Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...]

Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. DnaA can inhibit its own gene expression as well as that of other genes.

Nitrogen sensing transcriptional regulator; Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation. Also represses glnRA and gltAB in the absence of ammonium. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site.

Glutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Glutamine synthetase; Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA- binding active state and turns on the transcription of genes required for nitrogen assimilation. Under condi [...]

Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...]

Transcriptional regulator (NtrC/NifA family); Positive regulator of arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF and probably acts by binding to the corresponding upstream activating sequences.

Transcriptional regulator (nitrogen metabolism); Transcription repressor that represses many genes including ureABC and tnrA, during nitrogen excess. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, GlnR requires a DNA sequence of 17 nucleotides as minimal binding site.

Transcriptional repressor of citB and citZ; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator; Belongs to the LysR transcriptional regulatory family.