ID   LYS_CHASP               Reviewed;         211 AA.
AC   P00721;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=N,O-diacetylmuramidase;
DE            EC=3.2.1.17;
DE   AltName: Full=Lysozyme CH;
OS   Chalaropsis sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Chalara; unclassified Chalara.
OX   NCBI_TaxID=36534;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1168638; DOI=10.1016/s0021-9258(19)41457-9;
RA   Felch J.W., Inagami T., Hash J.H.;
RT   "The N, O-diacetylmuramidase of Chalaropsis species. V. The complete amino
RT   acid sequence.";
RL   J. Biol. Chem. 250:3713-3720(1975).
RN   [2]
RP   ACTIVE SITE.
RX   PubMed=567645; DOI=10.1016/s0021-9258(17)37988-7;
RA   Fouche P.B., Hash J.H.;
RT   "The N,O-diacetylmuramidase of Chalaropsis species. Identification of
RT   aspartyl and glutamyl residues in the active site.";
RL   J. Biol. Chem. 253:6787-6793(1978).
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, extracellular space.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. {ECO:0000305}.
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DR   PIR; A00876; MUKAD.
DR   AlphaFoldDB; P00721; -.
DR   SMR; P00721; -.
DR   CAZy; GH25; Glycoside Hydrolase Family 25.
DR   GO; GO:0005615; C:extracellular space; 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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
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   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SMART; SM00641; Glyco_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Secreted.
FT   CHAIN           1..211
FT                   /note="N,O-diacetylmuramidase"
FT                   /id="PRO_0000208263"
FT   ACT_SITE        6
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065,
FT                   ECO:0000269|PubMed:567645"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
FT   DISULFID        108..147
FT                   /evidence="ECO:0000269|PubMed:1168638"
SQ   SEQUENCE   211 AA;  22414 MW;  379D758A383EC38C CRC64;
     TVQGFDISSY QPSVNFAGAY SAGARFVIIK ATEGTSYTNP SFSSQYNGAT TATGNYFIRG
     GYHFAHPGET TGAAQADYFI AHGGGWSGDG ITLPGMLDLE SEGSNPACWG LSAASMVAWI
     KAFSDRYHAV TGRYPMLYTN PSWWSSCTGN SNAFVNTNPL VLANRYASAP GTIPGGWPYQ
     TIWQNSDAYA YGGSNNFING SIDNLKKLAT G