ID   LYSC_TRIVU              Reviewed;         147 AA.
AC   P51782;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYZ;
OS   Trichosurus vulpecula (Brush-tailed possum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX   NCBI_TaxID=9337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mammary gland;
RX   MEDLINE=97449326; PubMed=9305795; DOI=10.1016/S0304-4165(97)00033-0;
RA   Piotte C.P., Marshall C.J., Hubbard M.J., Collet C., Grigor M.R.;
RT   "Lysozyme and alpha-lactalbumin from the milk of a marsupial, the
RT   common brush-tailed possum (Trichosurus vulpecula).";
RL   Biochim. Biophys. Acta 1336:235-242(1997).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC       in tissues and body fluids are associated with the monocyte-
CC       macrophage system and enhance the activity of immunoagents.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- MASS SPECTROMETRY: Mass=14896; Method=MALDI; Range=19-147;
CC       Source=PubMed:9305795;
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It
CC       acts rapidly on both peptide-substituted and unsubstituted
CC       peptidoglycan, and slowly on chitin oligosaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
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DR   EMBL; U40664; AAB97109.1; -; Genomic_DNA.
DR   HSSP; P00695; 1LZ6.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   HOVERGEN; P51782; -.
DR   BRENDA; 3.2.1.17; 270554.
DR   GO; GO:0003796; F:lysozyme activity; IEA:EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     18
FT   CHAIN        19    147       Lysozyme C.
FT                                /FTId=PRO_0000018493.
FT   ACT_SITE     53     53       By similarity.
FT   ACT_SITE     71     71       By similarity.
FT   DISULFID     24    145       By similarity.
FT   DISULFID     48    133       By similarity.
FT   DISULFID     83     99       By similarity.
FT   DISULFID     95    113       By similarity.
SQ   SEQUENCE   147 AA;  16839 MW;  F281667A17F483AC CRC64;
     MKVLLLLGFI FCSMAAHGKR MERCEFARRI KQLHLDGYHQ ISLANWVCLA QWESGFDTKA
     TNYNPGDQST DYGILQINSH YWCDDGKTPH AANECKVRCS ELQEDDLVKA VNCAKKIVDQ
     QGIRAWVAWR NKCEGKDLSK YLEGCHL
//