ID LYSM1_STRGL Reviewed; 294 AA. AC P25310; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 28-JUN-2023, entry version 109. DE RecName: Full=Lysozyme M1; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase M1; DE Flags: Precursor; GN Name=acm; OS Streptomyces globisporus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1908; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 78-117, AND RP DISULFIDE BOND. RC STRAIN=ATCC 21553 / DSM 40991 / FERM P-596; RX PubMed=2341041; DOI=10.1016/0378-1119(90)90062-v; RA Lichenstein H.S., Hastings A.E., Langley K.E., Mendiaz E.A., Rohde M.F., RA Elmore R., Zukowski M.M.; RT "Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene RT from Streptomyces globisporus."; RL Gene 88:81-86(1990). CC -!- FUNCTION: This enzyme has both lysozyme (acetylmuramidase) and CC diacetylmuramidase activities. 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}. 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; M30645; AAA26687.1; -; Genomic_DNA. DR PIR; JQ0529; MUSMM1. DR PDB; 1JFX; X-ray; 1.65 A; A=78-294. DR PDBsum; 1JFX; -. DR AlphaFoldDB; P25310; -. DR SMR; P25310; -. DR CAZy; GH25; Glycoside Hydrolase Family 25. DR EvolutionaryTrace; P25310; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. 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:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR CDD; cd06412; GH25_CH-type; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR002053; Glyco_hydro_25. DR InterPro; IPR008270; Glyco_hydro_25_AS. DR InterPro; IPR018077; Glyco_hydro_fam25_subgr. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR34135; LYSOZYME; 1. DR PANTHER; PTHR34135:SF2; LYSOZYME; 1. DR Pfam; PF01183; Glyco_hydro_25; 1. DR SMART; SM00641; Glyco_25; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1. DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Secreted; Signal. FT SIGNAL 1..? FT /evidence="ECO:0000255" FT PROPEP ?..77 FT /evidence="ECO:0000269|PubMed:2341041" FT /id="PRO_0000018517" FT CHAIN 78..294 FT /note="Lysozyme M1" FT /id="PRO_0000018518" FT DOMAIN 81..294 FT /note="Ch-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252" FT ACT_SITE 86 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252" FT ACT_SITE 175 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252" FT ACT_SITE 177 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252, FT ECO:0000255|PROSITE-ProRule:PRU10065" FT DISULFID 185..224 FT /evidence="ECO:0000269|PubMed:2341041" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:1JFX" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:1JFX" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 149..158 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1JFX" FT TURN 184..187 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 190..208 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:1JFX" FT TURN 230..234 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 237..240 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 257..267 FT /evidence="ECO:0007829|PDB:1JFX" FT STRAND 270..281 FT /evidence="ECO:0007829|PDB:1JFX" FT HELIX 283..291 FT /evidence="ECO:0007829|PDB:1JFX" SQ SEQUENCE 294 AA; 31169 MW; D96EFE914FA04997 CRC64; MPAYSSLARR GRRPAVVLLG GLVSASLALT LAPTAAAAPL APPPGKDVGP GEAYMGVGTR IEQGLGAGPD ERTIGPADTS GVQGIDVSHW QGSINWSSVK SAGMSFAYIK ATEGTNYKDD RFSANYTNAY NAGIIRGAYH FARPNASSGT AQADYFASNG GGWSRDNRTL PGVLDIEHNP SGAMCYGLST TQMRTWINDF HARYKARTTR DVVIYTTASW WNTCTGSWNG MAAKSPFWVA HWGVSAPTVP SGFPTWTFWQ YSATGRVGGV SGDVDRNKFN GSAARLLALA NNTA //