Conserved hypothetical protein; Localized in the cytoplasm.

Possible ABC importer, ATPase component; Conserved hypothetical protein that could be an ATP-binding protein; Localized in the cytoplasm; Conserved hypothetical protein.

Protein of unknown function that could be the periplasmic component of a ABC transporter (importer); Contains a Mce (mammalian cell entry) domain and one N-terminal transmembrane segment; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Electron transfer flavoprotein, beta subunit; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various dehydrogenases. In Bacteria, ETFs are produced under specific growth conditions, receiving electrons only from the oxidation of specific substrates. ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and an AMP molecule. EtfB codes the beta subunit that binds the AMP molecule; Localized in the cytoplasm; High confidence in function and specificity.

Electron transfer flavoprotein, alpha subunit; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various dehydrogenases. In Bacteria, ETFs are produced under specific growth conditions, receiving electrons only from the oxidation of specific substrates. ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and an AMP molecule. EtfA codes the alpha subunit that participate, with the alpha subunit, to the binding of the FAD molecule; Localized in the cytoplasm; High confidence in function and specificity.

3-Hydroxyl-CoA dehydrogenase / Enoyl-CoA hydratase; Modular protein containing a N-terminal 3-Hydroxyl-CoA dehydrogenase domain and a C-terminal Enoyl-CoA hydratase domain. In Bacillus subtilis, this protein was formerly known as YusL, and has been renamed FadN by Matsuoka et al (JBC, 2007). FadN is involved in fatty acid degradation. 3-Hydroxyl-CoA dehydrogenase catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. It uses NAD as cofactor. Enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA. Localized in the cytoplasm; High confidence in [...]

Succinate dehydrogenase is a complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558. It is involved in the citrate cycle and catalyzes the reaction: succinate + acceptor = fumarate + reduced acceptor. It uses a FAD as a cofactor. SdhB is the iron-sulfur subunit. Localized in the cytoplasm; High confidence in function and specificity.

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.

Beta-N-acetylglucosaminidase, family GH3 / Serine peptidase, family S12; This is a modular protein with a N-terminal beta-N-acetylglucosaminidase domain and a C-terminal serine peptidase domain. The beta-N-acetylglucosaminidase module belongs to the family 3 of the glycoside hydrolases. It catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-beta-D-glucosaminides. The C-terminal domain belongs to the family 12 of the serine peptidases D-Ala-D-Ala carboxypeptidase B and aminopeptidase DmpB. Features a signal peptide cleaved between residues 19 an [...]