ID   LYSC_COLLI              Reviewed;         127 AA.
AC   P00708;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
GN   Name=LYZ;
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC   Columbidae; Columba.
OX   NCBI_TaxID=8932;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Egg white;
RX   PubMed=4091856;
RA   Rodriguez R., Menendez-Arias L., Gonzalez de Buitrago G., Gavilanes J.G.;
RT   "Amino acid sequence of pigeon egg-white lysozyme.";
RL   Biochem. Int. 11:841-843(1985).
RN   [2]
RP   CALCIUM-BINDING DATA.
RX   PubMed=3214551; DOI=10.1515/bchm3.1988.369.2.671;
RA   Nitta K., Tsuge H., Shimazaki K., Sugai S.;
RT   "Calcium-binding lysozymes.";
RL   Biol. Chem. Hoppe-Seyler 369:671-675(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=1607355; DOI=10.1093/oxfordjournals.jbchem.a123703;
RA   Yao M., Tanaka I., Hikichi K., Nitta K.;
RT   "Crystallization and preliminary X-ray structure analysis of pigeon egg-
RT   white lysozyme.";
RL   J. Biochem. 111:1-3(1992).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it also shows 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; A00863; LZPY.
DR   AlphaFoldDB; P00708; -.
DR   SMR; P00708; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   eggNOG; ENOG502S4CB; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:TreeGrafter.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter.
DR   CDD; cd16897; LYZ_C; 1.
DR   FunFam; 1.10.530.10:FF:000001; Lysozyme C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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; Calcium; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Metal-binding; Secreted.
FT   CHAIN           1..127
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208862"
FT   DOMAIN          1..127
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   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P11376"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P11376,
FT                   ECO:0000305|PubMed:1607355"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P11376"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P11376,
FT                   ECO:0000305|PubMed:1607355"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P11376,
FT                   ECO:0000305|PubMed:1607355"
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   127 AA;  14452 MW;  96D3BAFDFD934DD8 CRC64;
     KDIPRCELVK ILRRHGFEGF VGKTVANWVC LVKHESGYRT TAFNNNGPNS RDYGIFQINS
     KYWCNDGKTR GSKNACNINC SKLRDDNIAD DIQCAKKIAR EARGLTPWVA WKKYCQGKDL
     SSYVRGC
//