P00719 (LYG_STRCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 67.
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 g EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase Goose-type lysozyme |
| Organism | Struthio camelus (Ostrich) |
| Taxonomic identifier | 8801 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Struthioniformes › Struthionidae › Struthio![]() |
Protein attributes
| Sequence length | 204 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Has bacteriolytic activity against M.luteus. Ref.1 |
| 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. |
| Subcellular location | |
| Miscellaneous | Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase. |
| Sequence similarities | Belongs to the glycosyl hydrolase 23 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| 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 peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.2 Ref.3 | ||||||||
| Chain | 20 – 204 | 185 | Lysozyme g | PRO_0000193516 | |||||||
Sites | |||||||||||
| Active site | 92 | 1 | By similarity | ||||||||
| Active site | 105 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 23 ↔ 79 | By similarity | |||||||||
| Disulfide bond | 37 ↔ 48 | By similarity | |||||||||
Sequences
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References
| [1] | "Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white." Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T. Gene 492:244-249(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Tissue: Muscle. |
| [2] | "Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme." Schoentgen F., Jolles J., Jolles P. Eur. J. Biochem. 123:489-497(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-204. Tissue: Egg white. |
| [3] | "The ostrich (Struthio camelus) egg-white lysozyme." Jolles J., Perin J.-P., Jolles P. Mol. Cell. Biochem. 17:39-44(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-53. Tissue: Egg white. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB469329 Genomic DNA. Translation: BAL03620.1. |
| PIR | LZOSG. A00874. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH23. Glycoside Hydrolase Family 23. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG006299. |
Family and domain databases | |
| InterPro | IPR002152. Glyco_hydro_23. IPR023346. Lysozyme-like_dom. IPR008258. Lytic_TGlycosylase-like_cat. [Graphical view] |
| Pfam | PF01464. SLT. 1 hit. [Graphical view] |
| PIRSF | PIRSF001065. Lysozyme_g. 1 hit. |
| PRINTS | PR00749. LYSOZYMEG. |
| SUPFAM | SSF53955. SSF53955. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LYG_STRCA | ||||||||
| Accession | Primary (citable) accession number: P00719 Secondary accession number(s): G3XDE1 | ||||||||
| 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
