ID   LYG_DRONO               Reviewed;         204 AA.
AC   G3XDD8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Lysozyme G {ECO:0000312|EMBL:BAL03618.1};
DE            EC=3.2.1.17 {ECO:0000250|UniProtKB:Q90X99};
DE   AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000250|UniProtKB:Q90X99};
DE   Flags: Precursor;
OS   Dromaius novaehollandiae (Emu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX   NCBI_TaxID=8790;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAL03618.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary {ECO:0000312|EMBL:BAL03619.1}, and Oviduct
RC   {ECO:0000312|EMBL:BAL03618.1};
RX   PubMed=22044478; DOI=10.1016/j.gene.2011.10.021;
RA   Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.;
RT   "Molecular characterization of goose- and chicken-type lysozymes in emu
RT   (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in
RT   emu egg white.";
RL   Gene 492:244-249(2012).
CC   -!- FUNCTION: Has bacteriolytic activity against M.luteus.
CC       {ECO:0000269|PubMed:22044478}.
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; Evidence={ECO:0000250|UniProtKB:Q90X99};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q90X99}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000255}.
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DR   EMBL; AB451700; BAL03618.1; -; mRNA.
DR   EMBL; AB462632; BAL03619.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XDD8; -.
DR   SMR; G3XDD8; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   Ensembl; ENSDNVT00000031733.1; ENSDNVP00000026237.1; ENSDNVG00000018259.1.
DR   Ensembl; ENSDNVT00000031735.1; ENSDNVP00000026239.1; ENSDNVG00000018259.1.
DR   OrthoDB; 2964133at2759; -.
DR   Proteomes; UP000694423; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..204
FT                   /note="Lysozyme G"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000795990"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250|UniProtKB:P00718"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250|UniProtKB:P00718"
FT   DISULFID        23..79
FT                   /evidence="ECO:0000250|UniProtKB:P00718"
FT   DISULFID        37..48
FT                   /evidence="ECO:0000250|UniProtKB:P00718"
SQ   SEQUENCE   204 AA;  22493 MW;  4061327BB92C820C CRC64;
     MHLMLVLLGL AALLGTSQSQ TGCYGVVNRI DTTGASCETA KPEKLNYCGV AASRMIAERD
     LRSMDRYKTL IKKVGQKLCV DPAVIAGIIS RESHAGKALK NGWGDNGNGF GLMQVDKRSH
     TPVGEWNGER HLTQGTEILI SMIKKIQKKF PRWTKEQQLK GGISAYNAGS GNVRSYERMD
     IGTTHNDYAN DVVARAQYYK QHGY
//