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LysM peptidoglycan-binding domain-containing protein
The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function. The structure of this domain is known [2]. [1]. 1352512. Modular design of the Enterococcus hirae muramidase-2 and. Streptococcus faecalis autolysin.. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L,. Shockman GD, Ghuysen JM;. FEMS Microbiol Lett 1992;70:257-264.. [2]. 10843862. The structure of a LysM domain from E. coli membrane-bound lytic. murein transglycosylase D (MltD).. Bateman A, Bycroft M;. J Mol Biol 2000;299:1113-1119. (from Pfam)
spore coat assembly protein ExsA
C40 family peptidase
C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad
SafA/ExsA family spore coat assembly protein
SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see PFAM model PF01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. Because lysin motifs are repeated in many proteins, this model is built as a single-hit (-g option, hmms style) model.
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