DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Nature structural & molecular biology 2010 imex curation Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. Only protein-protein interactions ecolx Escherichia coli electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. DIP original experiment: DIP-217051X Nature structural & molecular biology 2010 IMEx Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Nature structural & molecular biology 2010 imex curation Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. DIP original experiment: DIP-217049X Nature structural & molecular biology 2010 IMEx Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Nature structural & molecular biology 2010 imex curation Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. Only protein-protein interactions ecolx Escherichia coli comigration in sds comigration in sds page comigration in sds weight by comassie molecular weight estimation by coomasie staining weight by comassie Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. DIP original experiment: DIP-217052X Nature structural & molecular biology 2010 IMEx Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. Nature structural & molecular biology 2010 imex curation Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. 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 Lee BG., Park EY., Lee KE., Jeon H., Sung KH., Paulsen H., Rübsamen-Schaeff H., Brötz-Oesterhelt H., Song HK. DIP original experiment: DIP-217050X Nature structural & molecular biology 2010 IMEx Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism. clpp_bacsu ATP-dependent Clp protease proteolytic subunit clpP BSU34540 yvdN Endopeptidase Clp Caseinolytic protease Stress protein G7 protein protein bacsu Bacillus subtilis MNLIPTVIEQTNRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDRDNFKSAEEALEYGLIDKILTHTEDKK 5D4D4BD548DC45A0 mint Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor rsiW. This results in the release of sigW and the transcription activation of the genes under the control of the sigma-W factor 5D4D4BD548DC45A0 bsclpp-1 3 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli covalent binding covalent binding bsclpp-2 2 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction bsclpp-3 4 5 unspecified role unspecified role unspecified role unspecified role P80244:p.Ile20Ser I19S/C mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I S Wed May 02 18:39:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile20ser' Tue Jun 30 19:37:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile20Ser' P80244:p.Leu24Ser L24S mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L S This feature has been corrected as a result of our quality control procedures. The original label was 'L24S'. Wed May 02 18:06:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu24ser' Tue Jun 30 18:59:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu24Ser' P80244:p.Phe50Ser F49S mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F S Wed May 02 18:49:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe50ser' Tue Jun 30 19:44:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe50Ser' P80244:p.Ile20Cys mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain I C Wed May 02 18:32:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile20cys' Tue Jun 30 19:54:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile20Cys' ecolx Escherichia coli direct interaction direct interaction bsclpp-4 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction