ID LYSC_COTJA Reviewed; 147 AA. AC P00701; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 120. 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 Coturnix japonica (Japanese quail) (Coturnix coturnix japonica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Perdicinae; Coturnix. OX NCBI_TaxID=93934; RN [1] RP PROTEIN SEQUENCE OF 1-18 (PRECURSOR PROTEIN). RX PubMed=3511061; DOI=10.1016/s0021-9258(17)35936-7; RA Weisman L.S., Krummel B.M., Wilson A.C.; RT "Evolutionary shift in the site of cleavage of prelysozyme."; RL J. Biol. Chem. 261:2309-2313(1986). RN [2] RP PROTEIN SEQUENCE OF 19-147. RX PubMed=5358633; RA Kaneda M., Kato I., Tominaga N., Titani K., Narita K.; RT "The amino acid sequence of quail lysozyme."; RL J. Biochem. 66:747-749(1969). RN [3] RP PROTEIN SEQUENCE OF 19-147, AND CATALYTIC ACTIVITY. RC TISSUE=Egg white; RA Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T., RA Svasti J.; RT "Quail lysozyme II."; RL Submitted (SEP-2006) to UniProtKB. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147. RA Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z.; RL Submitted (JUN-1993) to the PDB data bank. 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; Evidence={ECO:0000269|Ref.3}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; A91922; LZQJE. DR PIR; JU0237; JU0237. DR PDB; 2IHL; X-ray; 1.40 A; A=19-147. DR PDBsum; 2IHL; -. DR AlphaFoldDB; P00701; -. DR SMR; P00701; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR ABCD; P00701; 1 sequenced antibody. DR EvolutionaryTrace; P00701; -. DR Proteomes; UP000694412; Unplaced. DR Proteomes; UP000694961; Genome assembly. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR CDD; cd16897; LYZ_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 3D-structure; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:5358633, ECO:0000269|Ref.3" FT CHAIN 19..147 FT /note="Lysozyme C" FT /id="PRO_0000018496" FT DOMAIN 19..147 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 53 FT ACT_SITE 70 FT DISULFID 24..145 FT DISULFID 48..133 FT DISULFID 82..98 FT DISULFID 94..112 FT CONFLICT 39 FT /note="Q -> LK (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 43..54 FT /evidence="ECO:0007829|PDB:2IHL" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:2IHL" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:2IHL" FT TURN 72..75 FT /evidence="ECO:0007829|PDB:2IHL" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 98..102 FT /evidence="ECO:0007829|PDB:2IHL" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 127..132 FT /evidence="ECO:0007829|PDB:2IHL" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:2IHL" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:2IHL" SQ SEQUENCE 147 AA; 16278 MW; B1D03EDA0E85DED3 CRC64; MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA KFESNFNTQA TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDV HGMNAWVAWR NRCKGTDVNA WIRGCRL //