DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature structural & molecular biology 2015 imex curation Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. Only protein-protein interactions ecolx Escherichia coli comigration in sds comigration in sds page comigration in sds weight by staining molecular weight estimation by staining weight by staining Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. DIP original experiment: DIP-266005X Nature structural & molecular biology 2015 IMEx Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature structural & molecular biology 2015 imex curation Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. DIP original experiment: DIP-266004X Nature structural & molecular biology 2015 IMEx Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature structural & molecular biology 2015 imex curation Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. DIP original experiment: DIP-266007X Nature structural & molecular biology 2015 IMEx Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature structural & molecular biology 2015 imex curation Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. Only protein-protein interactions ecolx Escherichia coli crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Stinson BM., Baytshtok V., Schmitz KR., Baker TA., Sauer RT. DIP original experiment: DIP-266006X Nature structural & molecular biology 2015 IMEx Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. clpp_ecoli ATP-dependent Clp protease proteolytic subunit clpP lopP Endopeptidase Clp Caseinolytic protease Protease Ti Heat shock protein F21.5 b0437 JW0427 protein protein ecoli Escherichia coli (strain K12) MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN DIP protein P0A6G7 original sequence version: 51 DIP protein P0A6G7 original sequence version: 96 A7843D036C8CB3C2 clpx_ecoli ATP-dependent Clp protease ATP-binding subunit ClpX clpX lopC b0438 JW0428 ATP-dependent unfoldase ClpX protein protein ecoli Escherichia coli (strain K12) MTDKRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSKPLLIYGKPEAQQASGE DIP protein P0A6H1 original sequence version: 53 DIP protein P0A6H1 original sequence version: 90 DIP protein P0A6H1 original sequence version: 101 9DEF1B0786E42B6F clpp-clpx-3 3 5 unspecified role unspecified role unspecified role unspecified role P0A6G7:p.Tyr74Trp Y60W mutation mutation certain certain sequence position certain certain certain sequence position certain Y W Fri Jul 28 10:49:53 BST 2017 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr60trp' Wed May 02 14:35:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr74trp' Tue Jun 30 17:03:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr74Trp' ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 61-424 Region 61-424 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction clpx-4 2 6 unspecified role unspecified role unspecified role unspecified role Region 61-424 Region 61-424 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction clpx-5 1 6 unspecified role unspecified role unspecified role unspecified role Region 61-424 Region 61-424 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction clpx-6 4 6 unspecified role unspecified role unspecified role unspecified role Region 61-424 Region 61-424 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P0A6H1:p.[Asp144Cys;Lys330Cys] D144C/K330C mutation mutation certain certain sequence position certain certain certain sequence position certain K C certain certain sequence position certain certain certain sequence position certain D C This feature has been corrected as a result of our quality control procedures. The original label was 'D144C/K330C'. Wed May 02 16:46:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp144cys,lys330cys' Tue Jun 30 17:13:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp144Cys;Lys330Cys]' ecolx Escherichia coli direct interaction direct interaction