ID   LYG_STRCA               Reviewed;         204 AA.
AC   P00719; G3XDE1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   25-MAY-2022, entry version 88.
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;
DE   Flags: Precursor;
OS   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   TISSUE=Muscle;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-204.
RC   TISSUE=Egg white;
RX   PubMed=7075596; DOI=10.1111/j.1432-1033.1982.tb06557.x;
RA   Schoentgen F., Jolles J., Jolles P.;
RT   "Complete amino acid sequence of ostrich (Struthio camelus) egg-white
RT   lysozyme, a goose-type lysozyme.";
RL   Eur. J. Biochem. 123:489-497(1982).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-53.
RC   TISSUE=Egg white;
RX   PubMed=904618; DOI=10.1007/bf01732553;
RA   Jolles J., Perin J.-P., Jolles P.;
RT   "The ostrich (Struthio camelus) egg-white lysozyme.";
RL   Mol. Cell. Biochem. 17:39-44(1977).
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;
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
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DR   EMBL; AB469329; BAL03620.1; -; Genomic_DNA.
DR   PIR; A00874; LZOSG.
DR   PDB; 3WYH; X-ray; 1.77 A; A/B=20-204.
DR   PDBsum; 3WYH; -.
DR   AlphaFoldDB; P00719; -.
DR   BMRB; P00719; -.
DR   SMR; P00719; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 1.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:7075596,
FT                   ECO:0000269|PubMed:904618"
FT   CHAIN           20..204
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193516"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   DISULFID        23..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..48
FT                   /evidence="ECO:0000250"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           50..65
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           82..93
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            94..98
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            105..108
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           129..149
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           155..168
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            177..182
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   HELIX           188..199
FT                   /evidence="ECO:0007829|PDB:3WYH"
FT   TURN            200..203
FT                   /evidence="ECO:0007829|PDB:3WYH"
SQ   SEQUENCE   204 AA;  22514 MW;  DD9F02D65DA21A65 CRC64;
     MHLMLVLLGL AALLGTSQSR TGCYGDVNRV DTTGASCKSA KPEKLNYCGV AASRKIAERD
     LQSMDRYKAL IKKVGQKLCV DPAVIAGIIS RESHAGKALR NGWGDNGNGF GLMQVDRRSH
     KPVGEWNGER HLMQGTEILI SMIKAIQKKF PRWTKEQQLK GGISAYNAGP GNVRSYERMD
     IGTTHDDYAN DVVARAQYYK QHGY