LYSC_CALCC
ID LYSC_CALCC Reviewed; 129 AA.
AC P00699;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Callipepla californica (California quail) (Lophortyx californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=67771;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Egg white;
RX PubMed=89864; DOI=10.1021/bi00580a008;
RA Ibrahimi I.M., Prager E.M., White T.J., Wilson A.C.;
RT "Amino acid sequence of California quail lysozyme. Effect of evolutionary
RT substitutions on the antigenic structure of lysozyme.";
RL Biochemistry 18:2736-2744(1979).
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 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.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR PIR; A00854; LZQJEC.
DR AlphaFoldDB; P00699; -.
DR BMRB; P00699; -.
DR SMR; P00699; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
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 InterPro; IPR030056; Lysozyme_C.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 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; Secreted.
FT CHAIN 1..129
FT /note="Lysozyme C"
FT /id="PRO_0000208865"
FT DOMAIN 1..129
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 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 129 AA; 14308 MW; 144DA7001948E638 CRC64;
KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS
RWWCNDGRTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS DGNGMNAWVA WRNRCKGTDV
HAWIRGCRL
