Conserved hypothetical protein; Localized in the cytoplasm.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

L-alanine-DL-glutamate epimerase catalyzes the epimerization of D-Glu into L-Glu, in the context of the dipeptide L-Ala-D-Glu, which is a component of peptidoglycan. Involved in peptidoglycan metabolism. This enzyme belongs to the Mandelate racemase / muconate lactonizing enzyme family. These enzymes feature a N-terminal domain with a Enolase N-terminal domain-like fold and a C-terminal TIM alpha/beta barrel fold. Localized in the cytoplasm; High confidence in function and specificity.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

L-alanine-DL-glutamate epimerase catalyzes the epimerization of D-Glu into L-Glu, in the context of the dipeptide L-Ala-D-Glu, which is a component of peptidoglycan. Involved in peptidoglycan metabolism. This enzyme belongs to the Mandelate racemase / muconate lactonizing enzyme family. These enzymes feature a N-terminal domain with a Enolase N-terminal domain-like fold and a C-terminal TIM alpha/beta barrel fold. Localized in the cytoplasm; High confidence in function and specificity.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Family membership.

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (20-93) and the Plug module (110-246) acting as a channel gate; The signal peptide is cleaved between the residues 19 and 20; Family membership.

SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Family membership.

This conserved protein belongs to the OmpA-like family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space and/or in the outer membrane; Family membership.

SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Family membership.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (20-93) and the Plug module (110-246) acting as a channel gate; The signal peptide is cleaved between the residues 19 and 20; Family membership.

SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Family membership.

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (20-93) and the Plug module (110-246) acting as a channel gate; The signal peptide is cleaved between the residues 19 and 20; Family membership.

This conserved protein belongs to the OmpA-like family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space and/or in the outer membrane; Family membership.

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (20-93) and the Plug module (110-246) acting as a channel gate; The signal peptide is cleaved between the residues 19 and 20; Family membership.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

L-alanine-DL-glutamate epimerase catalyzes the epimerization of D-Glu into L-Glu, in the context of the dipeptide L-Ala-D-Glu, which is a component of peptidoglycan. Involved in peptidoglycan metabolism. This enzyme belongs to the Mandelate racemase / muconate lactonizing enzyme family. These enzymes feature a N-terminal domain with a Enolase N-terminal domain-like fold and a C-terminal TIM alpha/beta barrel fold. Localized in the cytoplasm; High confidence in function and specificity.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

Amidase catalyzes the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3. The specificity of this enzyme is unknown. Belongs to a protein family including N-acetylmuramoyl-L-alanine amidase. Features an uncleaved signal peptide. Localized in the cytoplasmic membrane; Specificity unclear.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

Peptidase family M14 contains mainly metallocarboxypeptidases. The single catalytic zinc ion is tetrahedrally coordinated by two histidines and a glutamate, as well as a water molecule. One of the histidines and the glutamate occur in the motif His-Xaa-Xaa-Glu. Features a signal peptide cleaved between the residues 18 and 19. Localized in the periplasm; Specificity unclear.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

Serine peptidase belonging to the family S12, which includes D-Ala-D-Ala carboxypeptidase B and aminopeptidase DmpB. The active site residues Ser and Lys form the catalytic dyad and are found in the motif Ser-Xaa- Thr-Lys. Localized in the cytoplasm; Specificity unclear.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

This conserved protein belongs to the OmpA-like family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space and/or in the outer membrane; Family membership.

SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Family membership.

This conserved protein belongs to the OmpA-like family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space and/or in the outer membrane; Family membership.

TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (20-93) and the Plug module (110-246) acting as a channel gate; The signal peptide is cleaved between the residues 19 and 20; Family membership.

This conserved protein belongs to the OmpA-like family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space and/or in the outer membrane; Family membership.

D-alanyl-D-alanine carboxypeptidase, also known as Penicillin-binding protein 4, is involved in the peptidoglycan biosynthesis. It hydrolyzes the D-Ala-D-Ala bond in the cross-linking peptide precursor, and performs the transpeptidation reaction between the D-Ala and the meso-2,6-diaminopimelate of adjacent crosslinking peptides of the bacterial cell wall; Belongs to the family S13 of the serine peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer membrane; High confidence in function and specificity.

Amidase catalyzes the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3. The specificity of this enzyme is unknown. Belongs to a protein family including N-acetylmuramoyl-L-alanine amidase. Features an uncleaved signal peptide. Localized in the cytoplasmic membrane; Specificity unclear.

Dipeptidyl peptidase, family C40; Dipeptidyl peptidase hydrolyzes gamma-D-Glu-L-(meso)A2pm linkages only in those peptide units that have a free N-terminal L-alanine. It is involved in peptidoglycan metabolism; Belongs to the family C40 of peptidases; Prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; High confidence in function and specificity.

Amidase catalyzes the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3. The specificity of this enzyme is unknown. Belongs to a protein family including N-acetylmuramoyl-L-alanine amidase. Features an uncleaved signal peptide. Localized in the cytoplasmic membrane; Specificity unclear.

Peptidase family M14 contains mainly metallocarboxypeptidases. The single catalytic zinc ion is tetrahedrally coordinated by two histidines and a glutamate, as well as a water molecule. One of the histidines and the glutamate occur in the motif His-Xaa-Xaa-Glu. Features a signal peptide cleaved between the residues 18 and 19. Localized in the periplasm; Specificity unclear.