ID LYS_ESTAC Reviewed; 18 AA. AC P82175; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 03-MAY-2023, entry version 57. DE RecName: Full=Lysozyme; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase; DE Flags: Fragment; OS Estigmene acrea (Salt marsh moth) (Phalaena acrea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea; OC Erebidae; Arctiinae; Estigmene. OX NCBI_TaxID=56594; RN [1] RP PROTEIN SEQUENCE, AND ACTIVITY REGULATION. RC TISSUE=Hemocyte; RX PubMed=9303271; DOI=10.1016/s0145-305x(97)00012-8; RA Wittwer D., Weise C., Goetz P., Wiesner A.; RT "LPS (lipopolysaccharide)-activated immune responses in a hemocyte cell RT line from Estigmene acraea (Lepidoptera)."; RL Dev. Comp. Immunol. 21:323-336(1997). CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in CC tissues and body fluids are associated with the monocyte-macrophage CC system and enhance the activity of immunoagents. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; CC -!- ACTIVITY REGULATION: By lipopolysaccharide (LPS). CC {ECO:0000269|PubMed:9303271}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; KW Glycosidase; Hydrolase. FT CHAIN 1..>18 FT /note="Lysozyme" FT /id="PRO_0000208878" FT NON_TER 18 SQ SEQUENCE 18 AA; 2214 MW; B229D8F5ECDD7F57 CRC64; KYFATRCDLV RELRKXGF //