ID G8J7N2_9CAUD Unreviewed; 397 AA.
AC G8J7N2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=30 {ECO:0000313|EMBL:AER14077.1};
GN ORFNames=DOTPRODUCT_30 {ECO:0000313|EMBL:AER14077.1};
OS Mycobacterium phage DotProduct.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Gracegardnervirinae; Cheoctovirus; Mycobacterium virus DotProduct.
OX NCBI_TaxID=2923008 {ECO:0000313|EMBL:AER14077.1, ECO:0000313|Proteomes:UP000007317};
RN [1] {ECO:0000313|EMBL:AER14077.1, ECO:0000313|Proteomes:UP000007317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22282335; DOI=10.1128/JVI.06870-11;
RG the Science Education Alliance Phage Hunters Advancing Genomics and Evolutionary Science Program;
RG the KwaZulu-Natal Research Institute for Tuberculosis and HIV Mycobacterial Genetics Course Students;
RG the Phage Hunters Integrating Research and Education Program;
RA Hatfull G.F.;
RT "Complete Genome Sequences of 138 Mycobacteriophages.";
RL J. Virol. 86:2382-2384(2012).
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; JN859129; AER14077.1; -; Genomic_DNA.
DR OrthoDB; 2745at10239; -.
DR Proteomes; UP000007317; Segment.
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; 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 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 SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-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:UP000007317}.
FT DOMAIN 158..310
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 397 AA; 44258 MW; 56C8E6F65ED5AE67 CRC64;
MTTKDQVAQI TIAEAKARGY TRSECLAIMS TFYQESGWND TIWDPTHTTY GIAQQDGSYP
HRFDGAAAQI KGFFDKLDVW RAKPGASTDI WLNICWMQQA PNWPSADYWY ANGRRAYLTE
IKSRIATVTP YLDKYWPADG GTAVPDEPRP DFNEFPIWSN NNSARSGKPT MFLIHTQEGG
GGDAAAENLA KWFQNGNGVS YHYTISQASD GGVTVVDCVD TDRAAWSVGN ANSISINLCF
AGSRASWTLD QWMKQSNAID VAAYLAVQDA KKYGFEPLVV PPPYVNGRPG ISDHRWVTDV
FKWGTHTDVG AWFPWDYFTE RVNHWAAGGK TEPEPPKVKH FPDDWTDREL AVETLRQQRG
YTLNGWPQLG GRTVVDVLGA IGAKLGVEGC YDVKDKS
//
