Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P82175

- LYS_ESTAC

UniProt

P82175 - LYS_ESTAC

Protein

Lysozyme

Gene
N/A
Organism
Estigmene acrea (Salt marsh moth) (Phalaena acrea)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. 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

    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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaArctiidaeEstigmene

    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

    KYFATRCDLV RELRKXGF                                      18
    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

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    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(1997) [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: October 1, 2014
    This is version 48 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