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   06-FEB-2013, entry version 62.
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   MEDLINE=96020653; PubMed=8577256;
RX   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.
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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   SMR; Q37979; 1-148, 155-289.
DR   MEROPS; M15.021; -.
DR   GeneID; 5601386; -.
DR   ProtClustDB; CLSP988457; -.
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:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.1380.10; Hedgehog/DD-pept_Zn-bd; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom.
DR   InterPro; IPR003709; Pept_M15B/M15C.
DR   Pfam; PF02557; VanY; 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
FT   HELIX        23     37
FT   TURN         38     40
FT   STRAND       43     47
FT   HELIX        52     60
FT   TURN         61     63
FT   STRAND       64     67
FT   HELIX        79     82
FT   STRAND       85     91
FT   STRAND       95     99
FT   STRAND      102    104
FT   HELIX       105    116
FT   HELIX       122    124
FT   STRAND      125    128
FT   STRAND      133    137
FT   HELIX       139    141
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
//