ID   ACMA_LACLC              Reviewed;         437 AA.
AC   P0C2T5; O52362; Q48603;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-MAY-2023, entry version 69.
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;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2250;
RX   PubMed=11131071; DOI=10.1017/s0022029900004519;
RA   Govindasamy-Lucey S., Gopal P.K., Sullivan P.A., Pillidge C.J.;
RT   "Varying influence of the autolysin, N-acetyl muramidase, and the cell
RT   envelope proteinase on the rate of autolysis of six commercial Lactococcus
RT   lactis cheese starter bacteria grown in milk.";
RL   J. Dairy Res. 67:585-596(2000).
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; AF036720; AAB93629.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C2T5; -.
DR   SMR; P0C2T5; -.
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: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   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_0000012113"
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          291..319
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;  46597 MW;  169778AF09E13963 CRC64;
     MPVSRVKVKN RHLKKKTKKP LAFYKPTTKF VGAVLIAGTL TTTHELLLQQ TSPMVQAATN
     SSEAFIESIA ASAKPVADAN GLYPSVMIAQ AILESNWGSS QLSRAPYYNL FGIQGTYQGK
     SVVFKTQEYL NGKWVTKDMP FRVYPSFNQS FQDNTYVLKT TNFGNGPYYA KAWRANAATY
     QDATAALTGK YATDPSYGAS LNRIISQYNL TRFDGASSAG NTNSGGSTTT NTNNNSGTNS
     SSTTYTVKSG DTLWGISQRY GISVAQIQSA NNLKSTIIYI GQKLLLTGSA SSTNSGGSNN
     SASTTPTTSV TPAKPASQTS VKVKSGDTLW ALSVKYKTSI AQLKSWNHLS SDTIYIGQNL
     IVSQSAATSN PSTGSGSTAT NNSNSTSSNS NASIHKVVKG DTLWGLSQKS GSPIASIKAW
     NHLSSDTILI GQYLRIK
//