LuxR family transcriptional regulator; Regulatory protein of bacterial bioluminescence. It probably binds the autoinducer molecule and potentiates the transcription of the bioluminescence operon.

AAA family ATPase; Acts negatively to control the expression of luminescence. At low cell density, LuxO is phosphorylated, and together with sigma-54, causes repression of the luxCDABEGH operon. This repression could be indirect, LuxO could activate a negative regulator of luminescence. At high cell density, LuxO is dephosphorylated and inactive, therefore the luxCDABEGH operon is not repressed and light is emitted. LuxO and sigma-54 have also a role in activating the production of siderophore and in regulating the rugose colony morphology phenotype (By similarity).

Isochorismate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.

Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.

tRNA uridine(34) 5-carboxymethylaminomethyl synthesis GTPase MnmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.

Isochorismate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.

TetR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.

tRNA uridine(34) 5-carboxymethylaminomethyl synthesis enzyme MnmG; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34; Belongs to the MnmG family.

Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.