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Protein

Lysozyme

Gene
N/A
Organism
Estigmene acrea (Salt marsh moth) (Phalaena acrea)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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 regulationi

By lipopolysaccharide (LPS).1 Publication

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiEstigmene acrea (Salt marsh moth) (Phalaena acrea)
Taxonomic identifieri56594 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaErebidaeArctiinaeEstigmene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›18›18LysozymePRO_0000208878Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.Curated

Sequencei

Sequence statusi: Fragment.

P82175-1 [UniParc]FASTAAdd to basket

« Hide

        10 
KYFATRCDLV RELRKXGF
Length:18
Mass (Da):2,214
Last modified:May 1, 2000 - v1
Checksum:iB229D8F5ECDD7F57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei18 – 181

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ENZYME REGULATION.
    Tissue: Hemocyte.

Entry informationi

Entry nameiLYS_ESTAC
AccessioniPrimary (citable) accession number: P82175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.