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 Mutations of the domain forming the dimeric interface of the ArdA protein affect dimerisation and antimodification activity but not antirestriction activity Mutations of the domain forming the dimeric interface of the ArdA protein affect dimerisation and antimodification activity but not antirestriction activity FEBS J. (1742-464X) 2013 imex curation Roberts G.A., Chen K., Bower E.K., Madrzak J., Woods A., Barker A.M., Cooper L.P., White J.H., Blakely G.W., Manfield I., Dryden D.T. david.dryden@ed.ac.uk 09-Aug-2013: Contacted by IntAct-Help. 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 Roberts G.A., Chen K., Bower E.K., Madrzak J., Woods A., Barker A.M., Cooper L.P., White J.H., Blakely G.W., Manfield I., Dryden D.T. david.dryden@ed.ac.uk Accepted 2013-JUL-31 by MARTA 09-Aug-2013: Contacted by IntAct-Help. FEBS J. (1742-464X) 2013 Only protein-protein interactions imex curation Mutations of the domain forming the dimeric interface of the ArdA protein affect dimerisation and antimodification activity but not antirestriction activity Mutations of the domain forming the dimeric interface of the ArdA protein affect dimerisation and antimodification activity but not antirestriction activity FEBS J. (1742-464X) 2013 imex curation Roberts G.A., Chen K., Bower E.K., Madrzak J., Woods A., Barker A.M., Cooper L.P., White J.H., Blakely G.W., Manfield I., Dryden D.T. david.dryden@ed.ac.uk 09-Aug-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Roberts G.A., Chen K., Bower E.K., Madrzak J., Woods A., Barker A.M., Cooper L.P., White J.H., Blakely G.W., Manfield I., Dryden D.T. david.dryden@ed.ac.uk Accepted 2013-JUL-31 by MARTA 09-Aug-2013: Contacted by IntAct-Help. FEBS J. (1742-464X) 2013 Only protein-protein interactions imex curation q47730_entfl EY666_08835 CUM81_08350 H7D67_09300 BZG32_16025 EGW70_06200 KUB3007_C27220 GTI81_09985 protein protein entfl Enterococcus faecalis Streptococcus faecalis MDDMQVYIANLGKYNEGELVGAWFTFPIDFEEVKEKIGLNDEYEEYAIHDYELPFTVDEYTSIGELNRLWEMVSELPEELQSELSALLTHFSSIEELSEHQEDIIIHSDCDDMYDVARYYIEETGALGEVPASLQNYIDYQAYGRDLDLSGTFISTNHGIFEIVY 104E4ECB7E6828CB q47730 1 ArdA 3 unspecified role unspecified role neutral component neutral component purified purified Q47730:p.[Asp109Asn;Asp111_Asp112delinsAsnAsn;Asp115Asn] mutation disrupting mutation disrupting interaction mutation disrupting predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain D N certain certain sequence position certain certain certain sequence position certain D N certain certain sequence position certain certain certain sequence position certain DD NN Fri Jul 22 10:56:02 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'asp109asn,asp111asn,asp112asn,asp115asn' Wed May 02 19:37:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp109asn,asp_asp111-112asn_asn,asp115asn' Tue Jun 30 20:23:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp109Asn;Asp111_Asp112delinsAsnAsn;Asp115Asn]' direct interaction direct interaction f2 sf5 If the monomer-dimer 179 equilibrium model for ArdA is correct then it would appear that Mut5 and L127E ArdA are 180 monomers at most concentrations. The Mut6 protein behaved in the same manner as the wt Orf18 181 ArdA protein showing a decrease in apparent molecular mass as concentration decreased, Figure 2 182 (and Supplementary Figure S5d) q47730-1 1 ArdA 3 unspecified role unspecified role neutral component neutral component purified purified Q47730:p.Leu127Glu mutation disrupting mutation disrupting interaction mutation disrupting predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain L E Wed May 02 17:56:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu127glu' Tue Jun 30 18:50:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu127Glu' direct interaction direct interaction f2 sf5 If the monomer-dimer 179 equilibrium model for ArdA is correct then it would appear that Mut5 and L127E ArdA are 180 monomers at most concentrations. The Mut6 protein behaved in the same manner as the wt Orf18 181 ArdA protein showing a decrease in apparent molecular mass as concentration decreased, Figure 2 182 (and Supplementary Figure S5d) q47730-2 2 ArdA 3 unspecified role unspecified role neutral component neutral component purified purified Q47730:p.[Asp109Asn;Asp111_Asp112delinsAsnAsn;Asp115Asn] mutation disrupting mutation disrupting interaction mutation disrupting predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain D N certain certain sequence position certain certain certain sequence position certain D N certain certain sequence position certain certain certain sequence position certain DD NN Fri Jul 22 10:52:17 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'asp109asn,asp111asn,asp112asn,asp115asn' Wed May 02 15:02:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp109asn,asp_asp111-112asn_asn,asp115asn' Tue Jun 30 20:22:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp109Asn;Asp111_Asp112delinsAsnAsn;Asp115Asn]' direct interaction direct interaction f3 sf6 t2 Individual analyses for L127E ArdA showed that the molecular mass changed with respect to concentration and the global analysis was inappropriate, Table 2. At low concentrations the molecular mass was between 21.2 and 17.0 kDa indicating that it is a monomer in solution at these concentrations q47730-2 2 ArdA 3 unspecified role unspecified role neutral component neutral component purified purified Q47730:p.Leu127Glu mutation disrupting mutation disrupting interaction mutation disrupting predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain L E Wed May 02 15:23:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu127glu' Tue Jun 30 15:56:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu127Glu' direct interaction direct interaction f3 sf6 t2 Individual analyses for L127E ArdA showed that the molecular mass changed with respect to concentration and the global analysis was inappropriate, Table 2. At low concentrations the molecular mass was between 21.2 and 17.0 kDa indicating that it is a monomer in solution at these concentrations