DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature structural & molecular biology 2012 imex curation Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. DIP original experiment: DIP-250769X Nature structural & molecular biology 2012 IMEx Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature structural & molecular biology 2012 imex curation Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. DIP original experiment: DIP-250768X Nature structural & molecular biology 2012 IMEx Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature structural & molecular biology 2012 imex curation Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. Only protein-protein interactions in vitro In vitro protein folding protein folding/unfolding protein folding predetermined predetermined participant predetermined Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. DIP original experiment: DIP-250770X Nature structural & molecular biology 2012 IMEx Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature structural & molecular biology 2012 imex curation Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. 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 Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. DIP original experiment: DIP-250767X Nature structural & molecular biology 2012 IMEx Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature structural & molecular biology 2012 imex curation Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. Only protein-protein interactions in vitro In vitro protein folding protein folding/unfolding protein folding predetermined predetermined participant predetermined Malet H., Canellas F., Sawa J., Yan J., Thalassinos K., Ehrmann M., Clausen T., Saibil HR. DIP original experiment: DIP-250771X Nature structural & molecular biology 2012 IMEx Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. degp_ecoli Periplasmic serine endoprotease DegP degP htrA ptd b0161 JW0157 Heat shock protein DegP Protease Do protein protein ecoli Escherichia coli (strain K12) MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ DIP protein P0C0V0 original sequence version: 94 DIP protein P0C0V0 original sequence version: 75 DIP protein P0C0V0 original sequence version: 62 DIP protein P0C0V0 original sequence version: 84 DIP protein P0C0V0 original sequence version: 67 5482E596F74B6D5F degq_ecoli Periplasmic pH-dependent serine endoprotease DegQ degQ hhoA b3234 JW3203 Protease Do protein protein ecoli Escherichia coli (strain K12) MKKQTQLLSALALSVGLTLSASFQAVASIPGQVADQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKKFFGDDLPDQPAQPFEGLGSGVIINASKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIVSALGRSGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPGSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAEMITPALEGATLSDGQLKDGGKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLMR DIP protein P39099 original sequence version: 102 DIP protein P39099 original sequence version: 107 DIP protein P39099 original sequence version: null 6A090F93AC021C83 amy1_ecoli Periplasmic alpha-amylase 1,4-alpha-D-glucan glucanohydrolase malS b3571 JW3543 protein protein ecoli Escherichia coli (strain K12) MKLAACFLTLLPGFAVAASWTSPGFPAFSEQGTGTFVSHAQLPKGTRPLTLNFDQQCWQPADAIKLNQMLSLQPCSNTPPQWRLFRDGEYTLQIDTRSGTPTLMISIQNAAEPVASLVRECPKWDGLPLTVDVSATFPEGAAVRDYYSQQIAIVKNGQIMLQPAATSNGLLLLERAETDTSAPFDWHNATVYFVLTDRFENGDPSNDQSYGRHKDGMAEIGTFHGGDLRGLTNKLDYLQQLGVNALWISAPFEQIHGWVGGGTKGDFPHYAYHGYYTQDWTNLDANMGNEADLRTLVDSAHQRGIRILFDVVMNHTGYATLADMQEYQFGALYLSGDEVKKSLGERWSDWKPAAGQTWHSFNDYINFSDKTGWDKWWGKNWIRTDIGDYDNPGFDDLTMSLAFLPDIKTESTTASGLPVFYKNKMDTHAKAIDGYTPRDYLTHWLSQWVRDYGIDGFRVDTAKHVELPAWQQLKTEASAALREWKKANPDKALDDKPFWMTGEAWGHGVMQSDYYRHGFDAMINFDYQEQAAKAVDCLAQMDTTWQQMAEKLQGFNVLSYLSSHDTRLFREGGDKAAELLLLAPGAVQIFYGDESSRPFGPTGSDPLQGTRSDMNWQDVSGKSAASVAHWQKISQFRARHPAIGAGKQTTLLLKQGYGFVREHGDDKVLVVWAGQQ DIP protein P25718 original sequence version: 110 DIP protein P25718 original sequence version: null 980110EFA45E011D degq-4 4 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction degp-mals-1 5 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction degq-5 2 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction degq-6 1 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction degq-mals-1 3 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction