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 Functional characterization of a novel Mn2+ dependent protein serine/threonine kinase KpnK, produced by Klebsiella pneumoniae strain MGH78578. Functional characterization of a novel Mn2+ dependent protein serine/threonine kinase KpnK, produced by Klebsiella pneumoniae strain MGH78578. FEBS Lett. (0014-5793) 2012 Srinivasan VB., Vaidyanathan V., Mondal A., Venkataramaiah M., Rajamohan G. in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Srinivasan VB., Vaidyanathan V., Mondal A., Venkataramaiah M., Rajamohan G. FEBS Lett. (0014-5793) 2012 a6tg64_klep7 Stress response kinase A Serine/threonine-protein kinase SrkA srkA KPN_04169 yihE protein protein klep7 Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) MHDKAFTFQTLRPDTIIDGLFDLGMRVDSGLTPLNSYENRVYQFQDEERHRYVVKFYRPERWSAEQILEEHQFALQLVEDEVPVAAPLLFNDSTLHQHQGFYFAVFPSLGGRQFEADNLDQMEWVGRYLGRLHQTGRKQRFTARPEIGVQEYLLEPRQVFEQATLIPSGLKADFLKATDKLIAAVMEQWHGRGNTLRLHGDCHAGNILWRDGPLFVDLDDARTGPAIQDLWMLLNGDKAEQRMQLETIVEAYEEFSPFNSDEIALIEPLRAMRLVYYLAWLLRRWDDPAFPVNFPWLTGEDYWRGQTSTFLEQVKVLQEPPLQLTPMY mint 0F8C083D5FC4040B yihe 1 KpnK 2 weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra predetermined predetermined participant predetermined self self self self purified purified phosphorylation phosphorylation reaction phosphorylation true f1 mint Autophosphorylating ability of KpnK was efficient in the presence of Mn2+ 225 as compared to the presence of Ni2+, Zn2+, Mg2+ or Ca2+226 , indicating that K. pneumoniae Ser/Thr 227 kinase utilizes manganese ion as the cofactor (Fig. 1A). The phosphorylating ability of KpnK 228 increased in a concentration (Fig. 1B) and time (Fig. 1C) dependent manner. The kinase activity 229 of KpnK was most efficient at 37°C (Fig. 1D) and between pH 7.0 and 7.5 (Fig. 1E). true