MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Redox-responsive in vitro modulation of the signalling state of the isolated PrrB sensor kinase of Rhodobacter sphaeroides NCIB 8253. Redox-responsive in vitro modulation of the signalling state of the isolated PrrB sensor kinase of Rhodobacter sphaeroides NCIB 8253. FEBS Lett. (0014-5793) 2006 imex curation Potter CA., Jeong EL., Williamson MP., Henderson PJ., Phillips-Jones MK. 2009-01-08 Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Potter CA., Jeong EL., Williamson MP., Henderson PJ., Phillips-Jones MK. FEBS Lett. (0014-5793) 2006 2009-01-08 Only protein-protein interactions imex curation regb_cers4 Sensor histidine kinase RegB regB prrB RHOS4_00950 RSP_1520 Protein PrrB protein protein rhos4 Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) MILGPDGILNRDTRGDWVRLRTLILLRWMAVAGQLAAIVVTDWYLGVRLPMGLCFMAVGASVIANVIATFVFPQNRRLTEFQALMILLFDLTQLSFLLFLTGGLTNPFALLILAPVTISALALELRTTVILGAIAIGLLTFTAYFHLPLILADGSSLSVPRMFEFGFWLAIVIGILFLGLYSRRVAIEIRSMSDALLATQMALDREQKLTDLGGVVAAAAHELGTPLATIKLVSSELAEELSEQPALRDDAELIREQADRCRDILRSMGRAGKDDLQMRQAPLGEVLREAAEPHVGRGKRVEFDLYPSRGGDERQPVILRRPEVIHGLRNLIQNAVDFARSTVWIDGEWTGDRIAIRIVDDGEGYPPAIIGRIGDPFVRQRRAEESQSRRPGYEGMGLGLFIAKTLLERSGAELSFANAADPFLRSHERPERCGAIVEVIWPVDRLVVVRNAPLGENVLIQT mint Member of the two-component regulatory system regB/regA. Involved in the positive regulation of photosynthesis gene expression in response to anaerobiosis. Also involved in positive regulation of the cbbI and cbbII Calvin cycle CO2 fixation operons, as well as in regulation of expression of genes involved in alternative CO2 fixation pathways. Phosphorylates regA/prrA 3BC7CEA8C7BA7D5E rega_cers4 Photosynthetic apparatus regulatory protein RegA Response regulator PrrA prrA RSP_1518 RHOS4_00930 regA protein protein rhos4 Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) MAEDLVFELGADRSLLLVDDDEPFLKRLAKAMEKRGFVLETAQSVAEGKAIAQARPPAYAVVDLRLEDGNGLDVVEVLRERRPDCRIVVLTGYGAIATAVAAVKIGATDYLSKPADANEVTHALLAKGESLPPPPENPMSADRVRWEHIQRIYEMCDRNVSETARRLNMHRRTLQRILAKRSPR D73447E037F1285B rega-regb 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified Stoichiometry: 1.0 phosphorylation phosphorylation reaction phosphorylation F1B Fig. 1 also shows that the higher levels of PrrB P obtained in these experiments resulted in a concomitant increase in phosphotransfer to PrrA, resulting in higher levels of PrrA P in our phosphotransfer assays. This therefore confirms that subsequent signal transduction from PrrB to PrrA also occurs successfully under all conditions of DTT used under these in vitro conditions (Fig. 1). FEBS-Letters mint regb-regb 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified Stoichiometry: 1.0 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined self self neutral component neutral component purified purified Stoichiometry: 1.0 phosphorylation phosphorylation reaction phosphorylation F1A We investigated this further by examining the effects of various concentrations of DTT between 0 and 100 mM and the results are shown in Fig. 1. As the concentration of DTT present in the assays was increased, so too were the resulting levels of PrrB P. This confirms that our intact purified protein here is functioning appropriately in response to reducing conditions. FEBS-Letters mint