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P86383 (LYS_MERLU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismMeretrix lusoria (Hard clam) (Common Orient clam)
Taxonomic identifier74491 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaVeneroidaVeneroideaVeneridaeMeretrix

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has antibacterial activity By similarity. UniProtKB P83673

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. UniProtKB P83673

Subcellular location

Secreted By similarity UniProtKB P83673.

Sequence similarities

Belongs to the lysozyme type I family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   Molecular functionAntibiotic
Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

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 electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Lysozyme
PRO_0000389530

Natural variations

Natural variant51I → T in isozyme B. Ref.1

Secondary structure

........................ 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P86383 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: 92366099E8AD7881

FASTA12213,377
        10         20         30         40         50         60 
FAGGIVSQRC LSCICKMESG CRNVGCKMDM GSLSCGYFQI KEAYWIDCGR PGSSWKSCAA 

        70         80         90        100        110        120 
SSYCASLCVQ NYMKRYAKWA GCPLRCEGFA REHNGGPRGC KKGSTIGYWN RLQKISGCHG 


VQ 

« Hide

References

[1]"The complete amino acid sequence of invertebrate lysozyme from common orient clam."
Araki T., Kuwano Y.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE (ISOZYMES A AND B).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AB6X-ray1.78A1-122[»]
3AYQX-ray1.77A1-122[»]
ProteinModelPortalP86383.
ModBaseSearch...
MobiDBSearch...

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 nameLYS_MERLU
AccessionPrimary (citable) accession number: P86383
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: October 16, 2013
This is version 11 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries