ID   LYSC_RABIT              Reviewed;         130 AA.
AC   P16973;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
GN   Name=LYZ;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Kidney;
RX   PubMed=2361954; DOI=10.1093/oxfordjournals.jbchem.a123032;
RA   Ito Y., Yamada H., Nakamura S., Imoto T.;
RT   "Purification, amino acid sequence, and some properties of rabbit kidney
RT   lysozyme.";
RL   J. Biochem. 107:236-241(1990).
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 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; JC2506; JC2506.
DR   PIR; JX0104; JX0104.
DR   PIR; JX0367; JX0367.
DR   AlphaFoldDB; P16973; -.
DR   SMR; P16973; -.
DR   FunCoup; P16973; 42.
DR   STRING; 9986.ENSOCUP00000011947; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 9986-ENSOCUP00000011947; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   InParanoid; P16973; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
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; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..130
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208855"
FT   DOMAIN          1..130
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        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   130 AA;  14722 MW;  000A3330EDB26C25 CRC64;
     KIYERCELAR TLKKLGLDGY KGVSLANWMC LAKWESSYNT RATNYNPGDK STDYGIFQIN
     SRYWCNDGKT PRAVNACHIP CSDLLKDDIT QAVACAKRVV SDPQGIRAWV AWRNHCQNQD
     LTPYIRGCGV
//