Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
The CbrA-CbrB two-component regulatory system controls the utilization of multiple carbon and nitrogen sources in Pseudomonas aeruginosa.
-
cbrA encodes a 983-residue sensor kinase with a 12-TM N-terminal membrane domain and an NtrB-like kinase domain.
"The amino-terminal half (490 residues) of CbrA appears to be a sensor membrane domain, as predicted by 12 possible transmembrane helices"
-
cbrA and cbrB mutants cannot use arginine, histidine, proline, polyamines and other carbon sources.
"cbrA and cbrB mutants of strain PAO were found to be unable to use several amino acids (such as arginine, histidine and proline), polyamines and agmatine as sole carbon and nitrogen sources"
The sensor kinase CbrA is a global regulator that modulates metabolism, virulence, and antibiotic resistance in Pseudomonas aeruginosa.
Transport and kinase activities of CbrA of Pseudomonas putida KT2440.
-
Purified P. putida CbrA autophosphorylates at His766 and phosphorylates CbrB; its SLC5 domain transports L-histidine.
"we show that CbrA and CbrAΔSLC5 can autophosphorylate at His766 and transfer the phosphoryl group to CbrB"
Role of the Transporter-Like Sensor Kinase CbrA in Histidine Uptake and Signal Transduction.