ID   ACMA_LACLM              Reviewed;         437 AA.
AC   A2RHZ5; O52362; Q48603;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Probable N-acetylmuramidase;
DE            EC=3.2.1.17;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Lysozyme;
DE   AltName: Full=Peptidoglycan hydrolase;
DE   Flags: Precursor;
GN   Name=acmA; OrderedLocusNames=llmg_0280;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7883712; DOI=10.1128/jb.177.6.1554-1563.1995;
RA   Buist G., Kok J., Leenhouts K.J., Dabrowska M., Venema G.,
RA   Haandrikman A.J.;
RT   "Molecular cloning and nucleotide sequence of the gene encoding the major
RT   peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell
RT   separation.";
RL   J. Bacteriol. 177:1554-1563(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Hydrolyzes the cell wall of L.lactis and M.lysodeikticus.
CC       Required for cell separation during growth.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: The LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
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DR   EMBL; U17696; AAC33367.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL96887.1; -; Genomic_DNA.
DR   RefSeq; WP_011834353.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RHZ5; -.
DR   SMR; A2RHZ5; -.
DR   STRING; 416870.llmg_0280; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   KEGG; llm:llmg_0280; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG1705; Bacteria.
DR   HOGENOM; CLU_013771_6_1_9; -.
DR   OrthoDB; 2155627at2; -.
DR   PhylomeDB; A2RHZ5; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0061784; F:peptidoglycan N-acetylglucosaminidase activity; IDA:CACAO.
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:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 3.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 3.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF01476; LysM; 3.
DR   PRINTS; PR01002; FLGFLGJ.
DR   SMART; SM00257; LysM; 3.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF54106; LysM domain; 3.
DR   PROSITE; PS51782; LYSM; 3.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cell cycle; Cell division;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Septation; Signal.
FT   SIGNAL          1..57
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..437
FT                   /note="Probable N-acetylmuramidase"
FT                   /id="PRO_0000285234"
FT   DOMAIN          243..286
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          319..362
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          393..436
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          217..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  46564 MW;  5C905633BD5DE28B CRC64;
     MPVSRVKVKN RHLKKKTKKP LAFYKPATKF AGAVLIAGTL TTTHELLLQQ TSPMVQAATN
     SSEVFIESIA ASAKPVADAN GLYPSVMIAQ AILESNWGSS QLSRAPYYNL FGIQGTYQGK
     SVVFKTQEYL NGKWVTKDMP FRVYPSFNQS FQDNAYVLKT TNFGNGPYYA KAWRANAATY
     QDATAALTGR YATDPSYGAS LNRIISQYNL TRFDGASSAG NTNSGGSTTT ITNNNSGTNS
     SSTTYTVKSG DTLWGISQRY GISVAQIQSA NNLKSTIIYI GQKLVLTGSA SSTNSGGSNN
     SASTTPTTSV TPAKPTSQTT VKVKSGDTLW ALSVKYKTSI AQLKSWNHLS SDTIYIGQNL
     IVSQSAAASN PSTGSGSTAT NNSNSTSSNS NASIHKVVKG DTLWGLSQKS GSPIASIKAW
     NHLSSDTILI GQYLRIK
//