Peptidase, family C40; Cysteine peptidase belonging to the family C40. Its exact function is not known. C40 peptidases contain single conserved cysteine and histidine residues that form a catalytic dyad in the order Cys, His. Features a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Peptidase, family C40; Cysteine peptidase belonging to the family C40. Its exact function is not known. C40 peptidases contain single conserved cysteine and histidine residues that form a catalytic dyad in the order Cys, His. Features a prokaryotic lipoprotein signal peptide cleaved between the residues 27 and 28; Localized in the outer 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Conserved hypothetical protein; Localized in the cytoplasm.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

tRNA/rRNA methyltransferase; Catalyzes the site-specific methylation of the 2' hydroxy group of the ribose in rRNA or tRNA, using the S-AdoMet; Contains a N-terminal RNA 2'-O ribose methyltransferase substrate binding domain and a C-terminal catalytic domain also involved in the dimer formation that adopts an alpha/beta knot fold; Belongs to the RNA methyltransferase TrmH family; Localized in the cytoplasm; Family membership.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Peptidase spr, family C40; The lipoprotein sprA was identified by genetic as a suppressor of a protease prc mutation. Its exact function is not known. The catalytic dyad is formed by a single conserved cysteine and histidine residues; Belongs to the family C40 of peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 34 and 35; Localized in the cytoplasmic or outer 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Acetyl-CoA acetyltransferase is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or mevalonate biogenesis. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Conserved hypothetical protein; This protein is a putative receptor with a N-terminal extracellular domain, a central membrane domain and a C-terminal metal-dependent phosphohydrolase domain. Its exact function is unknown; Contains a N-terminal transmembrane helix and seven transmembrane helices in the central region; Localized in the cytoplamic membrane; Function unclear.

Conserved hypothetical protein; Localized in the cytoplasm.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

tRNA/rRNA methyltransferase; Catalyzes the site-specific methylation of the 2' hydroxy group of the ribose in rRNA or tRNA, using the S-AdoMet; Contains a N-terminal RNA 2'-O ribose methyltransferase substrate binding domain and a C-terminal catalytic domain also involved in the dimer formation that adopts an alpha/beta knot fold; Belongs to the RNA methyltransferase TrmH family; Localized in the cytoplasm; Family membership.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Peptidase spr, family C40; The lipoprotein sprA was identified by genetic as a suppressor of a protease prc mutation. Its exact function is not known. The catalytic dyad is formed by a single conserved cysteine and histidine residues; Belongs to the family C40 of peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 34 and 35; Localized in the cytoplasmic or outer 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Acetyl-CoA acetyltransferase is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or mevalonate biogenesis. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family.

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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Acetyl-CoA acetyltransferase is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or mevalonate biogenesis. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family.

Conserved hypothetical protein; This protein is a putative receptor with a N-terminal extracellular domain, a central membrane domain and a C-terminal metal-dependent phosphohydrolase domain. Its exact function is unknown; Contains a N-terminal transmembrane helix and seven transmembrane helices in the central region; Localized in the cytoplamic membrane; Function unclear.

Conserved hypothetical protein; This protein is a putative receptor with a N-terminal extracellular domain, a central membrane domain and a C-terminal metal-dependent phosphohydrolase domain. Its exact function is unknown; Contains a N-terminal transmembrane helix and seven transmembrane helices in the central region; Localized in the cytoplamic membrane; Function 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 40 of the cysteine peptidases. These peptidases contain single conserved cysteine and histidine residues that form a putative catalytic dyad in the order Cys, His. Features also a bacterial SH3 domain in the N-terminal region; High confidence in function and specificity.

Conserved hypothetical protein; This protein is a putative receptor with a N-terminal extracellular domain, a central membrane domain and a C-terminal metal-dependent phosphohydrolase domain. Its exact function is unknown; Contains a N-terminal transmembrane helix and seven transmembrane helices in the central region; Localized in the cytoplamic membrane; Function unclear.

Acetyl-CoA acetyltransferase is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or mevalonate biogenesis. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family.