ID   LYSC_FELCA              Reviewed;          20 AA.
AC   P37155;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Fragment;
GN   Name=LYZ;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Milk;
RX   PubMed=2344734; DOI=10.1016/0305-0491(90)90316-l;
RA   Halliday J.A., Bell K., McKenzie H.A., Shaw D.C.;
RT   "Feline whey proteins: identification, isolation and initial
RT   characterization of alpha-lactalbumin, beta-lactoglobulin and lysozyme.";
RL   Comp. Biochem. Physiol. 95B:773-779(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   -!- 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. {ECO:0000305}.
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DR   PIR; A60525; A60525.
DR   AlphaFoldDB; P37155; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Proteomes; UP000011712; Unplaced.
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.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Milk protein; Reference proteome.
FT   CHAIN           1..>20
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000208850"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2314 MW;  EB8824EA59425E13 CRC64;
     KIFTKCELAR KLRAEGMDGF