ID   LYG_EPICO               Reviewed;         194 AA.
AC   Q90X99;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-MAY-2023, entry version 65.
DE   RecName: Full=Lysozyme g;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
OS   Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC   Epinephelini; Epinephelus.
OX   NCBI_TaxID=94232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX   PubMed=12911059; DOI=10.3354/dao055117;
RA   Yin Z.X., He J.G., Deng W.X., Chan S.M.;
RT   "Molecular cloning, expression of orange-spotted grouper goose-type
RT   lysozyme cDNA, and lytic activity of its recombinant protein.";
RL   Dis. Aquat. Organ. 55:117-123(2003).
CC   -!- FUNCTION: Has lytic activity against M.lysodeikticus, V.alginolyticus
CC       from Epinephelus fario, V.vulnificus from culture water, A.hydrophila
CC       from soft-shell turtle, A.hydrophila from goldfish and
CC       V.parahaemolyticus, P.fluorescens and V.fluvialis from culture water.
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   -!- TISSUE SPECIFICITY: Expressed in intestine, liver, spleen, anterior
CC       kidney, posterior kidney, heart, gill, muscle and leukocytes.
CC       {ECO:0000269|PubMed:12911059}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
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DR   EMBL; AF416458; AAL08021.2; -; mRNA.
DR   AlphaFoldDB; Q90X99; -.
DR   SMR; Q90X99; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd01021; GEWL; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR31698:SF8; LYSOZYME G; 1.
DR   PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 1.
DR   Pfam; PF01464; SLT; 1.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase.
FT   CHAIN           1..194
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193518"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   194 AA;  21179 MW;  8A12197359127023 CRC64;
     MGYGNIMNVE TTGASWQTAQ QDKLGYSGVR ASHTMANTDS GRMERYRSKI NSVGAKYGID
     PALIAAIISE ESRAGNVLHD GWGDYDSNRG AYNAWGLMQV DVNPNGGGHT ARGAWDSEEH
     LSQGAEILVY FIGRIRNKFP GWNTEQQLKG GIAAYNMGDG NVHSYDNVDG RTTGGDYSND
     VVARAQWYKT QKGF
//