Chitin-binding lectin, family GH18; This protein is homologous to chitinases but the catalytic acidic residues are replaced by polar residues. It likely binds chitin or chitin-derived oligosaccharides; Belongs to the family 18 of the glycoside hydrolases (GH18); Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Function unclear.

Conserved hypothetical lipoprotein; Protein belonging to the DUF1343 family. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Conserved hypothetical protein.

Beta-N-acetylhexosaminidase, family GH20; Beta-N-acetylhexosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Belongs to the family 20 of the glycoside hydrolases. Carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base in the family GH20. They are involved in different pathways such as the N-Glycan degradation, aminosugars metabolism, glycosaminoglycan degradation and globoside metabolism. Signal peptide cleaved between the residues 23 and 24. Localized in the periplas [...]

Beta-N-acetylhexosaminidase, family GH20; Beta-N-acetylhexosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides; Belongs to the family 20 of the glycoside hydrolases (GH20); Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

Beta-N-acetylhexosaminidase, family GH20; Beta-N-acetylhexosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base; Belongs to the family 20 of the glycoside hydrolases (GH20); Signal peptide cleaved between residues 22 and 23; Localized in the periplasmic space; High confidence in function and specificity.

Glycoside hydrolase, family GH18; Glycoside hydrolase with an unknown substrate specificity. It is a modular enzyme displaying a N-terminal catalytic module belonging to the family 18 of the glycoside hydrolases (GH18) and two C-terminal carbohydrate binding modules belonging to the family 5 of the carbohydrate binding modules that mainly bind to the cellulose and chitin; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; Specificity unclear.

N-acetyl-D-glucosamine 2-epimerase catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. It functions as a homodimer, where monomer has an alpha(6)/alpha(6)-barrel structure commonly found in glucoamylases and cellulases This enzyme is involved in sialic acid metabolism. Localized in the cytoplasm; High confidence in function and specificity.

UPF0075 family protein; Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling; Belongs to the anhydro-N-acetylmuramic acid kinase family.

N-acetylmuramoyl-L-alanine amidase; The protein contains two domains. A N-terminal N-acetylmuramoyl-L-alanine amidase domain (230 residues) that hydrolyzes the amide bond between N-acetylmuramoyl residues and L-amino acid residues in bacterial cell walls and a C-terminal domain (200 residues) of unknown function; Contains one N-terminal transmembrane segment; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family; Localized in the cytoplasmic membrane; High confidence in function and specificity.