ID LYSC_EQUAS Reviewed; 129 AA. AC P11375; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 08-NOV-2023, entry version 109. DE RecName: Full=Lysozyme C; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; GN Name=LYZ; OS Equus asinus (Donkey) (Equus africanus asinus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9793; RN [1] RP PROTEIN SEQUENCE. RX PubMed=3242541; DOI=10.1515/bchm3.1988.369.2.1109; RA Godovac-Zimmermann J., Conti A., Napolitano L.; RT "The primary structure of donkey (Equus asinus) lysozyme contains the RT Ca(II) binding site of alpha-lactalbumin."; RL Biol. Chem. Hoppe-Seyler 369:1109-1115(1988). 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305}; CC -!- SUBUNIT: Monomer. 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; S01661; S01661. DR PDB; 5XUW; X-ray; 1.76 A; A/B=1-129. DR PDBsum; 5XUW; -. DR AlphaFoldDB; P11375; -. DR SMR; P11375; -. DR Allergome; 12071; Equ as 6. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR Proteomes; UP000694387; Unplaced. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:SF69; LYSOZYME C, MILK ISOZYME; 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; Calcium; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Metal-binding; Milk protein; Reference proteome. FT CHAIN 1..129 FT /note="Lysozyme C" FT /id="PRO_0000208849" 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 53 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P81708" FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P81708" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P81708" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P81708" FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P81708" FT DISULFID 6..127 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 30..115 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 65..80 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 76..94 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT HELIX 5..14 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 25..36 FT /evidence="ECO:0007829|PDB:5XUW" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:5XUW" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:5XUW" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:5XUW" FT TURN 61..64 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:5XUW" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 89..100 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:5XUW" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:5XUW" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:5XUW" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:5XUW" SQ SEQUENCE 129 AA; 14688 MW; 094D0850B41A40F5 CRC64; KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG SYDYGLFQLN SKWWCKDNKR SSSNACNIMC SKLLDDNIDD DISCAKRVVR DPKGMSAWKA WVKHCKDKDL SEYLASCNL //