ID   ENLYS_BPA51             Reviewed;         341 AA.
AC   Q38653;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 83.
DE   RecName: Full=Endolysin;
DE            EC=3.5.1.28;
DE   AltName: Full=Probable N-acetylmuramoyl-L-alanine amidase;
GN   Name=PLY511;
OS   Listeria phage A511 (Bacteriophage A511).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Herelleviridae; Jasinkavirinae; Pecentumvirus.
OX   NCBI_TaxID=40523;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at about 20 minutes after infection.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X85010; CAA59368.1; -; Genomic_DNA.
DR   PIR; S69802; S69802.
DR   RefSeq; YP_001468459.1; NC_009811.2.
DR   SMR; Q38653; -.
DR   MEROPS; M15.950; -.
DR   GeneID; 5601499; -.
DR   KEGG; vg:5601499; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF158634; RPA2825-like; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Hydrolase; Repeat; Secreted.
FT   CHAIN           1..341
FT                   /note="Endolysin"
FT                   /id="PRO_0000164405"
FT   DOMAIN          23..153
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   REGION          175..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  36477 MW;  86C40B73F0FD8547 CRC64;
     MVKYTVENKI IAGLPKGKLK GANFVIAHET ANSKSTIDNE VSYMTRNWKN AFVTHFVGGG
     GRVVQVANVN YVSWGAGQYA NSYSYAQVEL CRTSNATTFK KDYEVYCQLL VDLAKKAGIP
     ITLDSGSKTS DKGIKSHKWV ADKLGGTTHQ DPYAYLSSWG ISKAQFASDL AKVSGGGNTG
     TAPAKPSTPA PKPSTPSTNL DKLGLVDYMN AKKMDSSYSN RDKLAKQYGI ANYSGTASQN
     TTLLSKIKGG APKPSTPAPK PSTSTAKKIY FPPNKGNWSV YPTNKAPVKA NAIGAINPTK
     FGGLTYTIQK DRGNGVYEIQ TDQFGRVQVY GAPSTGAVIK K
//