ID A8WA19_9CAUD Unreviewed; 402 AA.
AC A8WA19;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=31 {ECO:0000313|EMBL:ABW88426.1};
GN ORFNames=Giles_31 {ECO:0000313|EMBL:ABW88426.1};
OS Mycobacterium phage Giles.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Gilesvirus; Gilesvirus giles.
OX NCBI_TaxID=480808 {ECO:0000313|EMBL:ABW88426.1, ECO:0000313|Proteomes:UP000008551};
RN [1] {ECO:0000313|EMBL:ABW88426.1, ECO:0000313|Proteomes:UP000008551}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18178732; DOI=10.1128/JB.01657-07;
RA Morris P., Marinelli L.J., Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RT "Genomic characterization of mycobacteriophage Giles: evidence for phage
RT acquisition of host DNA by illegitimate recombination.";
RL J. Bacteriol. 190:2172-2182(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; EU203571; ABW88426.1; -; Genomic_DNA.
DR RefSeq; YP_001552360.1; NC_009993.2.
DR IntAct; A8WA19; 10.
DR MINT; A8WA19; -.
DR GeneID; 5758945; -.
DR KEGG; vg:5758945; -.
DR OrthoDB; 2745at10239; -.
DR Proteomes; UP000008551; Genome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 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; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 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};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008551}.
FT DOMAIN 144..290
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 402 AA; 43082 MW; 6128CD8EE4387477 CRC64;
MPVYAIQSGT VIYAGAASGY GGPDPAGWLV IDSDDAEGGG CLEYGHIVRE VNRGDHVTAG
QRIGHINPNN RTNGGVAPHL HVTDWPHAYG QGSRQNVMAR LSGAREPEAQ AAPTPTEQGT
VVGDPVWLAD VVRPTVAKFA EYPGWRNRGH GDFKDIRGVM VHHTGGPASA ASIANGRPDL
AGPLAQLHIS RDGTVTVVAV GVAWHAGAGS YPWLPTNMGN WHLIGIECEW PYGEPGINER
NAYTVRWRDP EIIALRNTCA AILLRLGLGV DRLIGHKDYA GRAQGKWDPG NMSMDWLRGE
VRKDMDGFVF PGEDIVNVTP PPVPAPVPAP PATANVLLHR GMSGPNVVKL QTTLRRWYSK
LAVDGDFGPH TEACVRDRQR IYGLDVDGIV GPLTAAKIGL VL
//
