ID   LYSC_AIXSP              Reviewed;         129 AA.
AC   Q7LZQ2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
GN   Name=LYZ;
OS   Aix sponsa (Wood duck) (Anas sponsa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Aix.
OX   NCBI_TaxID=8833;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Araki T., Torikata T.;
RL   Submitted (MAY-1997) to the PIR data bank.
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC       tissues and body fluids are associated with the monocyte-macrophage
CC       system and enhance the activity of immunoagents. {ECO:0000255|PROSITE-
CC       ProRule:PRU00680}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It acts
CC       rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC       and slowly on chitin oligosaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   PIR; JC5380; JC5380.
DR   AlphaFoldDB; Q7LZQ2; -.
DR   SMR; Q7LZQ2; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PRIDE; Q7LZQ2; -.
DR   BRENDA; 3.2.1.17; 220.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR030056; Lysozyme_C.
DR   PANTHER; PTHR11407; PTHR11407; 1.
DR   PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Secreted.
FT   CHAIN           1..129
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208858"
FT   DOMAIN          1..129
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        64..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        76..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   129 AA;  14476 MW;  037CFDF01A2FEAD0 CRC64;
     KVYERCELAA AMKRLGLDNY RGYSLGNWVC AAKYESNFNT QATNRNTDGS TDYGILEINS
     RWWCNDGKTP GAKNVCGIPC SVLLRSDITE AVKCAKRIVS DGNGMNAWVA WRNRCKGTDV
     SRWIRGCRL