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 http://mint.bio.uniroma2.it/mint yamasaki-2011a-1 Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus. 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 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 clpb-1 1143678 clpb_thet8 TClpB 1143679 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 false Stoichiometry: 6.0 direct interaction direct interaction false false false f6 mint clpb-1 1143678 clpb_thet8 TClpB 1143679 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 false Stoichiometry: 6.0 direct interaction direct interaction false false false f6 mint