ID   Q81AW1_BACCR            Unreviewed;       245 AA.
AC   Q81AW1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   SubName: Full=Lysozyme M1 {ECO:0000313|EMBL:AAP10376.1};
DE            EC=3.2.1.17 {ECO:0000313|EMBL:AAP10376.1};
GN   OrderedLocusNames=BC_3441 {ECO:0000313|EMBL:AAP10376.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10376.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP10376.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP10376.1; -; Genomic_DNA.
DR   RefSeq; WP_000727665.1; NC_004722.1.
DR   AlphaFoldDB; Q81AW1; -.
DR   SMR; Q81AW1; -.
DR   GeneID; 50194219; -.
DR   KEGG; bce:BC3441; -.
DR   PATRIC; fig|226900.8.peg.3529; -.
DR   HOGENOM; CLU_044973_6_2_9; -.
DR   OrthoDB; 9802228at2; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06413; GH25_muramidase_1; 1.
DR   FunFam; 3.20.20.80:FF:000209; Glycoside hydrolase family 25; 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|PROSITE-ProRule:PRU01252};
KW   Bacteriolytic enzyme {ECO:0000256|PROSITE-ProRule:PRU01252};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01252};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01252}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01252"
SQ   SEQUENCE   245 AA;  28833 MW;  7DA662E34FBA9FAA CRC64;
     MKKKLFIGGI FTLISVISVV VYLVFQGIFI PNQISADKYE IKGVDVASYQ GDIDWRELEK
     QNMKFAFIKA TEGSSFVDEY FSKNWRNANK TDMRIGAYHF FSFDSKGETQ AEQFIRTVPK
     YKQALPPVID VEFYANKKDN PPKREDVTKE LAVMIEMLEK HYDKKVILYA TQEAYDLYIK
     DAYPKCNIWI RSVLTKPSLS DERKWTFWQY TNRGRLSGYN GKEKYIDLNV FYGNEEEFEN
     YGMKD
//