ID   LYS_ARTBC               Reviewed;         235 AA.
AC   D4ANU4;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=N,O-diacetylmuramidase {ECO:0000250|UniProtKB:P00721};
DE            EC=3.2.1.17 {ECO:0000250|UniProtKB:P00721};
DE   AltName: Full=Lysozyme CH {ECO:0000250|UniProtKB:P00721};
DE   Flags: Precursor;
GN   ORFNames=ARB_05911;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: This enzyme has both lysozyme (acetylmuramidase) and
CC       diacetylmuramidase activities. {ECO:0000250|UniProtKB:P00721}.
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; Evidence={ECO:0000250|UniProtKB:P00721};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC       ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR   EMBL; ABSU01000004; EFE34955.1; -; Genomic_DNA.
DR   RefSeq; XP_003015600.1; XM_003015554.1.
DR   AlphaFoldDB; D4ANU4; -.
DR   SMR; D4ANU4; -.
DR   STRING; 663331.D4ANU4; -.
DR   EnsemblFungi; EFE34955; EFE34955; ARB_05911.
DR   GeneID; 9525881; -.
DR   KEGG; abe:ARB_05911; -.
DR   eggNOG; ENOG502S19Y; Eukaryota.
DR   HOGENOM; CLU_044973_4_0_1; -.
DR   OMA; GSYNVGM; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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: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; 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; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..235
FT                   /note="N,O-diacetylmuramidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434503"
FT   DOMAIN          29..235
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   DISULFID        132..171
FT                   /evidence="ECO:0000250|UniProtKB:P00721"
SQ   SEQUENCE   235 AA;  25164 MW;  1E59288EC2B5E79C CRC64;
     MKLSLLTVAA AAGAAVAAPA AEIDTRAGSV QGFDISGYQP NVDFRAAYNG GARFVMIKAT
     EGTTFKSSTF NSQYTGATNN KFIRGGYHFA HPDTSATAQC DYFLANGGGW SNDGITLPGM
     IDLEGTSGKP KCYGLSASAM IAWIKAFSDR YNAKTGRYPM IYTSPDWWQS CTGNTKTFGT
     TIPLVLARWA SSPGTPPGGW PYHTFWQNAD TYRFGGDSEI FNGGMDQLQR FAKGG