ID   ACMA_LACLA              Reviewed;         439 AA.
AC   Q9CIT4;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 129.
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=LL0272; ORFNames=L68758;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Required for cell separation during growth. {ECO:0000250}.
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; AE005176; AAK04370.1; -; Genomic_DNA.
DR   PIR; H86658; H86658.
DR   RefSeq; NP_266428.1; NC_002662.1.
DR   RefSeq; WP_010905256.1; NC_002662.1.
DR   AlphaFoldDB; Q9CIT4; -.
DR   SMR; Q9CIT4; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; 272623-L68758; -.
DR   EnsemblBacteria; AAK04370; AAK04370; L68758.
DR   KEGG; lla:L68758; -.
DR   PATRIC; fig|272623.7.peg.298; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG1705; Bacteria.
DR   HOGENOM; CLU_013771_6_1_9; -.
DR   OrthoDB; 2155627at2; -.
DR   Proteomes; UP000002196; 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: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;
KW   Reference proteome; Repeat; Secreted; Septation; Signal.
FT   SIGNAL          1..57
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..439
FT                   /note="Probable N-acetylmuramidase"
FT                   /id="PRO_0000012112"
FT   DOMAIN          241..284
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          321..364
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          395..438
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          218..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  46592 MW;  AE4551E4D04CB499 CRC64;
     MPVSRIKVKN RHLKKKAKKP LAFYKPATKF AGAVLIAGTL TTTHELLLQQ TSPMVQAATN
     STEAFIESIA ASAKPVADSN GLYPSVMIAQ AILESNWGSS QLSRAPYYNL FGIQGTYQGK
     SVVFKTQEYL NGKWVTKDMP FRVYPSFNQS FQDNAYVLKT TNFGNGPYYA KAWRANAATY
     QAATAALTGK YATDPNYGAS LNRIISQYNL TRFDGASSAG TSNSGGSTAT NTNNNSNTSS
     TTYTVKSGDT LWGISQKYGI SVAQIQSANN LKSTVIYIGQ KLVLTTSSSS SNTNSSTSSG
     NSAGTTTPTT SVTPAKPASQ TTIKVKSGDT LWGLSVKYKT TIAQLKSWNH LNSDTIFIGQ
     NLIVSQSAGS SSSSTGSSSA STSSTSNSSA ASNTSIHKVV KGDTLWGLSQ KSGSPIASIK
     AWNHLSSDTI LIGQYLRIK
//