ID   ENLYS_BPSPP             Reviewed;         271 AA.
AC   O48471;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   02-DEC-2020, entry version 76.
DE   RecName: Full=Endolysin {ECO:0000303|PubMed:27328857};
DE            EC=3.5.1.-;
DE   AltName: Full=LysSPP1 {ECO:0000303|PubMed:27328857};
DE   AltName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000305};
GN   Name=25;
OS   Bacillus phage SPP1 (Bacteriophage SPP1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=10724;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA   Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT   "The complete nucleotide sequence and functional organization of Bacillus
RT   subtilis bacteriophage SPP1.";
RL   Gene 204:201-212(1997).
RN   [2]
RP   FUNCTION.
RX   PubMed=27328857; DOI=10.1111/mmi.13448;
RA   Fernandes S., Sao-Jose C.;
RT   "More than a hole: the holin lethal function may be required to fully
RT   sensitize bacteria to the lytic action of canonical endolysins.";
RL   Mol. Microbiol. 102:92-106(2016).
CC   -!- FUNCTION: Endolysin that degrades host peptidoglycans and participates
CC       with the holin protein(s) in the sequential events which lead to the
CC       programmed host cell lysis releasing the mature viral particles. Once
CC       the holin(s) has permeabilized the host cell membrane, the endolysin
CC       can reach the periplasm and break down the peptidoglycan layer.
CC       {ECO:0000305|PubMed:27328857}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Note=The endolysin is
CC       cytoplasmic, but can reach the periplasmic space with the help of the
CC       holins which disrupt the host cell membrane. {ECO:0000305}.
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DR   EMBL; X97918; CAA66518.1; -; Genomic_DNA.
DR   PIR; T42311; T42311.
DR   RefSeq; NP_690702.1; NC_004166.2.
DR   SMR; O48471; -.
DR   GeneID; 955352; -.
DR   KEGG; vg:955352; -.
DR   Proteomes; UP000002559; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046729; C:viral procapsid; IDA:CACAO.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; 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   CDD; cd02696; MurNAc-LAA; 1.
DR   InterPro; IPR044081; DUF5776.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF19087; DUF5776; 1.
DR   SMART; SM00646; Ami_3; 1.
PE   4: Predicted;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus;
KW   Host cytoplasm; Hydrolase; Reference proteome;
KW   Viral release from host cell.
FT   CHAIN           1..271
FT                   /note="Endolysin"
FT                   /id="PRO_0000439629"
FT   DOMAIN          5..178
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   271 AA;  29882 MW;  4E5223BED61737AA CRC64;
     MSKLVWLDAG HGGKDSGAAA NGIKEKDIVL KIVKKVKSIL TSRYEVAVKL TRDSDVFYEL
     IDRARKANAA KADLFVSVHI NATPGGKGFE TYRYVKTSAS SSTGQQQKVL HDAIYKRIKK
     YGIKDRGEKA ADLSVLRNTS MPAVLTENLF IDNKDEAALL KKDSFLNDVA EGHAEGIAEI
     LNLKKKSGGS APKKEDKPSS GKTKMVIVKD NPDGFLWVYN KADWNARYKK VKPDEAFTID
     KTVTVNGSKM YKLKSGLYIT AASKYVTVKE K