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 Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. PLoS pathogens 2014 imex curation Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org 05-Jan-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protein kinase assay protein kinase assay ms participant Identification by mass spectrometry ms participant Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org Accepted 2020-NOV-12 AT 15:48 GMT AT 15:48 GMT by LUANA PLoS pathogens 2014 Only protein-protein interactions imex curation imex curation Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. PLoS pathogens 2014 imex curation Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org 05-Jan-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org Accepted 2020-NOV-12 AT 15:48 GMT AT 15:48 GMT by LUANA PLoS pathogens 2014 Only protein-protein interactions imex curation imex curation Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. PLoS pathogens 2014 imex curation Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org 05-Jan-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protein kinase assay protein kinase assay western blot western blot Immuno blot Immuno blot Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA., Horstmann N., Saldaña M., Sahasrabhojane P., Yao H., Su X., Thompson E., Koller A., Shelburne SA. shelburne@mdanderson.org Accepted 2020-NOV-12 AT 15:48 GMT AT 15:48 GMT by LUANA PLoS pathogens 2014 Only protein-protein interactions imex curation imex curation a0a0h2uvv3_strp3 Non-specific serine/threonine protein kinase SpyM3_1369 protein protein Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) MIQIGKLFAGRYRILKSIGRGGMADVYLANDLILDNEDVAIKVLRTNYQTDQVAVARFQREARAMAELNHPNIVAIRDIGEEDGQQFLVMEYVDGADLKRYIQNHAPLSNNEVVRIMEEVLSAMTLAHQKGIVHRDLKPQNILLTKEGVVKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATIQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSIIEENHNVPQALENVVIRATAKKLSDRYGSTFEMSRDLMTALSYNRSRERKIVFEDVESTKPLPKVASGPTASVKLSPPTPTVLTQESRLDQTNQTDALQPPTKKKKSGRFLGTLFKILFSFFIVGVALFTYLILTKPTSVKVPNVAGTSLKVAKQELYDVGLKVGKIRQIESDTVAEGNVVRTDPKAGTAKRQGSSITLYVSIGNKGFDMENYKGLDYQEAMNSLIETYGVPKSKIKIERIVTNEYPENTVISQSPSAGDKFNPNGKSKITLSVAVSDTITMPMVTEYSYADAVNTLTALGIDASRIKAYVPSSSSATGFVPIHSPSSKAIVSGQSPYYGTSLSLSDKGEISLYLYPEETHSSSSSSSSTSSSNSSSTNDSTAPGSNTELSPSETTAQTP 57E0AD519E63B864 j7m6z1_strp1 covR M1GAS476_0346 protein protein Streptococcus pyogenes M1 476 Streptococcus pyogenes M1 476 MTKKILIIEDEKNLARFVSLELQHEGYEVIVEVNGREGLETALEKEFDLILLDLMLPEMDGFEVTRRLQTEKTTYIMMMTARDSIMDVVAGLDRGADDYIVKPFAIEELLARIRAIFRRQDIESEKKVPSQGIYRDLVLNPQNRSVNRGDDEISLTKREYDLLNILMTNMNRVMTREELLSNVWKYDEAVETNVVDVYIRYLRGKIDIPGKESYIQTVRGMGYVIREK 0D501427A2CD3F95 covr-1 2 5 unspecified role unspecified role neutral component neutral component purified purified asp53 modasp modified L-aspartic acid residue ModAsp certain certain sequence position certain certain certain sequence position certain J7M6Z1:p.Asp53Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain D A Sun Dec 13 19:13:36 GMT 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'J7M6Z1:p.asp53ala' ecolx Escherichia coli direct interaction direct interaction fig. 1 a,b Phosphorylation of recombinant CovR by the small molecule phosphodonor acetyl phosphate induces homodimerization, which results in slower migration on a native polyacrylamide gel (Figure 1A). An alanine substitution at D53 abrogates phosphorylation at the altered site [22] and thereby homodimerization (Figure 1A). a0a0h2uvv3_strp3-covr-1 1 5 enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified thr65 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain resulting-ptm resulting-ptm resulting ptm resulting-ptm ecolx Escherichia coli 4 enzyme enzyme unspecified role unspecified role purified purified region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation fig. 2 a0a0h2uvv3_strp3-covr-2 3 5 enzyme target enzyme target substrate substrate neutral component neutral component purified purified J7M6Z1:p.Thr65Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain T A J7M6Z1:p.Thr65Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain T E J7M6Z1:p.Asp53Ala mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain D A ecolx Escherichia coli 4 enzyme enzyme neutral component neutral component purified purified region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation fig. 3 Consistent with our mass spectrometry data, incubation of CovR-T65A with StkKD resulted in no detectable phosphorylation using the Phos-tag assay (Figure 3A). In contrast, StkKD was able to phosphorylate CovR with an alanine substituted for threonine at position 73 (CovR-T73A, data not shown), further supporting the specific role of T65 in Stk-dependent CovR phosphorylation.