ID   LYS_CLOPE               Reviewed;         342 AA.
AC   P26836;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   02-SEP-2026, entry version 137.
DE   RecName: Full=Probable autolytic lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   AltName: Full=Autolysin;
GN   Name=lyc; OrderedLocusNames=CPE0382;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 256-342.
RC   STRAIN=CPN50;
RX   PubMed=8177218; DOI=10.1007/bf00280319;
RA   Canard B., Garnier T., Saint-Joanis B., Cole S.T.;
RT   "Molecular genetic analysis of the nagH gene encoding a hyaluronidase of
RT   Clostridium perfringens.";
RL   Mol. Gen. Genet. 243:215-224(1994).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. {ECO:0000305}.
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DR   EMBL; BA000016; BAB80088.1; -; Genomic_DNA.
DR   EMBL; M81878; AAA23261.1; -; Genomic_DNA.
DR   PIR; S43906; S43906.
DR   RefSeq; WP_011009775.1; NC_003366.1.
DR   AlphaFoldDB; P26836; -.
DR   SMR; P26836; -.
DR   STRING; 195102.gene:10489638; -.
DR   KEGG; cpe:CPE0382; -.
DR   HOGENOM; CLU_805866_0_0_9; -.
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; cd06525; GH25_Lyc-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR008270; Glyco_hydro_25_AS.
DR   InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR34135; LYSOZYME; 1.
DR   PANTHER; PTHR34135:SF2; LYSOZYME; 1.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   Pfam; PF08239; SH3_3; 2.
DR   SMART; SM00641; Glyco_25; 1.
DR   SMART; SM00287; SH3b; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
DR   PROSITE; PS51781; SH3B; 2.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase; Repeat.
FT   CHAIN           1..342
FT                   /note="Probable autolytic lysozyme"
FT                   /id="PRO_0000208265"
FT   DOMAIN          212..276
FT                   /note="SH3b 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   REPEAT          230..252
FT                   /note="1"
FT   REPEAT          253..272
FT                   /note="2"
FT   REPEAT          273..295
FT                   /note="3"
FT   DOMAIN          278..342
FT                   /note="SH3b 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   REPEAT          296..318
FT                   /note="4"
FT   REPEAT          319..342
FT                   /note="5"
FT   REGION          230..342
FT                   /note="5 X 23 AA tandem repeats"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
SQ   SEQUENCE   342 AA;  39558 MW;  EC3B4078A2FB4732 CRC64;
     MEGRNSNNLK GIDVSNWQGN INFKSVKNEG IEVVYIKATE GDYFKDSYAK QNYKRAKAEG
     LKVGFYHFFK PNKNAKRQAK YFIDYLNEIG ATDYDCKLAL DVETTEGRSA YELTTMCIEF
     LEEVRKITNR EVVVYTYTSF ANNNLDNRLG VYPLWIAEYG VKAPKDNRVW SSWIGFQYSD
     KGNVAGVSGN CDMNEFKEEI LDVKNNFKLY NATTKNISTY LNIREKGEID SKIIGKIPAG
     EEFMIKWVDS NYLGWYLIEY KNITGYVSSK YVEKFQMATT YNVSDFLNVR ERGTTDSKVV
     AIIDDGEIFR IDWVDSDYIG WYRITTKYGK NGFVKADFVK KI
//