CWLM_BACLI
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