Conserved yhpothetical protein. Homology to BP1565 of B.pertussis of 66% (tremble:Q7VY02) Has PF07311:Protein of unknown function (DUF1458)(IPR009923);This family consists of several hypothetical bacterial proteins as well as one archaeal sequence Q9HPW4. Members of this family are typically of around 70 residues in length. The function of this family is unknown. No signal peptide or TMH present.

Flagellar transcriptional activator FlhC; Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhC family.

Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity.

Flagellar transcriptional activator FlhD; Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhD family.

Conserved hypothetical secreted protein. Homology to bb3588 of B. bronchiseptica of 41% (trembl|Q7WGK1). Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. signal peptide. TMH in signal peptide; Conserved hypoth [...]

AMP nucleosidase; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations.

Conserved hypothetical membrane protein. Homology to PA1044 of P. aeruginosa of 44% (trembl|Q9I4T0). No domains predicted. Signal peptide. 3 TMHs; Conserved hypothetical protein.

Hypothetical protein, 51% identity (59% similarity) to TrEMBL;Q8Y0B0. TrEMBL; Q7NWN1(53% identity). Has PF04305, Protein of unknown function (DUF455).IPR007402. Has no signal Peptide or TMH present; Function unclear.

Flagellar biosynthesis protein,FliO, 26% identity to TrEMBL;Q8XBA2, Q83ML3. SProt;P22586 Has Signal peptide. Has PF04347, Flagellar biosynthesis protein,FliO;IPR007442; FliO is an essential component of the flagellum-specific protein export apparatus. It is an integral membrane protein. Its precise molecular function is unknown.