Conserved Protein Domain Family
CheD

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cd16352: CheD 
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chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins
This family contains bacterial chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). The CheD chemotaxis gene is not found in the Escherichia coli genome, but is present in many other organisms, including B. subtilis, where CheD appears to have two separate roles; it binds to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system, and it deamidates selected residues to activate chemoreceptors, enabling them to mediate amino acid chemotaxis. CheD has been shown to catalyze amide hydrolysis of specific glutaminyl side chains of the B. subtilis chemoreceptors McpA, McpB and McpC; deamination by CheD is required for the chemoreceptors to effectively transduce signals to the CheA kinase. CheD's ability to bind the receptors is controlled by CheC via a competitive binding mechanism; substituting Gln into the receptor motif of the signal-terminating phosphatase, CheC, turns the inhibitor into a receptor-modifying deamidase CheD substrate. Also, CheYp increases the affinity of CheD for CheC, controlling CheD binding to the receptors through its interactions with CheC. Thus, high levels of CheYp means CheC is a better binding target for CheD than the receptors, resulting in decreased CheA activity. The CheD structure reveals a distant homology with a class of bacterial toxins represented by the cytotoxic necrotizing factor 1 (CNF1) as well as a class of proteins of unknown function represented by B. subtilis YfiH. An invariant Cys-His pair forming a catalytic dyad is observed, and is required by the toxins for deamidation activity.
Statistics
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PSSM-Id: 319352
View PSSM: cd16352
Aligned: 476 rows
Threshold Bit Score: 76.3533
Threshold Setting Gi: 334902276
Created: 29-Mar-2013
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
heterodimerputative
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:heterodimer interface [polypeptide binding site]
Evidence:
  • Comment:complex between the receptor-modifying deamidase, CheD, and the signal-terminating phosphatase, CheC, reveals how CheD stimulates CheC phosphatase activity and CheC mimics receptor substrates to inhibit CheD
  • Structure:2F9Z: Thermotoga maritima chemotaxis deamidase CheD binds chemotaxis phosphatase CheC; contacts at 4.0A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                 ## ##                                                  
2F9Z_D         4 KKVIGIgEYAVMk-----nPGVIVTLGlGSCVAVCMRDpvakVGAMAHVMLPdsggkt-----dkpgkYADTAVKTLVEE 73
gi 170774472  31 SVQLAPgDVVVGt-----rGDRFETLL-GSCVAVVLSDprrtVGAMCHIVHAgepgrd----tpgdttFARPALQAMADG 100
gi 190685911  10 LHSLHPgEWYFGn-----nYERLHTVL-GSCVALSSWHphykIGGMCHYLLPlppghvs--skqgdcrYALNALEQMKKS 81
gi 374664940   9 HLVLMPgQLHFGr-----tAASIRTLL-GSCVAITLWHpekrLGGMCHFLLPsrtrppg---aaadgrFGDEAVGLMVER 79
gi 550801619   3 LYELLPgDVTLGr-----aGDQLKTLL-GSCVSVILTDrprtIGVMSHIVHVghpnaa----nhhntaYGSVAMAEMVRL 72
gi 633286838  27 ALNLLAgQLYFGt-----qAGTVKTLL-GSCVALVLWHpqrrIGAMCHYLLPcrqrgg----gmpdarFGDEAIGLLLQA 96
gi 694338793   7 CINLQPgEVYFSqsldgntTKELKTIL-GSCVAITIWHskskAAGMCHYLLTqeaknskatrimqkyrYGEEALNYLLKK 85
gi 699055019  19 QVFLLPgQWYFGh-----aGEIVKTVL-GSCVAITLWHpqrrIGGMCHFLLPnrrrrsd---grldgrFGDEAMALLVRE 89
gi 908205883  44 SHVLHPgDVVVAd-----qGDRLGTLL-GSCVAVVLTDprrtVGAMCHIVHAggsps-------gatsHGEPAFDAMRRG 110
gi 984916872  12 RIILLPgDVRFAq-----aPDQLCTLL-GSCLAITAWHpqrqLGGMCHFLLPqahrps-----apdgrYGSDAFELLCQL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
Feature 1                          #                                          # #            #
2F9Z_D        74 LKKmgakveRLEAKIAGGASmfes---kgmNIGARNVEAVKKHLKdfg-ikLLAEDTGgnrARSVEYNIetGKLLVR 146
gi 170774472 101 LGRiglsarLCQARVYGGGNmfpql-vkasHIGDTNGQRVLALLAaag-ieVVAQSLGgscYRKLAWVV--GPAEPE 173
gi 190685911  82 MLAcap-ldEYRIGIFGGGNmfsf--vsprSVGYENILYARQWLArek-vqLFQSDVGgrvSRSVILVLatGEIQLK 154
gi 374664940  80 LLRmgaqpnEFVAHLYGGADtmpdsartklNIGERNIEQGWSLIDkyg-fqLDGVDVGdnvPRTVMLDCssGQVNIK 155
gi 550801619  73 LYSvgftprSCEAYVFGGGNmfpkl-fshhHVGSNNVDWVLGYLEhhk-ipVLQHDLGghgYRKLLWTVgpSEPIVE 147
gi 633286838  97 IGRsstrpaDFQTHLYGGADtmpgrdgpnfNIGERNIAIGCELIDrhg-fdLQAVDVGdfvPRTVVLDLheGRIAVR 172
gi 694338793  86 MALlhp-ldEYELAIYGGSNmyps--ltspSIGEMNVIFAQNWANknklvfIKQDTLGn-nGRSVTLDLstGNVSLI 158
gi 699055019  90 IEAagthtdDYEAHVYGGADtmpdqlkdklNIGERNVEKAWTLIDeyg-fqLQSVDVGgnePRSLVMDLghGEVVLK 165
gi 908205883 111 LQRrgivpaLCEARVYGGGNmfpal-vrgrHVGEQNVAWVLERLAreg-irVAASDVGgtvYRRVDWTVgpGEPTVR 185
gi 984916872  81 MQQhasapnQYHYQIYGGSQilqpn-skesSIGSRNIKAAKQLLLnas-lnIEYEDTGggySRKVILDLstGKIGVK 155

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