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Q1XG90 (LYS2_CRAVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme 2

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase 2
cv-lysozyme 2
Gene names
Name:lysoz2
OrganismCrassostrea virginica (Eastern oyster)
Taxonomic identifier6565 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaOstreoidaOstreoideaOstreidaeCrassostrea

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secreted.

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 componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from direct assay Ref.1. Source: UniProtKB

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 135117Lysozyme 2 Ref.1
PRO_0000280510

Sequences

Sequence LengthMass (Da)Tools
Q1XG90 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 20465553F0D0D1BB

FASTA13514,950
        10         20         30         40         50         60 
MNFLILFCVV ASASVVYSSI SDQCLRCICE VESGCRAIGC HWDVYSNSCG YFQIKQGYWT 

        70         80         90        100        110        120 
DCGSPGHSME SCADNYNCAS GCVRSYMDHY IKYNGCADTC ESYARMHNGG PNGCKSSHHH 

       130 
ATDNYWRLVQ AKGCS 

« Hide

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] [Europe PMC] [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

ProteinModelPortalQ1XG90.
SMRQ1XG90. Positions 18-131.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008597. Destabilase.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PANTHERPTHR11195. PTHR11195. 1 hit.
PfamPF05497. Destabilase. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLYS2_CRAVI
AccessionPrimary (citable) accession number: Q1XG90
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 2, 2006
Last modified: October 3, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries