ID   LYSC_CHRAM              Reviewed;         129 AA.
AC   P22910;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
GN   Name=LYZ;
OS   Chrysolophus amherstiae (Lady Amherst's pheasant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Chrysolophus.
OX   NCBI_TaxID=9088;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Egg white;
RX   MEDLINE=91136781; PubMed=1368578;
RA   Araki T., Kuramoto M., Torikata T.;
RT   "The amino acid sequence of Lady Amherst's pheasant (Chrysolophus
RT   amherstiae) and golden pheasant (Chrysolophus pictus) egg-white
RT   lysozymes.";
RL   Agric. Biol. Chem. 54:2299-2308(1990).
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.
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   PIR; JH0211; JH0211.
DR   HSSP; P00698; 1UIB.
DR   SMR; P22910; 1-129.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   HOVERGEN; P22910; -.
DR   BRENDA; 3.2.1.17; 296717.
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.
FT   CHAIN         1    129       Lysozyme C.
FT                                /FTId=PRO_0000208861.
FT   ACT_SITE     35     35       By similarity.
FT   ACT_SITE     52     52       By similarity.
FT   DISULFID      6    127       By similarity.
FT   DISULFID     30    115       By similarity.
FT   DISULFID     64     80       By similarity.
FT   DISULFID     76     94       By similarity.
SQ   SEQUENCE   129 AA;  14311 MW;  E0A6D33123F39CF2 CRC64;
     KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS
     RWWCNDGRTP GSRNLCHIPC SALLSSDITA SVNCAKKIVS DGNGMNAWVA WRNRCKGTDV
     NAWTRGCRL
//