Reviewed,
UniProtKB/Swiss-Prot P00700 (LYSC_COLVI)
Last modified
June 16, 2009.
Version 72.
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 EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C | ||
| Gene names |
| ||
| Organism | Colinus virginianus (Bobwhite quail) (Common bobwhite) | ||
| Taxonomic identifier | 9014 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Odontophoridae › Colinus |
Protein attributes
| Sequence length | 129 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 |
| 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 – 129 | 129 | Lysozyme C | PRO_0000208863 | ||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 35 | 1 | ||||||||||||||||||||||||||||||
| Active site | 52 | 1 | ||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Disulfide bond | 6 ↔ 127 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 30 ↔ 115 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 64 ↔ 80 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 76 ↔ 94 | Ref.1 | ||||||||||||||||||||||||||||||
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 – 62 | 3 | ||||||||||||||||||||||||||||||
| Helix | 80 – 84 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 85 – 87 | 3 | ||||||||||||||||||||||||||||||
| Helix | 89 – 101 | 13 | ||||||||||||||||||||||||||||||
| Helix | 104 – 107 | 4 | ||||||||||||||||||||||||||||||
| Helix | 109 – 114 | 6 | ||||||||||||||||||||||||||||||
| Turn | 115 – 117 | 3 | ||||||||||||||||||||||||||||||
| Helix | 120 – 124 | 5 | ||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Amino acid sequence studies on bobwhite quail egg white lysozyme." Prager E.M., Arnheim N., Mross G.A., Wilson A.C. J. Biol. Chem. 247:2905-2916(1972) [PubMed: 4112539] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white. |
| [2] | "Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment." Chacko S., Silverton E.W., Smith-Gill S.J., Davies D.R., Schick K.A., Xavier K.A., Willson R.C., Jeffrey P.D., Chang C.Y., Sieker L.C., Sheriff S. Proteins 26:55-65(1996) [PubMed: 8880929] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | LZQJEB. A00855. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| CAZy | GH22. Glycoside Hydrolase Family 22. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOVERGEN | P00700. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BRENDA | 3.2.1.17. 273314. | ||||||||||||||||||||||||
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... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| BindingDB | P00700. | ||||||||||||||||||||||||
Entry information
| Entry name | LYSC_COLVI | ||||||||
| Accession | Primary (citable) accession number: P00700 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
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


