ID   AEPE_BPA18              Reviewed;         281 AA.
AC   Q37976; Q9T199;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   02-DEC-2020, entry version 84.
DE   RecName: Full=L-alanyl-D-glutamate peptidase;
DE            EC=3.4.24.-;
GN   Name=ply; Synonyms=ply118;
OS   Listeria phage A118 (Bacteriophage A118).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=40521;
OH   NCBI_TaxID=1639; Listeria monocytogenes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8577256; DOI=10.1111/j.1365-2958.1995.tb02345.x;
RA   Loessner M.J., Wendlinger G., Scherer S.;
RT   "Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new
RT   class of enzymes and evidence for conserved holin genes within the
RT   siphoviral lysis cassettes.";
RL   Mol. Microbiol. 16:1231-1241(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10652093; DOI=10.1046/j.1365-2958.2000.01720.x;
RA   Loessner M.J., Inman R.B., Lauer P., Calendar R.;
RT   "Complete nucleotide sequence, molecular analysis and genome structure of
RT   bacteriophage A118 of Listeria monocytogenes: implications for phage
RT   evolution.";
RL   Mol. Microbiol. 35:324-340(2000).
CC   -!- FUNCTION: Cell wall lytic enzyme. Hydrolyzes the link between L-alanine
CC       and D-glutamate residues in certain bacterial cell-wall glycopeptides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Expressed at about 20 minutes after infection.
CC   -!- SIMILARITY: Belongs to the peptidase M15C family. {ECO:0000305}.
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DR   EMBL; X85008; CAA59362.1; -; Genomic_DNA.
DR   EMBL; AJ242593; CAB53811.1; -; Genomic_DNA.
DR   PIR; S69799; S69799.
DR   RefSeq; NP_463486.1; NC_003216.1.
DR   SMR; Q37976; -.
DR   MEROPS; M15.020; -.
DR   GeneID; 922391; -.
DR   KEGG; vg:922391; -.
DR   Proteomes; UP000002666; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR044081; DUF5776.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR039561; Peptidase_M15C.
DR   Pfam; PF19087; DUF5776; 1.
DR   Pfam; PF13539; Peptidase_M15_4; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..281
FT                   /note="L-alanyl-D-glutamate peptidase"
FT                   /id="PRO_0000217835"
FT   CONFLICT        24
FT                   /note="A -> R (in Ref. 1; CAA59362)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  30799 MW;  9CADC9F02F54CB41 CRC64;
     MTSYYYSRSL ANVNKLADNT KAAARKLLDW SESNGIEVLI YETIRTKEQQ AANVNSGASQ
     TMRSYHLVGQ ALDFVMAKGK TVDWGAYRSD KGKKFVAKAK SLGFEWGGDW SGFVDNPHLQ
     FNYKGYGTDT FGKGASTSNS SKPSADTNTN SLGLVDYMNL NKLDSSFANR KKLATSYGIK
     NYSGTATQNT TLLAKLKAGK PHTPASKNTY YTENPRKVKT LVQCDLYKSV DFTTKNQTGG
     TFPPGTVFTI SGMGKTKGGT PRLKTKSGYY LTANTKFVKK I