Reviewed,
UniProtKB/Swiss-Prot P37156 (LYSC1_TACAC)
Last modified
June 16, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme C I EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C |
| Organism | Tachyglossus aculeatus aculeatus (Australian echidna) |
| Taxonomic identifier | 49271 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Monotremata › Tachyglossidae › Tachyglossus |
Protein attributes
| Sequence length | 125 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. |
| 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 |
| PTM | Disulfide bond |
| Technical term | 3D-structure 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 – 125 | 125 | Lysozyme C I | PRO_0000208857 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 35 | 1 | ||||||||||||||||||||||||||||
| Active site | 52 | 1 | ||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 9 ↔ 125 | |||||||||||||||||||||||||||||
| Disulfide bond | 30 ↔ 115 | |||||||||||||||||||||||||||||
| Disulfide bond | 64 ↔ 80 | |||||||||||||||||||||||||||||
| Disulfide bond | 76 ↔ 94 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 5 – 14 | 10 | ||||||||||||||||||||||||||||
| Helix | 25 – 36 | 12 | ||||||||||||||||||||||||||||
| Beta strand | 43 – 45 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 51 – 53 | 3 | ||||||||||||||||||||||||||||
| Turn | 54 – 57 | 4 | ||||||||||||||||||||||||||||
| Turn | 60 – 63 | 4 | ||||||||||||||||||||||||||||
| Helix | 80 – 83 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 84 – 86 | 3 | ||||||||||||||||||||||||||||
| Helix | 89 – 102 | 14 | ||||||||||||||||||||||||||||
| Helix | 109 – 114 | 6 | ||||||||||||||||||||||||||||
| Turn | 115 – 117 | 3 | ||||||||||||||||||||||||||||
| Helix | 121 – 123 | 3 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The isolation and amino acid sequences of echidna (Tachyglossus aculeatus) milk lysozyme I and II." Teahan C.G., McKenzie H.A., Shaw D.C., Griffiths M. Biochem. Int. 24:85-95(1991) [PubMed: 1768265] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Milk. |
| [2] | "Structure of the calcium-binding Echidna milk lysozyme at 1.9-A resolution." Guss J.M., Messer M., Costello M., Hardy K., Kumar V. Acta Crystallogr. D 53:355-363(1997) [PubMed: 15299900] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| [3] | Erratum Guss J.M., Messer M., Costello M., Hardy K., Kumar V. Acta Crystallogr. D 53:805-805(1997) |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A45660. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH22. Glycoside Hydrolase Family 22. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P37156. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.17. 306500. | ||||||||||||
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 | LYSC1_TACAC | ||||||||
| Accession | Primary (citable) accession number: P37156 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


