ACMA_LACLM
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 03-AUG-2022, entry version 85.
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; Firmicutes; 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 EnsemblBacteria; CAL96887; CAL96887; llmg_0280.
DR KEGG; llm:llmg_0280; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG1705; Bacteria.
DR HOGENOM; CLU_013771_6_1_9; -.
DR OMA; YSFRDHS; -.
DR PhylomeDB; A2RHZ5; -.
DR BioCyc; LLAC416870:LLMG_RS01460-MON; -.
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:0019835; P:cytolysis; 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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 3.
DR Gene3D; 3.10.350.10; -; 3.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF01476; LysM; 3.
DR SMART; SM00257; LysM; 3.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; SSF54106; 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