ID   A4F7M2_SACEN            Unreviewed;       241 AA.
AC   A4F7M2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN   OrderedLocusNames=SACE_0704 {ECO:0000313|EMBL:CAM00046.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM00046.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM00046.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- FUNCTION: This enzyme has both lysozyme (acetylmuramidase) and
CC       diacetylmuramidase activities. {ECO:0000256|ARBA:ARBA00055588}.
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:0000256|ARBA:ARBA00000632};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000256|ARBA:ARBA00010646, ECO:0000256|PROSITE-ProRule:PRU01252}.
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DR   EMBL; AM420293; CAM00046.1; -; Genomic_DNA.
DR   RefSeq; WP_009950544.1; NC_009142.1.
DR   AlphaFoldDB; A4F7M2; -.
DR   STRING; 405948.SACE_0704; -.
DR   GeneID; 306457609; -.
DR   KEGG; sen:SACE_0704; -.
DR   eggNOG; COG3757; Bacteria.
DR   HOGENOM; CLU_044973_4_0_11; -.
DR   OrthoDB; 287365at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06412; GH25_CH-type; 1.
DR   FunFam; 3.20.20.80:FF:000060; Lysozyme M1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR018077; Glyco_hydro_fam25_subgr.
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; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   3: Inferred from homology;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529, ECO:0000256|PROSITE-
KW   ProRule:PRU01252};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638, ECO:0000256|PROSITE-
KW   ProRule:PRU01252}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01252};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01252}; Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
SQ   SEQUENCE   241 AA;  25817 MW;  8764B2832F0B8D8D CRC64;
     MNIRRKLLVV LASSAALLAS VPGAANADSA AADALGIDVS NHNGEVDFAK VGADGRDFAF
     VLATDGESFT SDLFDSQYSG AGEAGLYRAG YHFARPDGSA TKQADRFLKT VGYTNDGRTM
     PPVLDMEANP NGATCYGLDD AQMEEWIKSF VGRVKEKTGR EAVIYTSPSF WKECTGNSEA
     FTSNPLWTAE WDVDKPSKVG GWPAHTFWQY SNSGKVDGVD GAVDVNRFNG GTAELEKFVK
     G
//