ID   ALYS_BPR1T              Reviewed;         270 AA.
AC   Q38135;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   07-OCT-2020, entry version 72.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
OS   Lactococcus phage r1t (Bacteriophage r1t).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=43685;
OH   NCBI_TaxID=1359; Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8730875; DOI=10.1111/j.1365-2958.1996.tb02478.x;
RA   van Sinderen D., Karsens H., Kok J., Terpstra P., Ruiters M.H., Venema G.,
RA   Nauta A.;
RT   "Sequence analysis and molecular characterization of the temperate
RT   lactococcal bacteriophage r1t.";
RL   Mol. Microbiol. 19:1343-1355(1996).
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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; U38906; AAB18724.1; -; Genomic_DNA.
DR   RefSeq; NP_695077.1; NC_004302.1.
DR   SMR; Q38135; -.
DR   PRIDE; Q38135; -.
DR   GeneID; 955499; -.
DR   KEGG; vg:955499; -.
DR   Proteomes; UP000001164; Genome.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; -; 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; SSF55846; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..270
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /id="PRO_0000164407"
FT   DOMAIN          22..151
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   270 AA;  30214 MW;  80A5E38F7F2A6675 CRC64;
     MTIYDKTFLL GTGQGSSQKA SNRYIVIHDT ANDNNQGDNS ATNEASYMHN NWQNAYTHAI
     AGWDKVYLVG EPGYVAYGAG SPANERSPFQ IELSHYSDPA KQRSSYINYI NAVREQAKVF
     GIPLTLDGAG NGIKTHKWVS DNLWGDHQDP YSYLTRIGIS KDQLAKDLAN GIGGASKSNQ
     SNNDDSTHAI NYTPNMEEKE MTYLIFAKDT KRWYITNGIE IRYIKTGRVL GNYQNQWLKF
     KLPVDTMFQA EVDKEFGTGA TNPNRDISKG