Q7LZQ1 (LYSC_TRISI)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 42.
History...
Clusters with 
Names and origin
| Protein names | Recommended name: Lysozyme C EC=3.2.1.17 Alternative name(s): Softshell turtle lysozyme C Short name=SSTL 1,4-beta-N-acetylmuramidase C | ||
| Gene names |
| ||
| Organism | Trionyx sinensis (Chinese softshell turtle) (Pelodiscus sinensis) | ||
| Taxonomic identifier | 13735 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines › Cryptodira › Trionychoidea › Trionychidae › Pelodiscus |
Protein attributes
| Sequence length | 131 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. Has strong bacteriolytic activity against M.luteus and V.cholerae, weak bacteriolytic activity against P.aeruginosa and no activity against A.hydrophila. 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. Ref.1 |
| Subunit structure | Monomer By similarity. |
| 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. |
| Biophysicochemical properties | pH dependence: Optimum pH is 6.0. Ref.1 Temperature dependence: Optimum temperature is 40 degrees Celsius. Activity rapidly decreases within 30 minutes of incubation at 90 degrees Celsius. |
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 – 131 | 131 | Lysozyme C | PRO_0000208876 | ||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||
| Active site | 36 | 1 | By similarity | |||||||||||||||||||||||||||||||
| Active site | 54 | 1 | By similarity | |||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||
| Disulfide bond | 7 ↔ 129 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 31 ↔ 117 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 66 ↔ 82 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 78 ↔ 96 | |||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Helix | 6 – 15 | 10 | ||||||||||||||||||||||||||||||||
| Helix | 21 – 23 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 26 – 37 | 12 | ||||||||||||||||||||||||||||||||
| Beta strand | 44 – 47 | 4 | ||||||||||||||||||||||||||||||||
| Turn | 48 – 51 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 52 – 55 | 4 | ||||||||||||||||||||||||||||||||
| Turn | 56 – 59 | 4 | ||||||||||||||||||||||||||||||||
| Turn | 62 – 65 | 4 | ||||||||||||||||||||||||||||||||
| Helix | 82 – 86 | 5 | ||||||||||||||||||||||||||||||||
| Helix | 91 – 102 | 12 | ||||||||||||||||||||||||||||||||
| Helix | 106 – 109 | 4 | ||||||||||||||||||||||||||||||||
| Helix | 111 – 116 | 6 | ||||||||||||||||||||||||||||||||
| Turn | 117 – 119 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 123 – 125 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 126 – 128 | 3 | ||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Purification, characterization and comparison of reptile lysozymes." Thammasirirak S., Ponkham P., Preecharram S., Khanchanuan R., Phonyothee P., Daduang S., Srisomsap C., Araki T., Svasti J. Comp. Biochem. Physiol. 143:209-217(2006) [PubMed: 16549391] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Egg white. |
| [2] | "The 1.9 A X-ray structure of egg-white lysozyme from Taiwanese soft-shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences from the standard chicken-type lysozyme." Siritapetawee J., Thammasirirak S., Robinson R.C., Yuvaniyama J. J. Biochem. 145:193-198(2009) [PubMed: 19029145] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). Tissue: Egg white. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | JC5493. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q7LZQ1. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH22. Glycoside Hydrolase Family 22. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | HBG052297. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.17. 39406. | ||||||||||||
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 | LYSC_TRISI | ||||||||
| Accession | Primary (citable) accession number: Q7LZQ1 | ||||||||
| 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 |
