ID LYS_BOMMO Reviewed; 137 AA. AC P48816; Q9TWL7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Lysozyme; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase; DE Flags: Precursor; OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7091; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fat body; RX PubMed=7665079; DOI=10.1016/0378-1119(95)00199-g; RA Lee W.J., Brey P.T.; RT "Isolation and characterization of the lysozyme-encoding gene from the RT silkworm Bombyx mori."; RL Gene 161:199-203(1995). RN [2] RP PROTEIN SEQUENCE OF 19-38, AND FUNCTION. RC STRAIN=NB18; TISSUE=Larval hemolymph; RX PubMed=7876591; DOI=10.1006/jipa.1995.1003; RA Abraham E.G., Nagaraju J., Salunke D., Gupta H.M., Datta R.K.; RT "Purification and partial characterization of an induced antibacterial RT protein in the silkworm, Bombyx mori."; RL J. Invertebr. Pathol. 65:17-24(1995). 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. Active against E.coli CC and M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680, CC ECO:0000269|PubMed:7876591}. 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 -!- DEVELOPMENTAL STAGE: Expressed within 6 hours after induction, reaches CC maximum levels after 48 hours and declines after 72 hours after CC induction. CC -!- INDUCTION: By bacterial infection. 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; L37416; AAB40947.1; -; mRNA. DR PIR; JC4233; JC4233. DR RefSeq; NP_001037448.1; NM_001043983.1. DR PDB; 1GD6; X-ray; 2.50 A; A=19-137. DR PDB; 2RSC; NMR; -; A=19-137. DR PDBsum; 1GD6; -. DR PDBsum; 2RSC; -. DR AlphaFoldDB; P48816; -. DR BMRB; P48816; -. DR SMR; P48816; -. DR STRING; 7091.P48816; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR PaxDb; 7091-BGIBMGA010439-TA; -. DR EnsemblMetazoa; NM_001043983.1; NP_001037448.1; GeneID_693015. DR GeneID; 693015; -. DR KEGG; bmor:693015; -. DR CTD; 693015; -. DR eggNOG; ENOG502S4CB; Eukaryota. DR HOGENOM; CLU_111620_2_0_1; -. DR InParanoid; P48816; -. DR OMA; TCNVKCE; -. DR OrthoDB; 5361006at2759; -. DR EvolutionaryTrace; P48816; -. DR Proteomes; UP000005204; Unassembled WGS sequence. 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; cd00119; LYZ; 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:SF63; 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; Antibiotic; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Reference proteome; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:7876591" FT CHAIN 19..137 FT /note="Lysozyme" FT /id="PRO_0000018505" FT DOMAIN 19..137 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 50 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 67 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 24..137 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 45..127 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 79..93 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 89..107 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:1GD6" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:1GD6" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:1GD6" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:1GD6" FT TURN 69..72 FT /evidence="ECO:0007829|PDB:1GD6" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:1GD6" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:1GD6" FT TURN 87..90 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:1GD6" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 102..115 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:1GD6" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:1GD6" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1GD6" SQ SEQUENCE 137 AA; 15668 MW; FFE5710506C61A1D CRC64; MQKLIIFALV VLCVGSEAKT FTRCGLVHEL RKHGFEENLM RNWVCLVEHE SSRDTSKTNT NRNGSKDYGL FQINDRYWCS KGASPGKDCN VKCSDLLTDD ITKAAKCAKK IYKRHRFDAW YGWKNHCQGS LPDISSC //