ID LYSC_PELSI Reviewed; 131 AA. AC Q7LZQ1; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 3. DT 24-JAN-2024, entry version 89. DE RecName: Full=Lysozyme C; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; DE AltName: Full=Softshell turtle lysozyme C; DE Short=SSTL; GN Name=LYZ; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia; OC Trionychidae; Pelodiscus. OX NCBI_TaxID=13735; RN [1] RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC TISSUE=Egg white; RX PubMed=16549391; DOI=10.1016/j.cbpc.2006.02.004; RA Thammasirirak S., Ponkham P., Preecharram S., Khanchanuan R., RA Phonyothee P., Daduang S., Srisomsap C., Araki T., Svasti J.; RT "Purification, characterization and comparison of reptile lysozymes."; RL Comp. Biochem. Physiol. 143:209-217(2006). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RC TISSUE=Egg white; RX PubMed=19029145; DOI=10.1093/jb/mvn156; RA Siritapetawee J., Thammasirirak S., Robinson R.C., Yuvaniyama J.; RT "The 1.9 A X-ray structure of egg-white lysozyme from Taiwanese soft- RT shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences RT from the standard chicken-type lysozyme."; RL J. Biochem. 145:193-198(2009). 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. Has strong CC bacteriolytic activity against M.luteus and V.cholerae, weak CC bacteriolytic activity against P.aeruginosa and no activity against CC A.hydrophila. {ECO:0000255|PROSITE-ProRule:PRU00680, CC ECO:0000269|PubMed:16549391}. 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|PubMed:16549391}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:16549391}; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. Activity rapidly decreases CC within 30 minutes of incubation at 90 degrees Celsius. CC {ECO:0000269|PubMed:16549391}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. 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; JC5493; JC5493. DR PDB; 2GV0; X-ray; 1.90 A; A=1-131. DR PDBsum; 2GV0; -. DR AlphaFoldDB; Q7LZQ1; -. DR SMR; Q7LZQ1; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR eggNOG; ENOG502RZU4; Eukaryota. DR HOGENOM; CLU_111620_0_1_1; -. DR BRENDA; 3.2.1.17; 6494. DR EvolutionaryTrace; Q7LZQ1; -. DR Proteomes; UP000007267; Unassembled WGS sequence. 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. FT CHAIN 1..131 FT /note="Lysozyme C" FT /id="PRO_0000208876" FT DOMAIN 2..131 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 36 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 54 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 7..129 FT DISULFID 31..117 FT DISULFID 66..82 FT DISULFID 78..96 FT HELIX 6..15 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 26..37 FT /evidence="ECO:0007829|PDB:2GV0" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:2GV0" FT TURN 48..51 FT /evidence="ECO:0007829|PDB:2GV0" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:2GV0" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:2GV0" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 91..102 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 111..116 FT /evidence="ECO:0007829|PDB:2GV0" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:2GV0" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:2GV0" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:2GV0" SQ SEQUENCE 131 AA; 14732 MW; D59A7791775E6AA1 CRC64; GKIYEQCELA REFKRHGMDG YHGYSLGDWV CTAKHESNFN TAATNYNRGD QSTDYGILQI NSRWWCNDGK TPKAKNACGI ECSELLKADI TAAVNCAKRI VRDPNGMGAW VAWTKYCKGK DVSQWIKGCK L //