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AEPE_BPA50
ID   AEPE_BPA50              Reviewed;         289 AA.
AC   Q37979;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=L-alanyl-D-glutamate peptidase;
DE            EC=3.4.24.-;
GN   Name=ply; Synonyms=ply500;
OS   Listeria phage A500 (Bacteriophage A500).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=40522;
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).
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; X85009; CAA59365.1; -; Genomic_DNA.
DR   PIR; S69801; S69801.
DR   RefSeq; YP_001468411.1; NC_009810.1.
DR   PDB; 2VO9; X-ray; 1.80 A; A/B/C=1-167.
DR   PDB; 6HX0; X-ray; 1.59 A; A=133-289.
DR   PDBsum; 2VO9; -.
DR   PDBsum; 6HX0; -.
DR   SMR; Q37979; -.
DR   MEROPS; M15.021; -.
DR   GeneID; 5601386; -.
DR   KEGG; vg:5601386; -.
DR   EvolutionaryTrace; Q37979; -.
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; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR039561; Peptidase_M15C.
DR   InterPro; IPR041341; PSA_CBD.
DR   Pfam; PF13539; Peptidase_M15_4; 1.
DR   Pfam; PF18341; PSA_CBD; 2.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Hydrolase; Secreted.
FT   CHAIN           1..289
FT                   /note="L-alanyl-D-glutamate peptidase"
FT                   /id="PRO_0000217836"
FT   HELIX           5..16
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           23..37
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           105..116
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:2VO9"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          165..173
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          195..203
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          206..211
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          227..231
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          260..264
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          267..275
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   STRAND          279..283
FT                   /evidence="ECO:0007829|PDB:6HX0"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:6HX0"
SQ   SEQUENCE   289 AA;  33424 MW;  1CD6B52B37260A6A CRC64;
     MALTEAWLIE KANRKLNAGG MYKITSDKTR NVIKKMAKEG IYLCVAQGYR STAEQNALYA
     QGRTKPGAIV TNAKGGQSNH NYGVAVDLCL YTNDGKDVIW ESTTSRWKKV VAAMKAEGFK
     WGGDWKSFKD YPHFELCDAV SGEKIPAATQ NTNTNSNRYE GKVIDSAPLL PKMDFKSSPF
     RMYKVGTEFL VYDHNQYWYK TYIDDKLYYM YKSFCDVVAK KDAKGRIKVR IKSAKDLRIP
     VWNNIKLNSG KIKWYAPNVK LAWYNYRRGY LELWYPNDGW YYTAEYFLK
 
 
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