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Conserved domains on  [gi|1024856779|ref|WP_063510971|]
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MULTISPECIES: TetR/AcrR family transcriptional regulator [Erythrobacteraceae]

Protein Classification

TetR/AcrR family transcriptional regulator( domain architecture ID 14302094)

TetR/AcrR family transcriptional regulator controls genes involved in a variety of processes including antibiotic production, osmotic stress response, efflux pump expression, and multidrug resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 104-209 2.18e-28

Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in family members such as HTH-type transcriptional repressor KstR2 as well as fatty acid metabolism regulator proteins. In Mycobacterium smegmatis, KstR2 is involved in involved in cholesterol catabolism, while YsiA in Bacillus subtilis is involved in fatty acid degradation.


:

Pssm-ID: 465574  Cd Length: 114  Bit Score: 103.02  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779 104 LAEVVRQVGRIVIDRQEYVVVYQREMKHLSAKDHERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWIGGLISWI 183
Cdd:pfam17932   8 LRALVRAHVRVHAERRDEAAVFLRELRSLSPEHRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPKLAALAILGMLNWV 87

                          90       100
                  ....*....|....*....|....*.
gi 1024856779 184 PTWYSPQGQKSAADVIDQLVDAAMRL 209
Cdd:pfam17932  88 YRWYRPDGPLSPEEIADQYADLLLRG 113
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
30-176 2.14e-16

DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];


:

Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 73.01  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  30 RIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICEVGISESLSVLERTLAGEhaDHRALLAEVVR 109
Cdd:COG1309    10 RILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALAAE--DPRERLRALLR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024856779 110 QVGRIVIDRQEYVVVYQREMKHLsakdhERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWI 176
Cdd:COG1309    88 AYLEFLAENPALARLLLAEAAEL-----PELRAALRALLRRLRALLAELLRAGGLLADVDPDALARA 149
 
Name Accession Description Interval E-value
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 104-209 2.18e-28

Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in family members such as HTH-type transcriptional repressor KstR2 as well as fatty acid metabolism regulator proteins. In Mycobacterium smegmatis, KstR2 is involved in involved in cholesterol catabolism, while YsiA in Bacillus subtilis is involved in fatty acid degradation.


Pssm-ID: 465574  Cd Length: 114  Bit Score: 103.02  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779 104 LAEVVRQVGRIVIDRQEYVVVYQREMKHLSAKDHERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWIGGLISWI 183
Cdd:pfam17932   8 LRALVRAHVRVHAERRDEAAVFLRELRSLSPEHRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPKLAALAILGMLNWV 87

                          90       100
                  ....*....|....*....|....*.
gi 1024856779 184 PTWYSPQGQKSAADVIDQLVDAAMRL 209
Cdd:pfam17932  88 YRWYRPDGPLSPEEIADQYADLLLRG 113
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
30-176 2.14e-16

DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 73.01  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  30 RIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICEVGISESLSVLERTLAGEhaDHRALLAEVVR 109
Cdd:COG1309    10 RILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALAAE--DPRERLRALLR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024856779 110 QVGRIVIDRQEYVVVYQREMKHLsakdhERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWI 176
Cdd:COG1309    88 AYLEFLAENPALARLLLAEAAEL-----PELRAALRALLRRLRALLAELLRAGGLLADVDPDALARA 149
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
31-77 5.98e-11

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 55.49  E-value: 5.98e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1024856779  31 IVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAI 77
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
29-185 1.30e-10

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 58.37  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  29 NRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAIcevgISESLSVLERTLAGEHADHRALLAEVV 108
Cdd:NF041196    9 RAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAV----LEEQVARLREAVEPQRAGGGSKLQELV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779 109 RQVGRIVIDRQEYVVVyqREMKHLSAKDHERILRLRHSF---DHQIAELIREGVEAGEFREDTD------SFVAVWIG-G 178
Cdd:NF041196   85 DLTHVLARRLRTDPVV--RAGVRLSIEQAAIGAGLPTPYrewIDLVAELLAEARAAGELLPGVDpeeaarLLVGAFTGvQ 162


                  ....*..
gi 1024856779 179 LISWIPT 185
Cdd:NF041196  163 MLSDVLS 169
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 29-204 2.44e-06

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 46.54  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  29 NRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICEvgISES-----------------LSVLER 91
Cdd:PRK10668   14 QHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFSEIWE--LSESkigeleleyqakfpddpLSVLRE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  92 TL-----AGEHADHRALLAEvvrqvgrIVIDRQEYV---VVYQREMKHLSAKDHERilrlrhsfdhqIAELIREGVEAGE 163
Cdd:PRK10668   92 ILiyileATVTDERRRLLME-------IIFHKCEFVgemAVVQQAQRNLCLESYDR-----------IEQTLKHCIEAKQ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024856779 164 FREDTDSF-VAVWIGGLISWI-PTW-YSPQG---QKSAADVIDQLVD 204
Cdd:PRK10668  154 LPANLMTRrAAIIMRGYISGLmENWlFAPESfdlKKEARDLVDILLE 200
PRK15008 PRK15008
HTH-type transcriptional regulator RutR; Provisional
 12-77 9.41e-04

HTH-type transcriptional regulator RutR; Provisional


Pssm-ID: 184970 [Multi-domain]  Cd Length: 212  Bit Score: 38.76  E-value: 9.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024856779  12 GKASKPSIKNEFTAFKTNRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAI 77
Cdd:PRK15008    4 GAVKTTGKRSRAVSAKKKAILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALYIAV 69
 
Name Accession Description Interval E-value
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 104-209 2.18e-28

Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in family members such as HTH-type transcriptional repressor KstR2 as well as fatty acid metabolism regulator proteins. In Mycobacterium smegmatis, KstR2 is involved in involved in cholesterol catabolism, while YsiA in Bacillus subtilis is involved in fatty acid degradation.


Pssm-ID: 465574  Cd Length: 114  Bit Score: 103.02  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779 104 LAEVVRQVGRIVIDRQEYVVVYQREMKHLSAKDHERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWIGGLISWI 183
Cdd:pfam17932   8 LRALVRAHVRVHAERRDEAAVFLRELRSLSPEHRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPKLAALAILGMLNWV 87

                          90       100
                  ....*....|....*....|....*.
gi 1024856779 184 PTWYSPQGQKSAADVIDQLVDAAMRL 209
Cdd:pfam17932  88 YRWYRPDGPLSPEEIADQYADLLLRG 113
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
30-176 2.14e-16

DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 73.01  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  30 RIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICEVGISESLSVLERTLAGEhaDHRALLAEVVR 109
Cdd:COG1309    10 RILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALAAE--DPRERLRALLR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024856779 110 QVGRIVIDRQEYVVVYQREMKHLsakdhERILRLRHSFDHQIAELIREGVEAGEFREDTDSFVAVWI 176
Cdd:COG1309    88 AYLEFLAENPALARLLLAEAAEL-----PELRAALRALLRRLRALLAELLRAGGLLADVDPDALARA 149
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
31-77 5.98e-11

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 55.49  E-value: 5.98e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1024856779  31 IVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAI 77
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
29-185 1.30e-10

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 58.37  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  29 NRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAIcevgISESLSVLERTLAGEHADHRALLAEVV 108
Cdd:NF041196    9 RAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAV----LEEQVARLREAVEPQRAGGGSKLQELV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779 109 RQVGRIVIDRQEYVVVyqREMKHLSAKDHERILRLRHSF---DHQIAELIREGVEAGEFREDTD------SFVAVWIG-G 178
Cdd:NF041196   85 DLTHVLARRLRTDPVV--RAGVRLSIEQAAIGAGLPTPYrewIDLVAELLAEARAAGELLPGVDpeeaarLLVGAFTGvQ 162


                  ....*..
gi 1024856779 179 LISWIPT 185
Cdd:NF041196  163 MLSDVLS 169
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 29-204 2.44e-06

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 46.54  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  29 NRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICEvgISES-----------------LSVLER 91
Cdd:PRK10668   14 QHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFSEIWE--LSESkigeleleyqakfpddpLSVLRE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024856779  92 TL-----AGEHADHRALLAEvvrqvgrIVIDRQEYV---VVYQREMKHLSAKDHERilrlrhsfdhqIAELIREGVEAGE 163
Cdd:PRK10668   92 ILiyileATVTDERRRLLME-------IIFHKCEFVgemAVVQQAQRNLCLESYDR-----------IEQTLKHCIEAKQ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024856779 164 FREDTDSF-VAVWIGGLISWI-PTW-YSPQG---QKSAADVIDQLVD 204
Cdd:PRK10668  154 LPANLMTRrAAIIMRGYISGLmENWlFAPESfdlKKEARDLVDILLE 200
PRK15008 PRK15008
HTH-type transcriptional regulator RutR; Provisional
 12-77 9.41e-04

HTH-type transcriptional regulator RutR; Provisional


Pssm-ID: 184970 [Multi-domain]  Cd Length: 212  Bit Score: 38.76  E-value: 9.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024856779  12 GKASKPSIKNEFTAFKTNRIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAI 77
Cdd:PRK15008    4 GAVKTTGKRSRAVSAKKKAILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALYIAV 69
PRK13756 PRK13756
TetR family transcriptional regulator;
30-79 5.81e-03

TetR family transcriptional regulator;


Pssm-ID: 172294 [Multi-domain]  Cd Length: 205  Bit Score: 36.41  E-value: 5.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024856779  30 RIVEVASHLFYERGYSSCTLDHVAERLGVTKPFLYSYFKNKEAILAAICE 79
Cdd:PRK13756    8 KVIDSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAI 57
TetR_C_27 pfam17935
Tetracyclin repressor-like, C-terminal domain; This is the C-terminal domain present in ...
 148-167 8.11e-03

Tetracyclin repressor-like, C-terminal domain; This is the C-terminal domain present in putative TetR transcriptional regulators.


Pssm-ID: 436155  Cd Length: 106  Bit Score: 34.83  E-value: 8.11e-03
                          10        20
                  ....*....|....*....|
gi 1024856779 148 DHQIAELIREGVEAGEFRED 167
Cdd:pfam17935  49 DGQLAEIIREGVADGEFTAA 68
 
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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