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 (22-95) and the Plug module (111-219) acting as a channel gate; Seems to possess a lipoprotein signal peptide is cleaved between the residues 16 and 17; 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 25 and 26; Putatively localized in the cytoplasmic membrane; Family membership.

The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity (here, a winged-helix DNA-binding domain) that acts as transcriptional regulator; Family membership.

Conserved hypothetical protein; Contains several Single hybrid motifs found in biotinyl/lipoyl-carrier proteins and domains, where the biotin and lipoic acid moieties act as covalently attached coenzyme in various enzymes; Signal peptide cleaved between the residues 23 and 24; Putatively localized in the cytoplasmic membrane.

O-linked N-acetylglucosaminyltransferase, family GT41; Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to an oligosaccharide. Contains Tetratricopeptide repeats; Seems to have an uncleavable N-terminal signal sequence; Localized in the cytoplasmic membrane; Specificity unclear.

Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Serine peptidase, family S8; Serine peptidase contains a catalytic triad in the order Asp, His and Ser in the sequence. Its structure consists of three layers with a seven-stranded beta sheet sandwiched between two layers of helices; Belongs to the family S8 of peptidases; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic membrane; Specificity unclear.

Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear.

Patatin-like phospholipase; Conserved protein containing a N-terminal Patatin-like phospholipase domain and a C-terminal domain of unknown function; Contains a signal peptide cleaved between the residues 32 and 33; Localized in the periplasmic space; Family membership.