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Conserved domains on  [gi|489904765|ref|WP_003808193|]
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MULTISPECIES: TetR/AcrR family transcriptional regulator [Bordetella]

Protein Classification

TetR/AcrR family transcriptional regulator( domain architecture ID 15841257)

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

CATH:  1.10.10.60|1.10.357.10
Gene Ontology:  GO:0003677|GO:0006355
SCOP:  4000333|3000001|3000086

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 ...
 85-207 2.02e-19

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: 80.30  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765   85 GGGAVGRLAAMALRHTQILLKEMPMQKVAVQGLeRHLLEAssaakRLRAVVKMRDDYEQMFVEVIDDGIREGSFVDLPPR 164
Cdd:pfam17932   1 GGSPVERLRALVRAHVRVHAERRDEAAVFLREL-RSLSPE-----HRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489904765  165 LLSKPFFGALNWATVWYSQRrlqSEEAIDDIAHALAAYALRGL 207
Cdd:pfam17932  75 LAALAILGMLNWVYRWYRPD---GPLSPEEIADQYADLLLRGL 114
ScbR_bind_reg super family cl49260
ScbR family autoregulator-binding transcription factor;
17-103 7.48e-13

ScbR family autoregulator-binding transcription factor;


The actual alignment was detected with superfamily member NF041196:

Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 64.54  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLAREGGGAVGRLAAMA 96
Cdd:NF041196   8 RRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLEEQVARLREAVEPQRAGGGSKLQELVDLT 87


                 ....*..
gi 489904765  97 LRHTQIL 103
Cdd:NF041196  88 HVLARRL 94
 
Name Accession Description Interval E-value
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 85-207 2.02e-19

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: 80.30  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765   85 GGGAVGRLAAMALRHTQILLKEMPMQKVAVQGLeRHLLEAssaakRLRAVVKMRDDYEQMFVEVIDDGIREGSFVDLPPR 164
Cdd:pfam17932   1 GGSPVERLRALVRAHVRVHAERRDEAAVFLREL-RSLSPE-----HRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489904765  165 LLSKPFFGALNWATVWYSQRrlqSEEAIDDIAHALAAYALRGL 207
Cdd:pfam17932  75 LAALAILGMLNWVYRWYRPD---GPLSPEEIADQYADLLLRGL 114
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
10-175 1.03e-14

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 68.77  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  10 DANGGESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPlAREGGGAV 89
Cdd:COG1309    1 RRRREATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEE-ALAAEDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  90 GRLAAMALRHTQILLKEmpmqkvavQGLERHLLEASSAAKRLRAVvkMRDDYEQMFVEVIDDGIREGSFVDLPPRLLSKP 169
Cdd:COG1309   80 ERLRALLRAYLEFLAEN--------PALARLLLAEAAELPELRAA--LRALLRRLRALLAELLRAGGLLADVDPDALARA 149


                 ....*.
gi 489904765 170 FFGALN 175
Cdd:COG1309  150 LLALLD 155
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
17-103 7.48e-13

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 64.54  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLAREGGGAVGRLAAMA 96
Cdd:NF041196   8 RRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLEEQVARLREAVEPQRAGGGSKLQELVDLT 87


                 ....*..
gi 489904765  97 LRHTQIL 103
Cdd:NF041196  88 HVLARRL 94
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
20-66 3.57e-11

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 56.26  E-value: 3.57e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489904765   20 ILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDV 66
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 15-63 2.91e-08

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 52.32  E-value: 2.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489904765  15 ESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLF 63
Cdd:PRK10668  11 ETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLF 59
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
17-96 6.07e-04

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 39.54  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLAREGGGAVGRLAAMA 96
Cdd:COG3226   10 RERILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRDELLAAAFERLAEREAARLRALLAAADDLEDAAEALA 89
 
Name Accession Description Interval E-value
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 85-207 2.02e-19

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: 80.30  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765   85 GGGAVGRLAAMALRHTQILLKEMPMQKVAVQGLeRHLLEAssaakRLRAVVKMRDDYEQMFVEVIDDGIREGSFVDLPPR 164
Cdd:pfam17932   1 GGSPVERLRALVRAHVRVHAERRDEAAVFLREL-RSLSPE-----HRAEIRALRREYERLLRDLIEEGVAAGEFRDLDPK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489904765  165 LLSKPFFGALNWATVWYSQRrlqSEEAIDDIAHALAAYALRGL 207
Cdd:pfam17932  75 LAALAILGMLNWVYRWYRPD---GPLSPEEIADQYADLLLRGL 114
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
10-175 1.03e-14

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 68.77  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  10 DANGGESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPlAREGGGAV 89
Cdd:COG1309    1 RRRREATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEE-ALAAEDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  90 GRLAAMALRHTQILLKEmpmqkvavQGLERHLLEASSAAKRLRAVvkMRDDYEQMFVEVIDDGIREGSFVDLPPRLLSKP 169
Cdd:COG1309   80 ERLRALLRAYLEFLAEN--------PALARLLLAEAAELPELRAA--LRALLRRLRALLAELLRAGGLLADVDPDALARA 149


                 ....*.
gi 489904765 170 FFGALN 175
Cdd:COG1309  150 LLALLD 155
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
17-103 7.48e-13

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 64.54  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLAREGGGAVGRLAAMA 96
Cdd:NF041196   8 RRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLEEQVARLREAVEPQRAGGGSKLQELVDLT 87


                 ....*..
gi 489904765  97 LRHTQIL 103
Cdd:NF041196  88 HVLARRL 94
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
20-66 3.57e-11

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 56.26  E-value: 3.57e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489904765   20 ILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDV 66
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 15-63 2.91e-08

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 52.32  E-value: 2.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489904765  15 ESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLF 63
Cdd:PRK10668  11 ETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLF 59
PRK09975 PRK09975
DNA-binding transcriptional regulator EnvR; Provisional
 4-63 1.15e-04

DNA-binding transcriptional regulator EnvR; Provisional


Pssm-ID: 182177 [Multi-domain]  Cd Length: 213  Bit Score: 41.65  E-value: 1.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765   4 AHQTPADANggESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLF 63
Cdd:PRK09975   2 AKKTKAEAL--KTRQELIETAIAQFALRGVSNTTLNDIADAANVTRGAIYWHFENKTQLF 59
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
17-96 6.07e-04

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 39.54  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLAREGGGAVGRLAAMA 96
Cdd:COG3226   10 RERILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRDELLAAAFERLAEREAARLRALLAAADDLEDAAEALA 89
PRK11552 PRK11552
putative DNA-binding transcriptional regulator; Provisional
 6-84 1.37e-03

putative DNA-binding transcriptional regulator; Provisional


Pssm-ID: 236928 [Multi-domain]  Cd Length: 225  Bit Score: 38.49  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489904765   6 QTPADANGGESRDEILRAAAELFMEFGYAATSIDaVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTAQVEPLARE 84
Cdd:PRK11552   4 NPAMTTRGEQAKQQLIAAALAQFGEYGLHATTRD-IAAQAGQNIAAITYYFGSKEDLYLAVAQWIADFIGEQFRPHAEE 81
PRK15008 PRK15008
HTH-type transcriptional regulator RutR; Provisional
 17-82 3.65e-03

HTH-type transcriptional regulator RutR; Provisional


Pssm-ID: 184970 [Multi-domain]  Cd Length: 212  Bit Score: 37.22  E-value: 3.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489904765  17 RDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLF-------FDVQVTAMNRLTAQVEPLA 82
Cdd:PRK15008  20 KKAILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALYiavlrqiLDIWLAPLKAFREDFAPLA 92
PRK14996 PRK14996
TetR family transcriptional regulator; Provisional
 15-76 6.59e-03

TetR family transcriptional regulator; Provisional


Pssm-ID: 184958 [Multi-domain]  Cd Length: 192  Bit Score: 36.22  E-value: 6.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489904765  15 ESRDEILRAAAELFMEFGYAATSIDAVAQRLGSTKGRIYHHYRSKADLFFDVQVTAMNRLTA 76
Cdd:PRK14996   8 ERREVILQAAMRVALAEGFAAMTVRRIASEAQVAAGQVHHHFSSAGELKALAFIHLIRQLLD 69
 
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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