equus asinus) lysozyme contains the Ca(II) binding site of alpha-lactalbumin." Godovac-Zimmermann J., Conti A., Napolitano L. Biol. Chem. Hoppe-Seyler 369:1109-1115(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S01661. |
3D structure databases | |
| ProteinModelPortal | P11375. |
| SMR | P11375. Positions 1-129. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG052297. |
Family and domain databases | |
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. IPR023346. Lysozyme-like_dom. [Graphical view] |
| Pfam | PF00062. Lys. 1 hit. [Graphical view] |
| PRINTS | PR00137. LYSOZYME. PR00135. LYZLACT. |
| SMART | SM00263. LYZ1. 1 hit. [Graphical view] |
| SUPFAM | SSF53955. SSF53955. 1 hit. |
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYSC_EQUAS | ||||||||
| Accession | Primary (citable) accession number: P11375 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
