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Conserved domains on  [gi|1170501119|emb|SLY91929|]
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colanic acid capsular biosynthesis activation accesory protein RcsA [Klebsiella variicola]

Protein Classification

helix-turn-helix transcriptional regulator( domain architecture ID 11487779)

helix-turn-helix (HTH) transcriptional regulator similar to MalT, which positively regulates the transcription of the maltose regulon, and transcriptional regulatory protein RcsA, which is involved in regulating K30 capsular polysaccharide synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rcsA PRK15411
transcriptional regulator RcsA;
1-207 5.06e-132

transcriptional regulator RcsA;


:

Pssm-ID: 185309 [Multi-domain]  Cd Length: 207  Bit Score: 369.07  E-value: 5.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119   1 MSTMIMDLCSYTRLGLTGYLTSRGIKKQEIVEVHCATDLQKHCASCCPAVVFLNEDCFVHDDESNGIIRQIITQNPATLF 80
Cdd:PRK15411    1 MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSLRPSVVFINEDCFIHDASNSQRIKQIINQHPNTLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119  81 VIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNSSLGQLNLPTLSLSKTESNMLQMWMAGHGTSQIST 160
Cdd:PRK15411   81 IVFMAIANIHFDEYLLVRKNLLISSKSIKPESLDDLLGDILKKETTITSFLNLPTLSLSRTESSMLRMWMAGQGTIQISD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1170501119 161 QMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRLTENVTSGIQVNLR 207
Cdd:PRK15411  161 QMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR 207
 
Name Accession Description Interval E-value
rcsA PRK15411
transcriptional regulator RcsA;
1-207 5.06e-132

transcriptional regulator RcsA;


Pssm-ID: 185309 [Multi-domain]  Cd Length: 207  Bit Score: 369.07  E-value: 5.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119   1 MSTMIMDLCSYTRLGLTGYLTSRGIKKQEIVEVHCATDLQKHCASCCPAVVFLNEDCFVHDDESNGIIRQIITQNPATLF 80
Cdd:PRK15411    1 MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSLRPSVVFINEDCFIHDASNSQRIKQIINQHPNTLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119  81 VIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNSSLGQLNLPTLSLSKTESNMLQMWMAGHGTSQIST 160
Cdd:PRK15411   81 IVFMAIANIHFDEYLLVRKNLLISSKSIKPESLDDLLGDILKKETTITSFLNLPTLSLSRTESSMLRMWMAGQGTIQISD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1170501119 161 QMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRLTENVTSGIQVNLR 207
Cdd:PRK15411  161 QMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR 207
GerE pfam00196
Bacterial regulatory proteins, luxR family;
137-192 1.55e-14

Bacterial regulatory proteins, luxR family;


Pssm-ID: 425517 [Multi-domain]  Cd Length: 57  Bit Score: 65.30  E-value: 1.55e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1170501119 137 SLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIV 192
Cdd:pfam00196   2 SLSPREREVLRWLAAGKSNKEIADELGISEKTVKVHRSNIMRKLNVHSRVELVRMA 57
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
 137-192 5.37e-12

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 58.69  E-value: 5.37e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1170501119  137 SLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIV 192
Cdd:smart00421   3 SLTPREREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVRLA 58
CsgD COG2771
DNA-binding transcriptional regulator, CsgD family [Transcription];
48-194 6.25e-12

DNA-binding transcriptional regulator, CsgD family [Transcription];


Pssm-ID: 442052 [Multi-domain]  Cd Length: 188  Bit Score: 61.70  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119  48 PAVVFLNEDCFVHDDESNGIIRQIITQNPATLFVIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNSS 127
Cdd:COG2771    38 LLLLAALLLLAAAAAALAAALAAALLLGLLLLLLIALLLLLLLLLALLLLLALLALLAALLARLAALLLALALAALLLAA 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170501119 128 LGQLNLPTLSLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNK-QVIYHIVRL 194
Cdd:COG2771   118 LARLLARAPGLTPREREVLRLLAEGLTLKEIARILGISERTVRTHLKRIYRKLGVSSRaELVALALRL 185
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
 138-194 1.35e-10

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 54.85  E-value: 1.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170501119 138 LSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRL 194
Cdd:cd06170     1 LTPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAIR 57
 
Name Accession Description Interval E-value
rcsA PRK15411
transcriptional regulator RcsA;
1-207 5.06e-132

transcriptional regulator RcsA;


Pssm-ID: 185309 [Multi-domain]  Cd Length: 207  Bit Score: 369.07  E-value: 5.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119   1 MSTMIMDLCSYTRLGLTGYLTSRGIKKQEIVEVHCATDLQKHCASCCPAVVFLNEDCFVHDDESNGIIRQIITQNPATLF 80
Cdd:PRK15411    1 MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSLRPSVVFINEDCFIHDASNSQRIKQIINQHPNTLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119  81 VIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNSSLGQLNLPTLSLSKTESNMLQMWMAGHGTSQIST 160
Cdd:PRK15411   81 IVFMAIANIHFDEYLLVRKNLLISSKSIKPESLDDLLGDILKKETTITSFLNLPTLSLSRTESSMLRMWMAGQGTIQISD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1170501119 161 QMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRLTENVTSGIQVNLR 207
Cdd:PRK15411  161 QMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR 207
GerE pfam00196
Bacterial regulatory proteins, luxR family;
137-192 1.55e-14

Bacterial regulatory proteins, luxR family;


Pssm-ID: 425517 [Multi-domain]  Cd Length: 57  Bit Score: 65.30  E-value: 1.55e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1170501119 137 SLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIV 192
Cdd:pfam00196   2 SLSPREREVLRWLAAGKSNKEIADELGISEKTVKVHRSNIMRKLNVHSRVELVRMA 57
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
 137-192 5.37e-12

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 58.69  E-value: 5.37e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1170501119  137 SLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIV 192
Cdd:smart00421   3 SLTPREREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVRLA 58
CsgD COG2771
DNA-binding transcriptional regulator, CsgD family [Transcription];
48-194 6.25e-12

DNA-binding transcriptional regulator, CsgD family [Transcription];


Pssm-ID: 442052 [Multi-domain]  Cd Length: 188  Bit Score: 61.70  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119  48 PAVVFLNEDCFVHDDESNGIIRQIITQNPATLFVIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNSS 127
Cdd:COG2771    38 LLLLAALLLLAAAAAALAAALAAALLLGLLLLLLIALLLLLLLLLALLLLLALLALLAALLARLAALLLALALAALLLAA 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170501119 128 LGQLNLPTLSLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNK-QVIYHIVRL 194
Cdd:COG2771   118 LARLLARAPGLTPREREVLRLLAEGLTLKEIARILGISERTVRTHLKRIYRKLGVSSRaELVALALRL 185
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
 138-194 1.35e-10

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 54.85  E-value: 1.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170501119 138 LSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRL 194
Cdd:cd06170     1 LTPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAIR 57
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 114-185 2.77e-07

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 47.58  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170501119 114 DVILVNylkyknsslgqLNLPTLS--------LSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNK 185
Cdd:COG2197    49 DVVLLD-----------IRMPGMDglealrrlLTPREREVLRLLAEGLSNKEIAERLGISERTVKTHVSNILRKLGVRNR 117
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
118-184 7.05e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 36.39  E-value: 7.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1170501119 118 VNYLKYKNSSLGQLNlpTLSLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHN 184
Cdd:PRK09935  132 LNYIKSNKCSTNSST--DTVLSNREVTILRYLVSGLSNKEIADQLLLSNKTVSAHKSNIYGKLGLHS 196
 
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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