ID LYSC_MELGA Reviewed; 147 AA. AC P00703; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 04-NOV-2026, entry version 171. 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 Meleagris gallopavo (Wild turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Meleagridinae; Meleagris. OX NCBI_TaxID=9103; 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. RC TISSUE=Egg white; RX PubMed=5440837; DOI=10.1016/s0021-9258(18)63195-3; RA Larue J.N., Speck J.C. Jr.; RT "Turkey egg white lysozyme. Preparation of the crystalline enzyme and RT investigation of the amino acid sequence."; RL J. Biol. Chem. 245:1985-1991(1970). RN [3] RP X-RAY CRYSTALLOGRAPHY, AND DISULFIDE BONDS. RX PubMed=886621; DOI=10.1016/0022-2836(77)90238-8; RA Sarma R., Bott R.; RT "Crystallographic study of turkey egg-white lysozyme and its complex with a RT disaccharide."; RL J. Mol. Biol. 113:555-565(1977). RN [4] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=1515108; DOI=10.1107/s0108768191012466; RA Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J.; RT "Structure determination of turkey egg-white lysozyme using Laue RT diffraction data."; RL Acta Crystallogr. B 48:200-207(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=15299795; DOI=10.1107/s0907444994013612; RA Howell P.L.; RT "Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution."; RL Acta Crystallogr. D 51:654-662(1995). RN [6] RP STRUCTURE BY NMR. RX PubMed=8344294; DOI=10.1111/j.1432-1033.1993.tb18030.x; RA Bartik K., Dobson C.M., Redfield C.; RT "1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg- RT white lysozyme."; RL Eur. J. Biochem. 215:255-266(1993). 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; C92574; LZTK. DR RefSeq; XP_003202118.1; XM_003202070.4. DR PDB; 135L; X-ray; 1.30 A; A=19-147. DR PDB; 1DZB; X-ray; 2.00 A; X/Y=19-147. DR PDB; 1JEF; X-ray; 1.77 A; A=19-147. DR PDB; 1JSE; X-ray; 1.12 A; A=19-147. DR PDB; 1JTP; X-ray; 1.90 A; L/M=19-147. DR PDB; 1LJN; X-ray; 1.19 A; A=19-147. DR PDB; 1LZ2; X-ray; 2.80 A; A=19-147. DR PDB; 1LZY; X-ray; 1.55 A; A=19-147. DR PDB; 1TEW; X-ray; 1.65 A; A=19-147. DR PDB; 1UAC; X-ray; 1.70 A; Y=19-147. DR PDB; 1XFT; X-ray; 3.35 A; A=19-147. DR PDB; 2LZ2; X-ray; 2.20 A; A=19-147. DR PDB; 3LZ2; X-ray; 2.50 A; A=19-147. DR AlphaFoldDB; P00703; -. DR BMRB; P00703; -. DR SMR; P00703; -. DR FunCoup; P00703; 36. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR ABCD; P00703; 7 sequenced antibodies. DR Ensembl; ENSMGAT00000011853.2; ENSMGAP00000010985.1; ENSMGAG00000010559.2. DR GeneID; 100547044; -. DR KEGG; mgp:100547044; -. DR CTD; 4069; -. DR GeneTree; ENSGT00940000153832; -. DR HOGENOM; CLU_111620_0_1_1; -. DR InParanoid; P00703; -. DR OMA; ACGIECS; -. DR OrthoDB; 17373at2759; -. DR EvolutionaryTrace; P00703; -. DR Proteomes; UP000001645; Chromosome 1. DR Bgee; ENSMGAG00000010559; Expressed in bursa of Fabricius and 12 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:CAFA. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0003796; F:lysozyme activity; IDA:CAFA. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:CAFA. 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:Ensembl. DR GO; GO:0031640; P:killing of cells of another organism; IEA:Ensembl. 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. 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:5440837" FT CHAIN 19..147 FT /note="Lysozyme C" FT /id="PRO_0000018497" FT DOMAIN 19..147 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 24..145 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:886621" FT DISULFID 48..133 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:886621" FT DISULFID 82..98 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:886621" FT DISULFID 94..112 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680, FT ECO:0000269|PubMed:886621" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:1JSE" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:1TEW" FT HELIX 43..54 FT /evidence="ECO:0007829|PDB:1JSE" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:2LZ2" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:1JSE" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1JSE" FT TURN 72..75 FT /evidence="ECO:0007829|PDB:1JSE" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:1JSE" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:1JSE" FT HELIX 98..102 FT /evidence="ECO:0007829|PDB:1JSE" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:1JSE" FT HELIX 107..117 FT /evidence="ECO:0007829|PDB:1JSE" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1JTP" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:1JSE" FT HELIX 127..132 FT /evidence="ECO:0007829|PDB:1JSE" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:1JSE" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:1JSE" SQ SEQUENCE 147 AA; 16135 MW; 77C54CD70834583F CRC64; MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA KFESNFNTHA TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA LLSSDITASV NCAKKIASGG NGMNAWVAWR NRCKGTDVHA WIRGCRL //