ID   CWLM_BACLI              Reviewed;         253 AA.
AC   P37134;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlM;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
GN   Name=cwlM;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FD0120;
RX   PubMed=1495475; DOI=10.1007/bf00272354;
RA   Kuroda A., Sugimoto Y., Funahashi T., Sekiguchi J.;
RT   "Genetic structure, isolation and characterization of a Bacillus
RT   licheniformis cell wall hydrolase.";
RL   Mol. Gen. Genet. 234:129-137(1992).
CC   -!- FUNCTION: Hydrolyzes the cell wall of M.luteus more efficiently than
CC       that of B.licheniformis and B.subtilis. The C-terminal region,
CC       including the repeats, determines substrate specificity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Accumulates in cells
CC       as inclusion bodies. May be secreted by a mechanism different from the
CC       normal export system.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; X62116; CAA44026.1; -; Genomic_DNA.
DR   PIR; S23572; S23572.
DR   AlphaFoldDB; P37134; -.
DR   SMR; P37134; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.30.70.1070; -; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF110997; SSF110997; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Repeat; Secreted.
FT   CHAIN           1..253
FT                   /note="N-acetylmuramoyl-L-alanine amidase CwlM"
FT                   /id="PRO_0000164420"
FT   DOMAIN          4..172
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          179..253
FT                   /note="SPOR"
FT   REPEAT          184..219
FT                   /note="1"
FT   REPEAT          220..253
FT                   /note="2"
FT   REGION          184..253
FT                   /note="2 X 35 AA approximate tandem repeats"
SQ   SEQUENCE   253 AA;  27600 MW;  28E86E017B68D768 CRC64;
     MVKIFIDPGH GGSDTGASAN GLQEKQLTLQ TALALRNMLL NEYQNVSVLL SRTSDQTVSL
     TQRTNAANSW GADYFLSIHM NAGGGTGFED YIYPGVGAPT TTYRDIMHEE ILKVVDFRDR
     GKKTANFHVL RETAMPALLT ENGFVDNTND AEKLKSSAFI QSIARGHANG LARAFNLSKN
     AAALYKVQIA AFRTKANADS LAAQAEAKGF DALVIYRDSL YKVQIGAFSS KENAEALVQQ
     AKNAEFDTFI YQE