ID   ALYS_BPDP1              Reviewed;         296 AA.
AC   O03979;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   13-SEP-2023, entry version 96.
DE   RecName: Full=Lysin;
DE            EC=3.5.1.28;
DE   AltName: Full=Cell wall hydrolase;
DE   AltName: Full=Lytic amidase;
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase;
GN   Name=PAL;
OS   Pneumococcus phage Dp-1 (Bacteriophage Dp-1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=59241;
OH   NCBI_TaxID=1313; Streptococcus pneumoniae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9379901; DOI=10.1046/j.1365-2958.1997.5101880.x;
RA   Sheehan M.M., Garcia J.L., Lopez R., Garcia P.;
RT   "The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of
RT   intergeneric origin.";
RL   Mol. Microbiol. 25:717-725(1997).
RN   [2]
RP   USE OF PAL IN ERADICATION OF S.PNEUMONIAE.
RX   PubMed=11739958; DOI=10.1126/science.1066869;
RA   Loeffler J.M., Nelson D., Fischetti V.A.;
RT   "Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall
RT   hydrolase.";
RL   Science 294:2170-2172(2001).
CC   -!- FUNCTION: Lysis of bacterial host cell wall.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Host cell wall. Note=Binds to the choline
CC       residues present in the cell wall substrate.
CC   -!- PHARMACEUTICAL: May have a use in the prevention of pneumococcal
CC       disease. Pal acts very effectively in killing 15 common serotypes of
CC       pneumococci, including highly penicillin-resistant strains. It could be
CC       used to eliminate the nasopharyngeal reservoir of these bacteria.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284}.
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DR   EMBL; Z93946; CAB07986.1; -; Genomic_DNA.
DR   RefSeq; YP_004306947.1; NC_015274.1.
DR   SMR; O03979; -.
DR   GeneID; 10358655; -.
DR   KEGG; vg:10358655; -.
DR   OrthoDB; 3568at10239; -.
DR   GO; GO:0044158; C:host cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO.
DR   Gene3D; 2.10.270.10; Cholin Binding; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 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; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR008044; Phage_lysin.
DR   Pfam; PF05382; Amidase_5; 1.
DR   Pfam; PF01473; Choline_bind_1; 2.
DR   Pfam; PF19127; Choline_bind_3; 1.
DR   SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS51170; CW; 6.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Hydrolase; Pharmaceutical; Protease; Repeat; Thiol protease.
FT   CHAIN           1..296
FT                   /note="Lysin"
FT                   /id="PRO_0000164428"
FT   DOMAIN          1..142
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REPEAT          152..171
FT                   /note="Cell wall-binding 1"
FT   REPEAT          173..194
FT                   /note="Cell wall-binding 2"
FT   REPEAT          196..216
FT                   /note="Cell wall-binding 3"
FT   REPEAT          217..236
FT                   /note="Cell wall-binding 4"
FT   REPEAT          237..256
FT                   /note="Cell wall-binding 5"
FT   REPEAT          259..278
FT                   /note="Cell wall-binding 6"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   296 AA;  34453 MW;  C17F0911B7D46CC1 CRC64;
     MGVDIEKGVA WMQARKGRVS YSMDFRDGPD SYDCSSSMYY ALRSAGASSA GWAVNTEYMH
     AWLIENGYEL ISENAPWDAK RGDIFIWGRK GASAGAGGHT GMFIDSDNII HCNYAYDGIS
     VNDHDERWYY AGQPYYYVYR LTNANAQPAE KKLGWQKDAT GFWYARANGT YPKDEFEYIE
     ENKSWFYFDD QGYMLAEKWL KHTDGNWYWF DRDGYMATSW KRIGESWYYF NRDGSMVTGW
     IKYYDNWYYC DATNGDMKSN AFIRYNDGWY LLLPDGRLAD KPQFTVEPDG LITAKV
//