Reviewed,
UniProtKB/Swiss-Prot Q1XG90 (LYS2_CRAVI)
Last modified
January 19, 2010.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme 2 EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase 2 cv-lysozyme 2 | ||
| Gene names |
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| Organism | Crassostrea virginica (Eastern oyster) | ||
| Taxonomic identifier | 6565 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Mollusca › Bivalvia › Pteriomorphia › Ostreoida › Ostreoidea › Ostreidae › Crassostrea |
Protein attributes
| Sequence length | 135 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 | The main role of this lysozyme is in digestion. Has antibacterial activity against the Gram-positive bacterium P.cerevisiae and the Gram-negative bacteria E.coli and V.vulnificus. Shows some chitinase activity but no isopeptidase activity. 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 |
| Enzyme regulation | Activity decreased by 80% by addition of 0.01 M calcium, zinc or magnesium. Activity only decreased by 17% by addition of ammonium, and by 2% by addition of sodium. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed in the epithelia of the basophil cells in the digestive tubules, but not in the epithelial cells lining the digestive ducts and stomach. Expressed at a much lower level in the style sac-midgut tissues. No expression detected in mantle, gills, labial palps or hemocytes. Ref.1 |
| Sequence similarities | Belongs to the lysozyme type I family. |
| Biophysicochemical properties | pH dependence: Retains more than 90% of its maximum activity between pH 5.4 and 6.4 in the ionic strength range of I=0.005-0.01. In buffers of I=0.005 more than 75% of maximum activity is retained between pH 5.3 and 7.5. In buffers of I=0.02 more than 75% of maximum activity is retained between pH 5.3 and 6.5. Ref.1 Temperature dependence: Optimum temperature is 55 degrees Celsius. No decrease in activity was detected after incubation at 30 degrees Celsius for 30 minutes. No activity could be detected after incubation at 90 degrees Celsius for 30 minutes or 100 degrees Celsius for 10 minutes. Ref.1 |
| Mass spectrometry | Molecular mass is 12984.6 Da from positions 19 - 135. Determined by MALDI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cytolysis Ref.1 Inferred from direct assay. Source: UniProtKB defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | lysozyme activity Ref.1 Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes." Xue Q.-G., Itoh N., Schey K.L., Li Y.-L., Cooper R.K., La Peyre J.F. Cell. Mol. Life Sci. 64:82-95(2007) [PubMed: 17160350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-105 AND 116-135, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Digestive gland. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB252064 mRNA. Translation: BAE93114.1. |
3D structure databases | |
| SMR | Q1XG90. Positions 18-131. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 141032. |
Family and domain databases | |
| InterPro | IPR008597. Destabilase. [Graphical view] |
| PANTHER | PTHR11195. Destabilase. 1 hit. |
| Pfam | PF05497. Destabilase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYS2_CRAVI | ||||||||
| Accession | Primary (citable) accession number: Q1XG90 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


