ID LYS_BPCP1 Reviewed; 339 AA. AC P15057; Q38009; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 08-NOV-2023, entry version 142. DE RecName: Full=Lysozyme; DE EC=3.2.1.17; DE AltName: Full=CP-1 lysin; DE AltName: Full=Endolysin; DE AltName: Full=Muramidase; GN Name=CPL1; Synonyms=22; OS Streptococcus phage Cp-1 (Bacteriophage Cp-1). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Salasmaviridae; Cepunavirus; Cepunavirus Cp1. OX NCBI_TaxID=10747; OH NCBI_TaxID=1313; Streptococcus pneumoniae. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3422470; DOI=10.1073/pnas.85.3.914; RA Garcia E., Garcia J.L., Garcia P., Arraras A., Sanchez-Puelles J.M., RA Lopez R.; RT "Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its RT bacteriophages."; RL Proc. Natl. Acad. Sci. U.S.A. 85:914-918(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8648702; DOI=10.1128/jvi.70.6.3678-3687.1996; RA Martin A.C., Lopez R., Garcia P.; RT "Analysis of the complete nucleotide sequence and functional organization RT of the genome of Streptococcus pneumoniae bacteriophage Cp-1."; RL J. Virol. 70:3678-3687(1996). RN [3] RP MUTAGENESIS OF ASP-10 AND GLU-37. RX PubMed=1390634; DOI=10.1021/bi00151a016; RA Sanz J.M., Garcia P., Garcia J.L.; RT "Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1 RT lysozyme: an evolutionary perspective of lysozyme mechanism."; RL Biochemistry 31:8495-8499(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH RP CHOLINE, AND MUTAGENESIS OF ASP-92; GLU-94 AND ASP-182. RX PubMed=14527392; DOI=10.1016/j.str.2003.09.005; RA Hermoso J.A., Monterroso B., Albert A., Galan B., Ahrazem O., Garcia P., RA Martinez-Ripoll M., Garcia J.L., Menendez M.; RT "Structural basis for selective recognition of pneumococcal cell wall by RT modular endolysin from phage Cp-1."; RL Structure 11:1239-1249(2003). 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 -!- INTERACTION: CC P15057; P67413: udk; Xeno; NbExp=2; IntAct=EBI-11615908, EBI-11615933; CC -!- DOMAIN: The C-terminal domain comprising the repeats is involved in CC choline binding. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J03586; AAA32204.1; -; Genomic_DNA. DR EMBL; Z47794; CAA87744.1; -; Genomic_DNA. DR PIR; A31086; MUBPCP. DR RefSeq; NP_044837.1; NC_001825.1. DR PDB; 1H09; X-ray; 2.10 A; A=2-339. DR PDB; 1OBA; X-ray; 2.45 A; A=1-339. DR PDB; 2IXU; X-ray; 2.28 A; A=1-339. DR PDB; 2IXV; X-ray; 1.96 A; A=1-339. DR PDB; 2J8F; X-ray; 1.84 A; A=1-339. DR PDB; 2J8G; X-ray; 1.69 A; A=1-339. DR PDBsum; 1H09; -. DR PDBsum; 1OBA; -. DR PDBsum; 2IXU; -. DR PDBsum; 2IXV; -. DR PDBsum; 2J8F; -. DR PDBsum; 2J8G; -. DR SMR; P15057; -. DR IntAct; P15057; 1. DR CAZy; GH25; Glycoside Hydrolase Family 25. DR GeneID; 1261221; -. DR KEGG; vg:1261221; -. DR OrthoDB; 5812at10239; -. DR EvolutionaryTrace; P15057; -. DR PRO; PR:P15057; -. DR Proteomes; UP000009089; Genome. DR GO; GO:0003796; F:lysozyme activity; IDA:CACAO. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO. DR CDD; cd06415; GH25_Cpl1-like; 1. DR Gene3D; 2.10.270.10; Cholin Binding; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 1. 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; (Trans)glycosidases; 1. DR SUPFAM; SSF69360; Cell wall binding repeat; 1. DR PROSITE; PS51170; CW; 5. 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 Reference proteome; Repeat. FT CHAIN 1..339 FT /note="Lysozyme" FT /id="PRO_0000208259" FT DOMAIN 5..206 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" FT MUTAGEN 10 FT /note="D->A,E,H,K,N: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:1390634" FT MUTAGEN 37 FT /note="E->A: 95% loss of activity." FT /evidence="ECO:0000269|PubMed:1390634" FT MUTAGEN 37 FT /note="E->D: 63% loss of activity." FT /evidence="ECO:0000269|PubMed:1390634" FT MUTAGEN 37 FT /note="E->K: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:1390634" FT MUTAGEN 37 FT /note="E->Q: 13% loss of activity." FT /evidence="ECO:0000269|PubMed:1390634" FT MUTAGEN 92 FT /note="D->A: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:14527392" FT MUTAGEN 94 FT /note="E->A,Q: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:14527392" FT MUTAGEN 182 FT /note="D->A: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:14527392" FT CONFLICT 44 FT /note="P -> R (in Ref. 2; AAA32204)" FT /evidence="ECO:0000305" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 20..26 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 30..37 FT /evidence="ECO:0007829|PDB:2J8G" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 53..61 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 68..80 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 101..117 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 120..127 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 128..134 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 171..177 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 179..188 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 200..204 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 290..295 FT /evidence="ECO:0007829|PDB:2J8G" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 302..309 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:2J8G" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:1H09" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:2J8G" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:2J8G" SQ SEQUENCE 339 AA; 39190 MW; E2947566AC676B05 CRC64; MVKKNDLFVD VSSHNGYDIT GILEQMGTTN TIIKISESTT YLNPCLSAQV EQSNPIGFYH FARFGGDVAE AEREAQFFLD NVPMQVKYLV LDYEDDPSGD AQANTNACLR FMQMIADAGY KPIYYSYKPF THDNVDYQQI LAQFPNSLWI AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDDKPKTAG TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK WYYLKDNGAM ATGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA //