ID LYSC1_HORSE Reviewed; 129 AA. AC P11376; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 08-NOV-2023, entry version 138. DE RecName: Full=Lysozyme C, milk isozyme; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; GN Name=LYZ; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Milk; RX PubMed=4039138; RA McKenzie H.A., Shaw D.C.; RT "The amino acid sequence of equine milk lysozyme."; RL Biochem. Int. 10:23-31(1985). RN [2] RP CALCIUM-BINDING DATA. RC TISSUE=Milk; RX PubMed=3666156; DOI=10.1016/0014-5793(87)80328-9; RA Nitta K., Tsuge H., Sugai S., Shimazaki K.; RT "The calcium-binding property of equine lysozyme."; RL FEBS Lett. 223:405-408(1987). RN [3] RP PROTEIN SEQUENCE OF 1-35, AND CRYSTALLIZATION. RC TISSUE=Milk; RX PubMed=2394704; DOI=10.1016/s0021-9258(18)77198-6; RA Zeng J., Rao K.R., Brew K., Fenna R.; RT "Crystallization of a calcium-binding lysozyme from horse milk."; RL J. Biol. Chem. 265:14886-14887(1990). RN [4] RP STRUCTURE BY NMR. RC TISSUE=Milk; RX PubMed=1646637; DOI=10.1016/0167-4838(91)90095-h; RA Tsuge H., Koseki K., Miyano M., Shimazaki K., Chuman T., Matsumoto T., RA Noma M., Nitta K., Sugai S.; RT "A structural study of calcium-binding equine lysozyme by two-dimensional RT 1H-NMR."; RL Biochim. Biophys. Acta 1078:77-84(1991). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC TISSUE=Milk; RX PubMed=1569037; DOI=10.1093/oxfordjournals.jbchem.a123727; RA Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M.; RT "Crystallographic studies of a calcium binding lysozyme from equine milk at RT 2.5-A resolution."; RL J. Biochem. 111:141-143(1992). 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; CC Note=Binds 1 Ca(2+) ion per subunit.; 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; S07435; S07435. DR PDB; 2EQL; X-ray; 2.50 A; A=1-129. DR PDBsum; 2EQL; -. DR AlphaFoldDB; P11376; -. DR SMR; P11376; -. DR STRING; 9796.ENSECAP00000008172; -. DR Allergome; 12069; Equ c 6. DR Allergome; 12070; Equ c 6.0101. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR PaxDb; 9796-ENSECAP00000008172; -. DR HOGENOM; CLU_111620_0_1_1; -. DR InParanoid; P11376; -. DR EvolutionaryTrace; P11376; -. DR Proteomes; UP000002281; Unplaced. DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central. 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; Reference proteome. FT CHAIN 1..129 FT /note="Lysozyme C, milk isozyme" FT /id="PRO_0000208851" 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:0000305|PubMed:3666156" FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:3666156" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:3666156" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:3666156" FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305|PubMed:3666156" 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..13 FT /evidence="ECO:0007829|PDB:2EQL" FT TURN 14..19 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 25..36 FT /evidence="ECO:0007829|PDB:2EQL" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:2EQL" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:2EQL" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:2EQL" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 61..64 FT /evidence="ECO:0007829|PDB:2EQL" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:2EQL" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 89..98 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:2EQL" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:2EQL" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:2EQL" FT TURN 121..126 FT /evidence="ECO:0007829|PDB:2EQL" SQ SEQUENCE 129 AA; 14653 MW; 87040531F4B60F46 CRC64; KVFSKCELAH KLKAQEMDGF GGYSLANWVC MAEYESNFNT RAFNGKNANG SSDYGLFQLN NKWWCKDNKR SSSNACNIMC SKLLDENIDD DISCAKRVVR DPKGMSAWKA WVKHCKDKDL SEYLASCNL //