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Reviewed, UniProtKB/Swiss-Prot P83673 (LYS1_CRAVI)

Last modified January 19, 2010. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysozyme 1
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase 1
    cv-lysozyme 1
Gene names
Name: lysoz1
Synonyms: lysoz
OrganismCrassostrea virginica (Eastern oyster)
Taxonomic identifier6565 [NCBI]
Taxonomic lineageEukaryotaMetazoaMolluscaBivalviaPteriomorphiaOstreoidaOstreoideaOstreidaeCrassostrea

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has antibacterial activity against the Gram-positive bacteria L.garvieae, M.luteus and Enterococcus sp., and the Gram-negative bacteria E.coli and V.vulnificus. Weak antibacterial activity against the Gram-negative bacterium A.hydrophila. No antibacterial activity detected against the Gram-positive bacterium S.iniae or against the Gram-negative bacterium E.ictaluri. Shows some chitinase activity but no isopeptidase activity. Ref.2 Ref.3

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.2

Subcellular location

Secreted Ref.2.

Tissue specificity

Hemolymph, labial palps, non-vesiculated cells of mantle connective tissue, cells of interlamellar junctions and epithelia surrounding the water tubes of the gills. Ref.3

Sequence similarities

Belongs to the lysozyme type I family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6.0. Ref.2

Temperature dependence:

Activity increases as temperature increases from 0 to 45 degrees Celsius and decreases markedly at temperatures greater than 55 degrees Celsius. Ref.2

Mass spectrometry

Molecular mass is 17771 Da from positions 21 - 184. Determined by MALDI. Ref.2

Molecular mass is 17861 Da from positions 21 - 184. Determined by MALDI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.2
Chain21 – 184164Lysozyme 1 Ref.2
PRO_0000084532

Experimental info

Sequence conflict431Y → T AA sequence Ref.2
Sequence conflict751Q → K AA sequence Ref.2
Sequence conflict1221Q → K AA sequence Ref.2
Sequence conflict1281L → I AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P83673-1 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: 239FC8C991546523

FASTA18419,986
        10         20         30         40         50         60 
MNGLILFCAV VFATAVCTYG SDAPCLRAGG RCQHDSITCS GRYRTGLCSG GVRRRCCVPS 

        70         80         90        100        110        120 
SSNSGSFSTG MVSQQCLRCI CNVESGCRPI GCHWDVNSDS CGYFQIKRAY WIDCGSPGGD 

       130        140        150        160        170        180 
WQTCANNLAC SSRCVQAYMA RYHRRSGCSN SCESFARIHN GGPRGCRNSN TEGYWRRVQA 


QGCN 

« Hide

References

[1]"Lysozyme gene in the eastern oyster, Crassostrea virginica."
Itoh N., Xue Q.-G., Cooper R.K., La Peyre J.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and characterization of lysozyme from plasma of the eastern oyster (Crassostrea virginica)."
Xue Q.-G., Schey K.L., Volety A.K., Chu F.-L., La Peyre J.F.
Comp. Biochem. Physiol. 139B:11-25(2004) [PubMed: 15364284] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-85; 109-141; 146-157 AND 168-176, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
Tissue: Hemolymph.
[3]"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: FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB206328 mRNA. Translation: BAE47520.1.

3D structure databases

SMRP83673. Positions 67-179.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Enzyme and pathway databases

BRENDA3.2.1.17. 141032.

Family and domain databases

InterProIPR008597. Destabilase.
[Graphical view]
PANTHERPTHR11195. Destabilase. 1 hit.
PfamPF05497. Destabilase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS1_CRAVI
AccessionPrimary (citable) accession number: P83673
Secondary accession number(s): Q33DU2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 20, 2007
Last modified: January 19, 2010
This is version 34 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents