ID   D2XS97_9CAUD            Unreviewed;       429 AA.
AC   D2XS97;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Lysin A {ECO:0000313|EMBL:ADA83978.1};
GN   Name=49 {ECO:0000313|EMBL:ADA83978.1};
GN   ORFNames=SCOOT17C_49 {ECO:0000313|EMBL:ADA83978.1};
OS   Mycobacterium phage Scoot17C.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Bclasvirinae; Pegunavirus; Pegunavirus Pg1.
OX   NCBI_TaxID=701455 {ECO:0000313|EMBL:ADA83978.1, ECO:0000313|Proteomes:UP000001898};
RN   [1] {ECO:0000313|EMBL:ADA83978.1, ECO:0000313|Proteomes:UP000001898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hohenstein V.G., Ko C., Russell D.A., Edgar R.H., Jacobs-Sera D.,
RA   Hendrix R.W., Hatfull G.F.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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; GU247134; ADA83978.1; -; Genomic_DNA.
DR   SMR; D2XS97; -.
DR   Proteomes; UP000001898; Genome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; cd12797; M23_peptidase; 1.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR   PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   4: Predicted;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638}.
FT   DOMAIN          160..315
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   429 AA;  46613 MW;  B279E8BF16C77779 CRC64;
     MRAGTYTLSS GFGPRWGSQH RGLDFAAKDG TPIYAAQGGT VAYIGRADGF GQWIVIDHPA
     ADGGGTTVYG HMWDAFATGL RQGQRVEAGQ LIAYVGTNGQ STGPHLHFEV HPTVWRQGSQ
     IDPKPWLANA RNPGDPAPAP APPKGGTLAT LTDPFTGELW SPNRYHPRGL GDPRWIVVHT
     QEGGRTARDL AAYLAQKSSQ VSYHVVVDDR EVLKVVAEGD APWAAAGANK YAFHICMAGS
     YASWSRNKWL DVDTSDGKNE DLQLTKTAHV IAWWCDKYGI PPVWIGGRNI PPWGLDGVCG
     HVDLGAWGGG HTDPGPNFPR DELMRRVSQF LAGTELPPLP TPPPVTVPGT KPDQYGDWML
     YRGNPRNDAD RVRRVQRRLK AAYRSYAGHL EIDGDFGPLT ELAVREFQRR SLLIADGIVG
     PNTAAALKP
//