ID   LYG_CASCA               Reviewed;         185 AA.
AC   Q7LZR3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Lysozyme g;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   AltName: Full=Goose-type lysozyme;
OS   Casuarius casuarius (Southern cassowary) (Struthio casuarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Casuariiformes; Casuariidae; Casuarius.
OX   NCBI_TaxID=8787;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RA   Thammasirirak S., Torikata T., Takami K., Murata K., Araki T.;
RL   Submitted (OCT-2000) to the PIR data bank.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Shows preference for N-acetylmuramic acid residues that
CC       are substituted with a peptide moiety. It acts only as a
CC       glycanohydrolase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
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DR   PIR; A59351; A59351.
DR   AlphaFoldDB; Q7LZR3; -.
DR   SMR; Q7LZR3; -.
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   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Pyrrolidone carboxylic acid;
KW   Secreted.
FT   CHAIN           1..185
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193514"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|Ref.1"
FT   DISULFID        4..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..29
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  20426 MW;  0522F8187896F53A CRC64;
     QTGCYGVVNR IDTTGASCET AKPEKLNYCG VAASRKIAEG DLQSMDRYKT LIKKVGQKLC
     VDPAVIAGII SRESHAGKAL KDGWGDNGNG FGLMQVDKRS HTPVGKWNGE RHLTQGTEIL
     ISMIKKIQKK FPRWTKEQQL KGGISAYNAG SGNVRTYERM DIGTTHNDYA NDVVARAQYY
     KQHGY
//