ID   A0A1C9M298_9CAUD        Unreviewed;       429 AA.
AC   A0A1C9M298;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Lysin A {ECO:0000313|EMBL:AOQ29304.1};
GN   ORFNames=SEA_PINKMAN_47 {ECO:0000313|EMBL:AOQ29304.1};
OS   Mycobacterium phage Pinkman.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Bclasvirinae; Pegunavirus; Pegunavirus oline.
OX   NCBI_TaxID=1897426 {ECO:0000313|EMBL:AOQ29304.1, ECO:0000313|Proteomes:UP000229304};
RN   [1] {ECO:0000313|EMBL:AOQ29304.1, ECO:0000313|Proteomes:UP000229304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Flickinger H., Loeb A., Murray M., Ortbals C., Stricker A., Suderman E.,
RA   Ward R., Delesalle V.A., Garlena R.A., Johnson A.A., Russell D.A.,
RA   Pope W.H., Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KX702319; AOQ29304.1; -; Genomic_DNA.
DR   SMR; A0A1C9M298; -.
DR   Proteomes; UP000229304; 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;  46667 MW;  911CD923E603199C CRC64;
     MRAGTYTLSS GFGPRWGSQH RGLDFAAKDG TPIYAAQGGT VAYIGRADGF GQWIVIDHPA
     ADGGGTTVYG HMWDAFATGL RQGQRVEAGQ LIAYVGTNGQ STGPHLHFEV HPTVWRQGSQ
     IDPKPWLANA RNPGDPAPAP APPKGGTLAK LTDPFTGELW SPNRYHPRGL GDPRWIVVHT
     QEGGRTARDL AAYLAQKSSQ VSYHVVVDDR EVLKVVAEGD APWAAAGANK YAFHICMAGS
     YASWSRNKWL DVDTSDGKNE DLQLTKTAHV IAWWCDKYGI PPVWIGGRNI PPWGLDGVCG
     HVDLGAWGGG HTDPGPNFPR DELMRRVNQF LAGTELPPLP TPPPVTVPGT KPDQYGDWML
     YRGNPRNDAD RVRRVQRRLK AAYRSYAGHL EIDGDFGPLT ELAVREFQRR SLLIADGIVG
     PNTAAALKP
//