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Conserved domains on  [gi|2191953106|ref|WP_237810589|]
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MULTISPECIES: chemotaxis protein CheX [Anoxybacillus]

Protein Classification

chemotaxis protein CheX( domain architecture ID 14438278)

chemotaxis protein CheX dephosphorylates CheY to control levels of CheY-P

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheX cd17906
chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very ...
 5-148 1.44e-36

chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.


:

Pssm-ID: 381734 [Multi-domain]  Cd Length: 148  Bit Score: 122.64  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   5 EKITTILNGTIESIRSVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGETMFGM--PLEGEM 82
Cdd:cd17906     2 EYINPFIEATKEVFKTMLGLEVEPGKPYLKKDPFLSGDVSGIIGITGDLKGSVIISFSEETALKIASAMLGEevTELDEM 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2191953106  83 LESFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQ-TKIYGFD-KAFRVPIHFEnKGELQLILTI 148
Cdd:cd17906    82 VKDAIGELANMIAGNAKTKLSEKGIDIDISPPTVITGKnHKISSPKgPTIVIPFETE-GGEFEVEIAL 148
 
Name Accession Description Interval E-value
CheX cd17906
chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very ...
 5-148 1.44e-36

chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.


Pssm-ID: 381734 [Multi-domain]  Cd Length: 148  Bit Score: 122.64  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   5 EKITTILNGTIESIRSVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGETMFGM--PLEGEM 82
Cdd:cd17906     2 EYINPFIEATKEVFKTMLGLEVEPGKPYLKKDPFLSGDVSGIIGITGDLKGSVIISFSEETALKIASAMLGEevTELDEM 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2191953106  83 LESFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQ-TKIYGFD-KAFRVPIHFEnKGELQLILTI 148
Cdd:cd17906    82 VKDAIGELANMIAGNAKTKLSEKGIDIDISPPTVITGKnHKISSPKgPTIVIPFETE-GGEFEVEIAL 148
CheX COG1406
Chemotaxis protein CheX, a CheY~P-specific phosphatase [Cell motility];
7-151 2.39e-34

Chemotaxis protein CheX, a CheY~P-specific phosphatase [Cell motility];


Pssm-ID: 441016 [Multi-domain]  Cd Length: 155  Bit Score: 117.31  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   7 ITTILNGTIESIRSVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGETMFGMPLE--GEMLE 84
Cdd:COG1406     6 INPFIEATIEVLKTMLGLEVEVGKPYLKEDPVPSGDVSGVIGLTGDIKGSVIISFPEETALKIASAMLGEEVEeiDEMVK 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106  85 SFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQTKIYGF---DKAFRVPIHFENkGELQLILTIDNE 151
Cdd:COG1406    86 DAVGELANMIAGNAKTELSEKGYDIDISPPTVITGENHSISHpsgGPVLVIPFTTEG-GKFEIEVALEEG 154
CheX_Thtogales NF041094
CheY-P phosphatase CheX;
10-148 2.56e-15

CheY-P phosphatase CheX;


Pssm-ID: 469020 [Multi-domain]  Cd Length: 152  Bit Score: 68.48  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106  10 ILNGTIESIRSVIPLAM----TIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIE-GHETMFGSIGETMFGMPLEG--EM 82
Cdd:NF041094    5 IINALLAAVVNTFKALLkikpKVGKPQVLKEIEPKYDVVTVIGFTGVLEGNLIYSfSEETALKIVSKMMGGMEYDEldEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2191953106  83 LESFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQT-KIYGFDKAFRVPIHFENKGELQLILTI 148
Cdd:NF041094   85 ALSAIGELGNMISGAIAMNLEKIGYKIDITPPTVVRGKDlKVSVEGLILKLPVSIFEEEEMELYLVI 151
CheX pfam13690
Chemotaxis phosphatase CheX; CheX is very closely related to the CheC chemotaxis phosphatase, ...
 43-119 4.42e-08

Chemotaxis phosphatase CheX; CheX is very closely related to the CheC chemotaxis phosphatase, but it dimerizes in a different way, via a continuous beta sheet between the subunits. CheC and CheX both dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. The ability of bacteria to modulate their swimming behaviour in the presence of external chemicals (nutrients and repellents) is one of the most rudimentary behavioural responses known, but the the individual components are very sensitively tuned.


Pssm-ID: 433406 [Multi-domain]  Cd Length: 94  Bit Score: 48.02  E-value: 4.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2191953106  43 ISVLIGMTGDLRGRLMIEGHETMFGSIGEtMFGMPLEG--EMLESFTGELGNMIAGNLATivfQKGITIDITPPTVLVG 119
Cdd:pfam13690   1 VTGIIGLAGDISGLVILSFPEALALKIAS-ALGEDEEEldEDVLDAVGELANMIAGNAKS---KLGEPVKLSPPSVIDG 75
 
Name Accession Description Interval E-value
CheX cd17906
chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very ...
 5-148 1.44e-36

chemotaxis phosphatase CheX; This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.


Pssm-ID: 381734 [Multi-domain]  Cd Length: 148  Bit Score: 122.64  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   5 EKITTILNGTIESIRSVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGETMFGM--PLEGEM 82
Cdd:cd17906     2 EYINPFIEATKEVFKTMLGLEVEPGKPYLKKDPFLSGDVSGIIGITGDLKGSVIISFSEETALKIASAMLGEevTELDEM 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2191953106  83 LESFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQ-TKIYGFD-KAFRVPIHFEnKGELQLILTI 148
Cdd:cd17906    82 VKDAIGELANMIAGNAKTKLSEKGIDIDISPPTVITGKnHKISSPKgPTIVIPFETE-GGEFEVEIAL 148
CheX COG1406
Chemotaxis protein CheX, a CheY~P-specific phosphatase [Cell motility];
7-151 2.39e-34

Chemotaxis protein CheX, a CheY~P-specific phosphatase [Cell motility];


Pssm-ID: 441016 [Multi-domain]  Cd Length: 155  Bit Score: 117.31  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   7 ITTILNGTIESIRSVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGETMFGMPLE--GEMLE 84
Cdd:COG1406     6 INPFIEATIEVLKTMLGLEVEVGKPYLKEDPVPSGDVSGVIGLTGDIKGSVIISFPEETALKIASAMLGEEVEeiDEMVK 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106  85 SFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQTKIYGF---DKAFRVPIHFENkGELQLILTIDNE 151
Cdd:COG1406    86 DAVGELANMIAGNAKTELSEKGYDIDISPPTVITGENHSISHpsgGPVLVIPFTTEG-GKFEIEVALEEG 154
CheX_Thtogales NF041094
CheY-P phosphatase CheX;
10-148 2.56e-15

CheY-P phosphatase CheX;


Pssm-ID: 469020 [Multi-domain]  Cd Length: 152  Bit Score: 68.48  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106  10 ILNGTIESIRSVIPLAM----TIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIE-GHETMFGSIGETMFGMPLEG--EM 82
Cdd:NF041094    5 IINALLAAVVNTFKALLkikpKVGKPQVLKEIEPKYDVVTVIGFTGVLEGNLIYSfSEETALKIVSKMMGGMEYDEldEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2191953106  83 LESFTGELGNMIAGNLATIVFQKGITIDITPPTVLVGQT-KIYGFDKAFRVPIHFENKGELQLILTI 148
Cdd:NF041094   85 ALSAIGELGNMISGAIAMNLEKIGYKIDITPPTVVRGKDlKVSVEGLILKLPVSIFEEEEMELYLVI 151
CheX pfam13690
Chemotaxis phosphatase CheX; CheX is very closely related to the CheC chemotaxis phosphatase, ...
 43-119 4.42e-08

Chemotaxis phosphatase CheX; CheX is very closely related to the CheC chemotaxis phosphatase, but it dimerizes in a different way, via a continuous beta sheet between the subunits. CheC and CheX both dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. The ability of bacteria to modulate their swimming behaviour in the presence of external chemicals (nutrients and repellents) is one of the most rudimentary behavioural responses known, but the the individual components are very sensitively tuned.


Pssm-ID: 433406 [Multi-domain]  Cd Length: 94  Bit Score: 48.02  E-value: 4.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2191953106  43 ISVLIGMTGDLRGRLMIEGHETMFGSIGEtMFGMPLEG--EMLESFTGELGNMIAGNLATivfQKGITIDITPPTVLVG 119
Cdd:pfam13690   1 VTGIIGLAGDISGLVILSFPEALALKIAS-ALGEDEEEldEDVLDAVGELANMIAGNAKS---KLGEPVKLSPPSVIDG 75
CheC_CheX_FliY cd16353
CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins ...
 2-119 4.88e-07

CheC/CheX/FliY (CXY) family phosphatases; The CXY family includes CheY-P-hydrolyzing proteins that function in bacterial chemotaxis, which involves cellular processes that control the movement of organisms toward favorable environments via rotating flagella, which in turn determines the sense of rotation by the intracellular response regulator CheY. When phosphorylated, CheY-P interacts directly with the flagellar motor, and this signal is terminated by the CXY family of phosphatases (Escherichia coli uses CheZ). CheC acts as a weak CheY-P phosphatase but increases activity in the presence of CheD. Bacillus subtilis has only CheC and FliY while many systems also have CheX. CheC and CheX appear to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. Unlike CheC and CheX, FliY is localized in the flagellar switch complex, which also contains the stator-coupling protein FliG and the target of CheY-P, FliM. CheC, CheX, and FliY phosphatases share a consensus sequence ([DS]xxxExxNx(22)P) with four conserved residues thought to form the phosphatase active site. CheC class I and FliY each have two active sites, while CheC class II and III, and CheX have only one. This family also includes FliM, a component of the flagellar switch complex and a target of CheY, which lacks the phosphatase active site consensus sequence, and is not a CheY phosphatase.


Pssm-ID: 381732 [Multi-domain]  Cd Length: 162  Bit Score: 46.72  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2191953106   2 ALGEKITTILNGTIEsirsVIPLAMTIEKPSLFTQPFTQASISVLIGMTGDLRGRLMIEGHETMFGSIGE-TMFGMPLEG 80
Cdd:cd16353    10 AAATTLSGRLRTGIE----PEVGSPDQVKYEEVIRDVMIPSVVVVVGITGGIEGSAILEMRKDLAYKVLDi*MGGPGEPN 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2191953106  81 EMLESFT----GELGNMIAGNLATIVFQKGITIDITPPTVLVG 119
Cdd:cd16353    86 RPLDEIElsavGEEGNNMLGLLAQALSDFGQTFDISPPNVEIG 128
CheC pfam04509
CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, ...
 82-118 1.23e-03

CheC-like family; The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low. In some cases, the region represented by this entry is present as multiple copies.


Pssm-ID: 398287 [Multi-domain]  Cd Length: 38  Bit Score: 34.75  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2191953106  82 MLESFTGELGNMIAGNLATIVFQK-GITIDITPPTVLV 118
Cdd:pfam04509   1 MELSALGEIGNILAGSAATALATLlGFKIDISPPTVVY 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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