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 07-NOV-2018, entry version 80. 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. Hydrolyzes the link between L- CC alanine and D-glutamate residues in certain bacterial cell-wall CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; -. 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: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 Pfam; PF13539; Peptidase_M15_4; 1. 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 //