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   02-JUN-2021, entry version 56.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; 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