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   05-OCT-2016, entry version 75.
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; dsDNA viruses, no RNA stage; 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
RT   new 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.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes the link between L-alanine and D-
CC       glutamate residues in certain bacterial cell-wall glycopeptides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Expressed at about 20 minutes after
CC       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   PDBsum; 2VO9; -.
DR   ProteinModelPortal; Q37979; -.
DR   MEROPS; M15.021; -.
DR   GeneID; 5601386; -.
DR   KEGG; vg:5601386; -.
DR   KO; K17733; -.
DR   EvolutionaryTrace; Q37979; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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_dom.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Hydrolase; Secreted.
FT   CHAIN         1    289       L-alanyl-D-glutamate peptidase.
FT                                /FTId=PRO_0000217836.
FT   HELIX         5     16       {ECO:0000244|PDB:2VO9}.
FT   HELIX        23     37       {ECO:0000244|PDB:2VO9}.
FT   TURN         38     40       {ECO:0000244|PDB:2VO9}.
FT   STRAND       43     47       {ECO:0000244|PDB:2VO9}.
FT   HELIX        52     60       {ECO:0000244|PDB:2VO9}.
FT   TURN         61     63       {ECO:0000244|PDB:2VO9}.
FT   STRAND       64     67       {ECO:0000244|PDB:2VO9}.
FT   HELIX        79     82       {ECO:0000244|PDB:2VO9}.
FT   STRAND       85     91       {ECO:0000244|PDB:2VO9}.
FT   STRAND       95     99       {ECO:0000244|PDB:2VO9}.
FT   STRAND      102    104       {ECO:0000244|PDB:2VO9}.
FT   HELIX       105    116       {ECO:0000244|PDB:2VO9}.
FT   HELIX       122    124       {ECO:0000244|PDB:2VO9}.
FT   STRAND      125    128       {ECO:0000244|PDB:2VO9}.
FT   STRAND      133    137       {ECO:0000244|PDB:2VO9}.
FT   HELIX       139    141       {ECO:0000244|PDB:2VO9}.
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
//