ACMA_LACLC
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 25-MAY-2022, entry version 66.
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; Firmicutes; 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: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_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