ID   LYG_CYGAT               Reviewed;         185 AA.
AC   P00717;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 98.
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   Cygnus atratus (Black swan) (Anas atrata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anserinae; Cygnus.
OX   NCBI_TaxID=8868;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Egg white;
RX   PubMed=7378374; DOI=10.1021/bi00550a013;
RA   Simpson R.J., Begg G.S., Dorow D.S., Morgan F.J.;
RT   "Complete amino acid sequence of the goose-type lysozyme from the egg white
RT   of the black swan.";
RL   Biochemistry 19:1814-1819(1980).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-68 AND 95-111.
RX   PubMed=2302197; DOI=10.1016/0006-291x(90)91922-f;
RA   Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.;
RT   "Internal amino acid sequencing of proteins by in situ cyanogen bromide
RT   cleavage in polyacrylamide gels.";
RL   Biochem. Biophys. Res. Commun. 166:139-145(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=15299299; DOI=10.1107/s0907444994009893;
RA   Zao Z., Esnouf R., Isaacs N., Stuart D.;
RT   "A strategy for rapid and effective refinement applied to black swan
RT   lysozyme.";
RL   Acta Crystallogr. D 51:331-336(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX   PubMed=15299731; DOI=10.1107/s0907444995008468;
RA   Karlsen S., Hough E., Rao Z.H., Isaacs N.W.;
RT   "Structure of a bulgecin-inhibited g-type lysozyme from the egg white of
RT   the Australian black swan. A comparison of the binding of bulgecin to three
RT   muramidases.";
RL   Acta Crystallogr. D 52:105-114(1996).
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   PIR; A00872; LZWSG.
DR   PDB; 1GBS; X-ray; 1.50 A; A=1-185.
DR   PDB; 1LSP; X-ray; 2.45 A; A=1-185.
DR   PDBsum; 1GBS; -.
DR   PDBsum; 1LSP; -.
DR   AlphaFoldDB; P00717; -.
DR   SMR; P00717; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EvolutionaryTrace; P00717; -.
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.
FT   CHAIN           1..185
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193515"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..60
FT   DISULFID        18..29
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           30..46
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           49..59
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           110..130
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   TURN            158..163
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   HELIX           169..181
FT                   /evidence="ECO:0007829|PDB:1GBS"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:1GBS"
SQ   SEQUENCE   185 AA;  20400 MW;  22358F632C98342A CRC64;
     RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VPASKTIAER DLKAMDRYKT IIKKVGEKLC
     VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS HKPQGTWNGE VHITQGTTIL
     TDFIKRIQKK FPSWTKDQQL KGGISAYNAG AGNVRSYARM DIGTTHDDYA NDVVARAQYY
     KQHGY