ID   LYSC_NUMME              Reviewed;         129 AA.
AC   P00704;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
GN   Name=LYZ;
OS   Numida meleagris (Helmeted guineafowl) (Phasianus meleagris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Numididae;
OC   Numida.
OX   NCBI_TaxID=8996;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Egg white;
RX   PubMed=5063251; DOI=10.1016/0005-2795(72)90302-9;
RA   Jolles J., van Leemputten E., Mouton A., Jolles P.;
RT   "Amino acid sequence of guinea-hen egg-white lysozyme.";
RL   Biochim. Biophys. Acta 257:497-510(1972).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=1794991; DOI=10.1093/oxfordjournals.jbchem.a123702;
RA   Fukamizo T., Ikeda Y., Torikata T., Araki T., Kuramoto M., Goto S.;
RT   "1H-NMR study on the structure of lysozyme from guinea hen egg white.";
RL   J. Biochem. 110:997-1003(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=8061608; DOI=10.1002/pro.5560030508;
RA   Lescar J., Souchon H., Alzari P.M.;
RT   "Crystal structures of pheasant and guinea fowl egg-white lysozymes.";
RL   Protein Sci. 3:788-798(1994).
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.
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.
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; A00859; LZUH.
DR   PDB; 1FBI; X-ray; 3.00 A; X/Y=1-129.
DR   PDB; 1HHL; X-ray; 1.90 A; A=1-129.
DR   PDBsum; 1FBI; -.
DR   PDBsum; 1HHL; -.
DR   AlphaFoldDB; P00704; -.
DR   SMR; P00704; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   ABCD; P00704; 2 sequenced antibodies.
DR   EvolutionaryTrace; P00704; -.
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   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted.
FT   CHAIN           1..129
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208868"
FT   DOMAIN          1..129
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT   ACT_SITE        52
FT   DISULFID        6..127
FT   DISULFID        30..115
FT   DISULFID        64..80
FT   DISULFID        76..94
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1FBI"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           80..84
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           89..101
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           104..107
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           109..114
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1HHL"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:1HHL"
SQ   SEQUENCE   129 AA;  14309 MW;  6D5917000E7D8CFD CRC64;
     KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS
     RWWCNDGRTP GSRNLCNIPC SALQSSDITA TANCAKKIVS DGNGMNAWVA WRKHCKGTDV
     RVWIKGCRL