ID LYSC_TITST Reviewed; 15 AA. AC P0C8X2; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 03-MAY-2023, entry version 19. DE RecName: Full=Lysozyme-like peptide; DE EC=3.2.1.17; DE Flags: Fragment; OS Tityus stigmurus (Brazilian scorpion). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus. OX NCBI_TaxID=50344; RN [1] RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=17270501; DOI=10.1016/j.cbpc.2006.12.004; RA Batista C.V.F., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z., RA Gomez-Lagunas F., Possani L.D.; RT "Proteomic analysis of the venom from the scorpion Tityus stigmurus: RT biochemical and physiological comparison with other Tityus species."; RL Comp. Biochem. Physiol. 146C:147-157(2007). CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function. CC {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- MASS SPECTROMETRY: Mass=14226; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:17270501}; 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 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. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; KW Glycosidase; Hydrolase; Secreted. FT PEPTIDE 1..>15 FT /note="Lysozyme-like peptide" FT /id="PRO_0000366110" FT NON_TER 15 SQ SEQUENCE 15 AA; 1865 MW; 4D47889874236608 CRC64; SIYERCELAR ELINR //