ID   LYS_BPCP9               Reviewed;         339 AA.
AC   P19386;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   29-SEP-2021, entry version 104.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=CP-9 lysin;
DE   AltName: Full=Endolysin;
DE   AltName: Full=Muramidase;
GN   Name=CPL9;
OS   Streptococcus phage Cp-9 (Bacteriophage Cp-9).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Cepunavirus.
OX   NCBI_TaxID=10749;
OH   NCBI_TaxID=1313; Streptococcus pneumoniae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2311937; DOI=10.1016/0378-1119(90)90116-9;
RA   Garcia P., Garcia J.L., Garcia E., Sanchez-Puelles J.M., Lopez R.;
RT   "Modular organization of the lytic enzymes of Streptococcus pneumoniae and
RT   its bacteriophages.";
RL   Gene 86:81-88(1990).
CC   -!- FUNCTION: Responsible for the separation of the host daughter cells at
CC       the end of cell division and participates in the liberation of progeny
CC       bacteriophage into the medium. Strictly depends on the presence of
CC       choline-containing cell walls for activity.
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   -!- DOMAIN: The C-terminal domain comprising the repeats is involved in
CC       choline binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR   EMBL; M34780; AAA72845.1; -; Genomic_DNA.
DR   PIR; JQ0438; MUBPC9.
DR   SMR; P19386; -.
DR   CAZy; GH25; Glycoside Hydrolase Family 25.
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; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF01473; Choline_bind_1; 2.
DR   Pfam; PF19127; Choline_bind_3; 1.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SMART; SM00641; Glyco_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51170; CW; 5.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase; Repeat.
FT   CHAIN           1..339
FT                   /note="Lysozyme"
FT                   /id="PRO_0000208261"
FT   DOMAIN          5..201
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   REPEAT          200..219
FT                   /note="Cell wall-binding 1"
FT   REPEAT          220..239
FT                   /note="Cell wall-binding 2"
FT   REPEAT          241..260
FT                   /note="Cell wall-binding 3"
FT   REPEAT          261..280
FT                   /note="Cell wall-binding 4"
FT   REPEAT          281..300
FT                   /note="Cell wall-binding 5"
FT   REPEAT          303..322
FT                   /note="Cell wall-binding 6"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
SQ   SEQUENCE   339 AA;  39151 MW;  A2143F05BDED4EDD CRC64;
     MVKKNDLFID VSSHNGYDIT GILEQMGTTN TIVKISESTT YLNPCLSAQV EQSTPIGFYH
     FARFGGDVAE AEREAQFFLD NVPTQVKYLV LDYEDDPSGN AQANTNACLR FMQMIADAGY
     TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI AGYGLNDGNA DFEYFPSMDG IRWWQYSSNP
     FDKNIVLLDD EEDEKPKTAG TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL
     TSEWLKDNEK WYYLKDNGAM VTGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN
     MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA