ID LYSC_COLVI Reviewed; 129 AA. AC P00700; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 126. DE RecName: Full=Lysozyme C; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; GN Name=LYZ; OS Colinus virginianus (Northern bobwhite) (Tetrao virginianus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae; OC Colinus. OX NCBI_TaxID=9014; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Egg white; RX PubMed=4112539; DOI=10.1016/s0021-9258(19)45297-6; RA Prager E.M., Arnheim N., Mross G.A., Wilson A.C.; RT "Amino acid sequence studies on bobwhite quail egg white lysozyme."; RL J. Biol. Chem. 247:2905-2916(1972). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8880929; RX DOI=10.1002/(sici)1097-0134(199609)26:1<55::aid-prot5>3.0.co;2-f; RA Chacko S., Silverton E.W., Smith-Gill S.J., Davies D.R., Schick K.A., RA Xavier K.A., Willson R.C., Jeffrey P.D., Chang C.Y., Sieker L.C., RA Sheriff S.; RT "Refined structures of bobwhite quail lysozyme uncomplexed and complexed RT with the HyHEL-5 Fab fragment."; RL Proteins 26:55-65(1996). 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 also shows 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; A00855; LZQJEB. DR PDB; 1BQL; X-ray; 2.60 A; Y=1-129. DR PDB; 1DKJ; X-ray; 2.00 A; A=1-129. DR PDB; 1DKK; X-ray; 1.90 A; A/B=1-129. DR AlphaFoldDB; P00700; -. DR BMRB; P00700; -. DR SMR; P00700; -. DR ABCD; P00700; 1 sequenced antibody. DR EvolutionaryTrace; P00700; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:TreeGrafter. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter. DR CDD; cd16897; LYZ_C; 1. DR FunFam; 1.10.530.10:FF:000001; Lysozyme 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. DR PDBsum; 1BQL; -. DR PDBsum; 1DKJ; -. DR PDBsum; 1DKK; -. PE 1: Evidence at protein level; KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Secreted. FT CHAIN 1..129 FT /note="Lysozyme C" FT /id="PRO_0000208863" FT DOMAIN 1..129 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 35 FT ACT_SITE 52 FT DISULFID 6..127 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:4112539" FT DISULFID 30..115 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:4112539" FT DISULFID 64..80 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:4112539" FT DISULFID 76..94 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:4112539" FT HELIX 5..14 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 25..36 FT /evidence="ECO:0007829|PDB:1DKK" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:1DKK" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1DKK" FT TURN 54..57 FT /evidence="ECO:0007829|PDB:1DKK" FT TURN 60..63 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 80..84 FT /evidence="ECO:0007829|PDB:1DKK" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 89..99 FT /evidence="ECO:0007829|PDB:1DKK" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:1DKK" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1DKK" FT HELIX 120..124 FT /evidence="ECO:0007829|PDB:1DKK" SQ SEQUENCE 129 AA; 14271 MW; 1C5797001951FF38 CRC64; KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS RWWCNDGKTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL //