The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.

Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.

Glycosyl hydrolases family 25.

Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]

ChainB, SLPH (HMW SLP) [Clostridioides difficile R20291],7ACZ_D Chain D, SLPH (HMW SLP) [Clostridioides difficile R20291]

ChainB, S-layer protein [Clostridioides difficile 630],7ACY_D Chain D, S-layer protein [Clostridioides difficile 630],7QGQ_B Chain B, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_D Chain D, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_J Chain J, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_K Chain K, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_L Chain L, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_M Chain M, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_N Chain N, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_T Chain T, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_U Chain U, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_V Chain V, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_W Chain W, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_X Chain X, Precursor of the S-layer proteins [Clostridioides difficile 630]

ChainB, S-layer protein [Clostridioides difficile],7ACX_D Chain D, S-layer protein [Clostridioides difficile]

Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1

Amidase enhancer OS=Bacillus subtilis (strain 168) OX=224308 GN=lytB PE=1 SV=1

Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2