ID   LYS_BPCP7               Reviewed;         342 AA.
AC   P19385;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   29-SEP-2021, entry version 100.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=CP-7 lysin;
DE   AltName: Full=Endolysin;
DE   AltName: Full=Muramidase;
GN   Name=CPL7;
OS   Streptococcus phage Cp-7 (Bacteriophage Cp-7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Cepunavirus.
OX   NCBI_TaxID=10748;
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).
RN   [2]
RP   SEQUENCE REVISION TO 63; 114; 230; 278 AND 326.
RA   Garcia P., Garcia J.L., Garcia E., Sanchez-Puelles J.M., Lopez R.;
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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. Degrades cell walls containing either
CC       choline or ethanolamine.
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 could be responsible for the substrate
CC       recognition.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR   EMBL; M34779; AAA72844.2; -; Genomic_DNA.
DR   PIR; JQ0437; MUBPC7.
DR   PDB; 4CVD; X-ray; 1.67 A; A=253-300.
DR   PDB; 5I8L; X-ray; 2.80 A; A=199-342.
DR   PDBsum; 4CVD; -.
DR   PDBsum; 5I8L; -.
DR   SMR; P19385; -.
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; IPR013168; Cpl_7_lyso_C.
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; PF08230; CW_7; 3.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SMART; SM01095; Cpl-7; 3.
DR   SMART; SM00641; Glyco_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase;
KW   Repeat.
FT   CHAIN           1..342
FT                   /note="Lysozyme"
FT                   /id="PRO_0000208260"
FT   DOMAIN          5..210
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   REPEAT          205..242
FT                   /note="1; truncated"
FT   REPEAT          243..290
FT                   /note="2"
FT   REPEAT          291..338
FT                   /note="3"
FT   REGION          205..338
FT                   /note="3 X 48 AA tandem repeats"
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"
FT   HELIX           205..214
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   HELIX           220..229
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   HELIX           234..247
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   HELIX           254..262
FT                   /evidence="ECO:0007829|PDB:4CVD"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:4CVD"
FT   HELIX           269..277
FT                   /evidence="ECO:0007829|PDB:4CVD"
FT   HELIX           282..295
FT                   /evidence="ECO:0007829|PDB:4CVD"
FT   HELIX           301..310
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   TURN            311..313
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   HELIX           317..326
FT                   /evidence="ECO:0007829|PDB:5I8L"
FT   HELIX           330..339
FT                   /evidence="ECO:0007829|PDB:5I8L"
SQ   SEQUENCE   342 AA;  38248 MW;  6B1F431DD068CC52 CRC64;
     MVKKNDLFVD VASHQGYDIS GILEEAGTTN TIIKVSESTS YLNPCLSAQV SQSNPIGFYH
     FAWFGGNEEE AEAEARYFLD NVPTQVKYLV LDYEDHASAS VQRNTTACLR FMQIIAEAGY
     TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP
     FDKNIVLLDD EKEDNINNEN TLKSLTTVAN EVIQGLWGNG QERYDSLANA GYDPQAVQDK
     VNEILNAREI ADLTTVANEV IQGLWGNGQE RYDSLANAGY DPQAVQDKVN EILNAREIAD
     LTTVANEVIQ GLWGNGQERY DSLANAGYDP QAVQDKVNEL LS