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Conserved domains on  [gi|544734822|ref|WP_021164320|]
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MULTISPECIES: chemotaxis protein CheW [Burkholderia]

Protein Classification

CheW domain-containing protein( domain architecture ID 378)

CheW domain-containing protein similar to chemotaxis protein CheW that couples methyl-accepting chemoreceptors and histidine kinase CheA and is essential for chemotaxis

Gene Ontology:  GO:0007165|GO:0006935
PubMed:  12011495|10049806

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheW_like super family cl00256
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
19-169 1.29e-79

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


The actual alignment was detected with superfamily member PRK10612:

Pssm-ID: 469692  Cd Length: 167  Bit Score: 233.55  E-value: 1.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  19 GDATGQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIIL 98
Cdd:PRK10612  12 GEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVL 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544734822  99 NVAHRVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSREMALIETL 169
Cdd:PRK10612  92 NLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGERMLILVNIEKLLNSEEMALLDSA 162
 
Name Accession Description Interval E-value
PRK10612 PRK10612
chemotaxis protein CheW;
19-169 1.29e-79

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 233.55  E-value: 1.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  19 GDATGQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIIL 98
Cdd:PRK10612  12 GEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVL 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544734822  99 NVAHRVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSREMALIETL 169
Cdd:PRK10612  92 NLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGERMLILVNIEKLLNSEEMALLDSA 162
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
18-167 3.54e-54

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 168.51  E-value: 3.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  18 QGDATGQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVII 97
Cdd:COG0835    2 EAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTERTRIIV 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  98 LNVAHRVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSREMALIE 167
Cdd:COG0835   82 LEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGVAKLDDRLILLLDLEKLLAEEELAALA 151
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
23-162 2.11e-52

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 163.51  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  23 GQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNVAH 102
Cdd:cd00732    1 ELEVVTFRLGDEEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLGLPPAEDTKNTRIIVVEVGD 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822 103 RVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSRE 162
Cdd:cd00732   81 QVVGLLVDSVSEVLRLSTDDIQPPPPVLSDINAKFIRGVVKLEGRLLILLDLDKILDERE 140
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
26-157 2.28e-40

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 132.71  E-value: 2.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822   26 FLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNVAHRVV 105
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERTRVVVVEVGGQVV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 544734822  106 GMVVDGVSDVLTLQTDQIMPApeFGATLTTEYLTGLGTV-DGRMLILMDIEKL 157
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQIEPP--LGLGRVAGYISGATILgDGRVVLILDVEAL 131
CheW smart00260
Two component signalling adaptor domain;
22-158 3.36e-35

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 119.65  E-value: 3.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822    22 TGQEFLVFTLG-DEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNV 100
Cdd:smart00260   1 TIRLPLTFAIGkDETYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDETRVIVVET 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 544734822   101 AHRVVGMVVDGVSDVLTLQTDQIMPAPEFGaTLTTEYLTGLGTV-DGRMLILMDIEKLM 158
Cdd:smart00260  81 GDRKVGLVVDSVLGVREVVVKSIEPPPPVS-LSNAPGISGATILgDGRVVLILDVDKLL 138
 
Name Accession Description Interval E-value
PRK10612 PRK10612
chemotaxis protein CheW;
19-169 1.29e-79

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 233.55  E-value: 1.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  19 GDATGQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIIL 98
Cdd:PRK10612  12 GEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVL 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544734822  99 NVAHRVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSREMALIETL 169
Cdd:PRK10612  92 NLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGERMLILVNIEKLLNSEEMALLDSA 162
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
18-167 3.54e-54

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 168.51  E-value: 3.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  18 QGDATGQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVII 97
Cdd:COG0835    2 EAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTERTRIIV 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  98 LNVAHRVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSREMALIE 167
Cdd:COG0835   82 LEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGVAKLDDRLILLLDLEKLLAEEELAALA 151
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
23-162 2.11e-52

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 163.51  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  23 GQEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNVAH 102
Cdd:cd00732    1 ELEVVTFRLGDEEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLGLPPAEDTKNTRIIVVEVGD 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822 103 RVVGMVVDGVSDVLTLQTDQIMPAPEFGATLTTEYLTGLGTVDGRMLILMDIEKLMSSRE 162
Cdd:cd00732   81 QVVGLLVDSVSEVLRLSTDDIQPPPPVLSDINAKFIRGVVKLEGRLLILLDLDKILDERE 140
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
26-157 2.28e-40

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 132.71  E-value: 2.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822   26 FLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNVAHRVV 105
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERTRVVVVEVGGQVV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 544734822  106 GMVVDGVSDVLTLQTDQIMPApeFGATLTTEYLTGLGTV-DGRMLILMDIEKL 157
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQIEPP--LGLGRVAGYISGATILgDGRVVLILDVEAL 131
CheW smart00260
Two component signalling adaptor domain;
22-158 3.36e-35

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 119.65  E-value: 3.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822    22 TGQEFLVFTLG-DEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYDHQTVVIILNV 100
Cdd:smart00260   1 TIRLPLTFAIGkDETYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDETRVIVVET 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 544734822   101 AHRVVGMVVDGVSDVLTLQTDQIMPAPEFGaTLTTEYLTGLGTV-DGRMLILMDIEKLM 158
Cdd:smart00260  81 GDRKVGLVVDSVLGVREVVVKSIEPPPPVS-LSNAPGISGATILgDGRVVLILDVDKLL 138
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
24-157 2.98e-33

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 114.68  E-value: 2.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  24 QEFLVFTLGDEEYGIDILKVQEIRGYDSVTRIANAPDFIKGVINLRGIIVPIVDMRIKFHLGRVEYD-HQTVVIILNVAH 102
Cdd:cd00588    2 LQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDtDETRIVVVEVGD 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544734822 103 RVVGMVVDGVSDVLTLQTDQIMPAPEFGATLtTEYLTGLGTV-DGRMLILMDIEKL 157
Cdd:cd00588   82 RKVGLVVDSVLGVLEVVIKDIEPPPDVGSSN-APGISGATILgDGRVVLILDVDKL 136
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
27-112 4.08e-06

CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 44.09  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  27 LVFTLGDEEYGIDILKVQEIRGYDS--VTRIANApdfiKGVINLRGIIVPIVDMRIKFHLGRVEYD-HQTVVIILNVAHR 103
Cdd:cd00731    7 LLVRVGDETYAIPLSAVVETVRIKPkdIKRVDGG----KEVINVRGELLPLVRLGELFNVRGENEEpDEGVVVVVRTGGR 82

                 ....*....
gi 544734822 104 VVGMVVDGV 112
Cdd:cd00731   83 KAALVVDQI 91
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
27-160 1.08e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544734822  27 LVFTLGDEEYGIDILKVQEIRGYDS--VTRIANAPdfikgVINLRGIIVPIVDMRIKFHLGRVEYDHQTV-VIILNVAHR 103
Cdd:COG0643  426 LLVRVGGETYAIPLSSVEEVLRLDPddIETVEGRE-----VIRLRGELLPLVRLGELLGLPGAEPEGERGpVVVVRSGGR 500
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544734822 104 VVGMVVDGVSD----VLTLQTDQIMPAPEF-GATLtteyltgLGtvDGR-MLILmDIEKLMSS 160
Cdd:COG0643  501 RVALVVDELLGqqevVIKPLGPLLRRVPGIsGATI-------LG--DGRvALIL-DVAALVRS 553
 
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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