mpidb The Microbial Protein Interaction Database Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli. Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli. J. Bacteriol. (0021-9193) 2011 imex curation Thakor H., Nicholas S., Porter I.M., Hand N., Stewart R.C. The rapid decrease in fluorescence following mixing of P-CheA with CheY reflects decreased emission signal from CheY residue trp-58 as the protein becomes phosphorylated on Asp-57. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro phosphotransferase phosphotransferase assay phosphotransferase predetermined predetermined participant predetermined Thakor H., Nicholas S., Porter I.M., Hand N., Stewart R.C. The rapid decrease in fluorescence following mixing of P-CheA with CheY reflects decreased emission signal from CheY residue trp-58 as the protein becomes phosphorylated on Asp-57. Accepted 2012-DEC-10 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli. Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli. J. Bacteriol. (0021-9193) 2011 imex curation Thakor H., Nicholas S., Porter I.M., Hand N., Stewart R.C. The rapid decrease in fluorescence following mixing of P-CheA with CheY reflects decreased emission signal from CheY residue trp-58 as the protein becomes phosphorylated on Asp-57. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence tag fluorescence tag visualisation by fluorescence tag fluorescence Thakor H., Nicholas S., Porter I.M., Hand N., Stewart R.C. The rapid decrease in fluorescence following mixing of P-CheA with CheY reflects decreased emission signal from CheY residue trp-58 as the protein becomes phosphorylated on Asp-57. Accepted 2012-DEC-10 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation chey_ecoli Chemotaxis protein CheY cheY b1882 JW1871 protein protein ecoli Escherichia coli (strain K12) MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM DIP protein P0AE67 original sequence version: 95 DIP protein P0AE67 original sequence version: 56 DIP protein P0AE67 original sequence version: 96 E4B60B8A73DA14DC chea_ecoli Chemotaxis protein CheA cheA b1888 JW1877 protein protein ecoli Escherichia coli (strain K12) MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYICQALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA DIP protein P07363 original sequence version: 116 DIP protein P07363 original sequence version: 144 DIP protein P07363 original sequence version: 157 009B824154E269B4 chey-chea-4 2 3 unspecified role unspecified role bait bait p0ae67-- P0AE67-- fluorescent prot tag fluorescent protein tag fluorescent prot tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 4 unspecified role unspecified role prey prey P07363:p.Glu178Ala P07363-178-178 mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain E A Wed May 02 19:45:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu178ala' Tue Jun 30 19:12:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu178Ala' region P07363-159-227 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P07363:p.Phe214Ala P07363-214-214 mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain F A Wed May 02 16:48:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe214ala' Tue Jun 30 19:43:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe214Ala' P07363:p.Ile216Ala P07363-216-216 mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain I A Wed May 02 16:29:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile216ala' Tue Jun 30 20:09:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile216Ala' n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P07363:p.Glu171Ala P07363-171-171 mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain E A Wed May 02 15:39:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu171ala' Tue Jun 30 19:31:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu171Ala' c-terminal flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli direct interaction direct interaction figure 2 chea-chey-3 1 3 phosphate acceptor phosphate acceptor unspecified role unspecified role 4 phosphate donor phosphate donor unspecified role unspecified role region P07363-- phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P07363:p.Phe214Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain F A Wed May 02 17:46:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe214ala' Tue Jun 30 15:37:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe214Ala' phosphotransfer phosphotransfer reaction phosphotransfer figure 4