DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure (London, England : 1993) 2009 imex curation Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. DIP original experiment: DIP-131984X Structure (London, England : 1993) 2009 IMEx Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure (London, England : 1993) 2009 imex curation Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. Only protein-protein interactions in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. DIP original experiment: DIP-131983X Structure (London, England : 1993) 2009 IMEx Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure (London, England : 1993) 2009 imex curation Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. Only protein-protein interactions in vitro In vitro phosphotransferase phosphotransferase assay phosphotransferase predetermined predetermined participant predetermined Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. DIP original experiment: DIP-131985X Structure (London, England : 1993) 2009 IMEx Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure (London, England : 1993) 2009 imex curation Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. DIP original experiment: DIP-131987X Structure (London, England : 1993) 2009 IMEx Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure of PAS-linked histidine kinase and the response regulator complex. Structure (London, England : 1993) 2009 imex curation Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., Shiro Y. DIP original experiment: DIP-131986X Structure (London, England : 1993) 2009 IMEx Structure of PAS-linked histidine kinase and the response regulator complex. q9x181_thema TM_1360 protein protein thema Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) MKRILVVDDEPNIRELLKEELQEEGYEIDTAENGEEALKKFFSGNYDLVILDIEMPGISGLEVAGEIRKKKKDAKIILLTAYSHYRSDLSSWAADEYVVKSFNFDELKEKVKKLLS 145302A42E89EB78 q9x180_thema TM_1359 protein protein thema Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) MVPERLKQIKGIRILESEDEIPQEGFTCRFGKHTVVANDEESFEIVRLYKRLTVYELLLSLVDSICVHPKEEALRFSLKKVREFLDAEEVYLIEGDASYSSKGEKLSIDEIKKKHPGASVREWRNKLHLVVVREGAFDEEEEVLCTKLLEFIGNVSEKLWRLKEEVQKLKKSYEEQLKVSEIQKEHIKKMRIIYYVSQAMRSVYDPNNLYRVILLSLVSERGFNFDRAVLLKKDEGTGSLMVVSAVGGDTLQEHEELKRYLRKRTLRYTDLVQFLREEALTFSFETKFNEKIRGKRFYYREHPIFERVVLRKSIVRTSRETLEKIRYEIEDVISILENDEFIVFPLVGRWDTLGVVVVDNKFSKKEVTDLDLDVLKLFSESAGLALENAYNYENLRKKTLDLQRQNELVEHLRNFSESILESLETAIITLSKDGRITEWNKKAEQLFGLKKENVLGRRLKDLPDFEEIGSVAESVFENKEPVFLNFYKFGERYFNIRFSPFRNAKTQLLEGVIITIDDVTELYKYEEERKRRERLSILGEMTARVAHEIRNPITIIGGFIMRMKKHLDDPETLKKYINIITNELSRLETIVKEILEYSKERQVLEFTEFNLNELIREVYVLFEEKIRKMNIDFCFETDNEDLRVEADRTRIKQVLINLVQNAIEATGENGKIKITSEDMYTKVRVSVWNSGPPIPEELKEKIFSPFFTTKTQGTGLGLSICRKIIEDEHGGKIWTENRENGVVFIFEIPKTPEKR 61D11F4FDC4D0E9E thka-trra-1 2 6 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 7 enzyme enzyme unspecified role unspecified role Region 408-755 Region 408-755 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli dephosphorylation dephosphorylation reaction dephosphorylation thka-trra-2 5 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 517-755 Region 517-755 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction thka-trra-3 1 6 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 7 enzyme enzyme unspecified role unspecified role Region 408-755 Region 408-755 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation thka-trra-4 4 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 408-755 Region 408-755 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction thka-trra-5 3 6 phosphate acceptor phosphate acceptor unspecified role unspecified role ecolx Escherichia coli 7 phosphate donor phosphate donor unspecified role unspecified role Region 517-755 Region 517-755 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphotransfer phosphotransfer reaction phosphotransfer