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 Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus. Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus. FEBS J. (1742-464X) 2011 imex curation Yamasaki T., Nakazaki Y., Yoshida M., Watanabe YH. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Yamasaki T., Nakazaki Y., Yoshida M., Watanabe YH. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation clpb_thet8 Chaperone protein ClpB clpB TTHA1487 protein protein thet8 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) MNLERWTQAAREALAQAQVLAQRMKHQAIDLPHLWAVLLKDERSLAWRLLEKAGADPKALKELQERELARLPKVEGAEVGQYLTSRLSGALNRAEALMEELKDRYVAVDTLVLALAEATPGLPGLEALKGALKELRGGRTVQTEHAESTYNALEQYGIDLTRLAAEGKLDPVIGRDEEIRRVIQILLRRTKNNPVLIGEPGVGKTAIVEGLAQRIVKGDVPEGLKGKRIVSLQMGSLLAGAKYRGEFEERLKAVIQEVVQSQGEVILFIDELHTVVGAGKAEGAVDAGNMLKPALARGELRLIGATTLDEYREIEKDPALERRFQPVYVDEPTVEETISILRGLKEKYEVHHGVRISDSAIIAAATLSHRYITERRLPDKAIDLIDEAAARLRMALESAPEEIDALERKKLQLEIEREALKKEKDPDSQERLKAIEAEIAKLTEEIAKLRAEWEREREILRKLREAQHRLDEVRREIELAERQYDLNRAAELRYGELPKLEAEVEALSEKLRGARFVRLEVTEEDIAEIVSRWTGIPVSKLLEGEREKLLRLEEELHKRVVGQDEAIRAVADAIRRARAGLKDPNRPIGSFLFLGPTGVGKTELAKTLAATLFDTEEAMIRIDMTEYMEKHAVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSHGRTVDFRNTVIILTSNLGSPLILEGLQKGWPYERIRDEVFKVLQQHFRPEFLNRLDEIVVFRPLTKEQIRQIVEIQLSYLRARLAEKRISLELTEAAKDFLAERGYDPVFGARPLRRVIQRELETPLAQKILAGEVKEGDRVQVDVGPAGLVFAVPARVEA DIP protein Q9RA63 original sequence version: 92 mint Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of clpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by dnaK FB9A39BB040363E0 clpb-1 1 TClpB 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q9RA63:p.Arg322Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A Tue Jul 12 10:22:03 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 18:50:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg322ala' Tue Jun 30 18:01:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg322Ala' Stoichiometry: 6.0 direct interaction direct interaction f6 mint Gel filtration analyses were performed at 55 °C in the presence of 2 mM ATP because stable hexamerization of TClpB is dependent on high temperature and ATP. When the elution buffer contained 150 mM KCl, the elution time of the 1R/A(P1) and 1R/A(P2) were slightly delayed compared to wild-type (Figure 6A). At a higher concentration of KCl (300 mM), these delays increased, particularly in the case of 1R/A(P2) (Figure 6B). In both conditions, the elution profiles of 2R/A were same as that of wild-type. clpb-1 1 TClpB 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q9RA63:p.Arg323Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A Tue Jul 12 10:22:13 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 18:28:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg323ala' Tue Jun 30 20:07:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg323Ala' Stoichiometry: 6.0 direct interaction direct interaction f6 mint Gel filtration analyses were performed at 55 °C in the presence of 2 mM ATP because stable hexamerization of TClpB is dependent on high temperature and ATP. When the elution buffer contained 150 mM KCl, the elution time of the 1R/A(P1) and 1R/A(P2) were slightly delayed compared to wild-type (Figure 6A). At a higher concentration of KCl (300 mM), these delays increased, particularly in the case of 1R/A(P2) (Figure 6B). In both conditions, the elution profiles of 2R/A were same as that of wild-type.