P00704 (LYSC_NUMME) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
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 | Numida meleagris (Helmeted guineafowl) | ||
| Taxonomic identifier | 8996 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Numididae › Numida![]() |
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. |
| Subunit structure | Monomer. |
| Subcellular location | |
| 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 | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| 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 |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 129 | 129 | Lysozyme C | PRO_0000208868 | ||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 35 | 1 | ||||||||||||||||||||||||||||||
| Active site | 52 | 1 | ||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Disulfide bond | 6 ↔ 127 | |||||||||||||||||||||||||||||||
| 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 | 37 – 39 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 43 – 45 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 51 – 53 | 3 | ||||||||||||||||||||||||||||||
| Turn | 54 – 57 | 4 | ||||||||||||||||||||||||||||||
| Turn | 60 – 63 | 4 | ||||||||||||||||||||||||||||||
| Helix | 80 – 84 | 5 | ||||||||||||||||||||||||||||||
| Helix | 89 – 101 | 13 | ||||||||||||||||||||||||||||||
| Helix | 104 – 107 | 4 | ||||||||||||||||||||||||||||||
| Helix | 109 – 114 | 6 | ||||||||||||||||||||||||||||||
| Turn | 115 – 117 | 3 | ||||||||||||||||||||||||||||||
| Helix | 121 – 124 | 4 | ||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Amino acid sequence of guinea-hen egg-white lysozyme." Jolles J., van Leemputten E., Mouton A., Jolles P. Biochim. Biophys. Acta 257:497-510(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white. |
| [2] | "1H-NMR study on the structure of lysozyme from guinea hen egg white." Fukamizo T., Ikeda Y., Torikata T., Araki T., Kuramoto M., Goto S. J. Biochem. 110:997-1003(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR. |
| [3] | "Crystal structures of pheasant and guinea fowl egg-white lysozymes." Lescar J., Souchon H., Alzari P.M. Protein Sci. 3:788-798(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | LZUH. A00859. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P00704. | ||||||||||||||||||
| SMR | P00704. Positions 1-129. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| CAZy | GH22. Glycoside Hydrolase Family 22. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P00704. | ||||||||||||||||||
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... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P00704. | ||||||||||||||||||
Entry information
| Entry name | LYSC_NUMME | ||||||||
| Accession | Primary (citable) accession number: P00704 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
