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P82175 (LYS_ESTAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismEstigmene acrea (Salt marsh moth)
Taxonomic identifier56594 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaArctiidaeEstigmene

Protein attributes

Sequence length18 AA.
Sequence statusFragment.
Protein existenceEvidence 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 By similarity.

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.

Enzyme regulation

By lipopolysaccharide (LPS). Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   Technical termDirect 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

   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 – ›18›18Lysozyme
PRO_0000208878

Experimental info

Non-terminal residue181

Sequences

Sequence LengthMass (Da)Tools
P82175 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B229D8F5ECDD7F57

FASTA182,214
        10 
KYFATRCDLV RELRKXGF 

« Hide

References

[1]"LPS (lipopolysaccharide)-activated immune responses in a hemocyte cell line from Estigmene acraea (Lepidoptera)."
Wittwer D., Weise C., Goetz P., Wiesner A.
Dev. Comp. Immunol. 21:323-336(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, ENZYME REGULATION.
Tissue: Hemocyte.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameLYS_ESTAC
AccessionPrimary (citable) accession number: P82175
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 46 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