ID LYSC_SEMEN Reviewed; 148 AA. AC P67977; P07232; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 03-MAY-2023, entry version 67. 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; Synonyms=LZM; OS Semnopithecus entellus (Northern plains gray langur) (Presbytis entellus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Semnopithecus. OX NCBI_TaxID=88029; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Stomach; RX PubMed=1960739; DOI=10.1007/bf02103133; RA Swanson K.W., Irwin D.M., Wilson A.C.; RT "Stomach lysozyme gene of the langur monkey: tests for convergence and RT positive selection."; RL J. Mol. Evol. 33:418-425(1991). RN [2] RP PROTEIN SEQUENCE OF 19-148. RX PubMed=3120013; DOI=10.1038/330401a0; RA Stewart C.-B., Schilling J.W., Wilson A.C.; RT "Adaptive evolution in the stomach lysozymes of foregut fermenters."; RL Nature 330:401-404(1987). 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. Also plays a role in CC digestion in this species. 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 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 EMBL; X60235; CAA42795.1; -; mRNA. DR EMBL; X60234; CAA42794.1; -; Genomic_DNA. DR PIR; I61852; I61852. DR AlphaFoldDB; P67977; -. DR SMR; P67977; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. 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:0007586; P:digestion; 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 Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:3120013" FT CHAIN 19..148 FT /note="Lysozyme C" FT /id="PRO_0000018482" FT DOMAIN 19..148 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 53 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 71 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 24..146 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 48..134 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 83..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 95..113 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" SQ SEQUENCE 148 AA; 16219 MW; 57C9E1BA4986AA89 CRC64; MKALTILGLV LLSVTVQGKI FERCELARTL KKLGLDGYKG VSLANWVCLA KWESGYNTEA TNYNPGDEST DYGIFQINSR YWCNNGKTPG AVDACHISCS ALLQNNIADA VACAKRVVSD PQGIRAWVAW RNHCQNKDVS QYVKGCGV //