Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].

sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.

N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.

amidase domain-containing protein.

ChainA, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_B Chain B, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_C Chain C, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_D Chain D, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325]

ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1]

Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1]

CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e]

E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1]

Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1

N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=SAOUHSC_02979 PE=1 SV=1

Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1

Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2

Peptidoglycan hydrolase FlgJ OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=flgJ PE=3 SV=1