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Conserved domains on  [gi|857324850|gb|KMN92782|]
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TetR family transcriptional regulator [Bacillus subtilis]

Protein Classification

TetR/AcrR family transcriptional regulator( domain architecture ID 14302086)

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_17 pfam17922
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 87-186 1.10e-42

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. This entry represents the C-terminal domain present in Yfir transcription regulator proteins found in Bacillus subtilus. 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.


:

Pssm-ID: 436144  Cd Length: 100  Bit Score: 138.95  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   87 AISIYLDELTEGLRDVADTLAPVQFEYLVTAWRNEERRQYLEKRYDLFVERFSKLLQKGIDQGEFQPLQPLATIAKFFLN 166
Cdd:pfam17922   1 QIESWLDSQEEEIEEIDDSLLPVAYEYFVTSWREKERRAYLQNRYERAVKVFKAFLQKGVDRGEFKPVLPLESIARFFIS 80

                          90       100
                  ....*....|....*....|
gi 857324850  167 MNDGIIQNALYFDEEKADVS 186
Cdd:pfam17922  81 FIDGLILNALVLGPETVKVS 100
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
17-63 2.62e-12

Bacterial regulatory proteins, tetR family;


:

Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 58.96  E-value: 2.62e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 857324850   17 ILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRI 63
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
 
Name Accession Description Interval E-value
TetR_C_17 pfam17922
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 87-186 1.10e-42

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. This entry represents the C-terminal domain present in Yfir transcription regulator proteins found in Bacillus subtilus. 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.


Pssm-ID: 436144  Cd Length: 100  Bit Score: 138.95  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   87 AISIYLDELTEGLRDVADTLAPVQFEYLVTAWRNEERRQYLEKRYDLFVERFSKLLQKGIDQGEFQPLQPLATIAKFFLN 166
Cdd:pfam17922   1 QIESWLDSQEEEIEEIDDSLLPVAYEYFVTSWREKERRAYLQNRYERAVKVFKAFLQKGVDRGEFKPVLPLESIARFFIS 80

                          90       100
                  ....*....|....*....|
gi 857324850  167 MNDGIIQNALYFDEEKADVS 186
Cdd:pfam17922  81 FIDGLILNALVLGPETVKVS 100
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
7-170 1.80e-19

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 81.10  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   7 KEHKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIETGLDEGLRKLDKSAEHQSVWS 86
Cdd:COG1309    1 RRRREATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALAAEDPRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  87 AISIYLDELTEGLRDVADTLAPVqfeyLVTAWRNEERRQYLEKRYDLFVERFSKLLQkgidQGEFQPLQPLATIAKFFLN 166
Cdd:COG1309   81 RLRALLRAYLEFLAENPALARLL----LAEAAELPELRAALRALLRRLRALLAELLR----AGGLLADVDPDALARALLA 152


                 ....
gi 857324850 167 MNDG 170
Cdd:COG1309  153 LLDG 156
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
17-63 2.62e-12

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 58.96  E-value: 2.62e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 857324850   17 ILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRI 63
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
13-65 1.19e-08

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 52.60  E-value: 1.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 857324850  13 RQAkILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIE 65
Cdd:NF041196   8 RRA-ILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLE 59
PRK14996 PRK14996
TetR family transcriptional regulator; Provisional
 9-161 9.03e-06

TetR family transcriptional regulator; Provisional


Pssm-ID: 184958 [Multi-domain]  Cd Length: 192  Bit Score: 44.31  E-value: 9.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   9 HKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEM----FRRIIETGLDeglrkLDKSAEHQSV 84
Cdd:PRK14996   5 NRDERREVILQAAMRVALAEGFAAMTVRRIASEAQVAAGQVHHHFSSAGELkalaFIHLIRQLLD-----AEQVPQTASW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  85 WSAISIYLDELTEGlrdvadtlapvqFEYLVTAWRNE----ERRQYLEKRYDLFVERFSK----LLQKGIDQGEFQPLQP 156
Cdd:PRK14996  80 RERLHAMLGSEDGR------------FEPYIRLWREAqilaDRDPEIKDAYLLTMQMWHQetvaIIEQGKAAGEFRSTSN 147


                 ....*
gi 857324850 157 LATIA 161
Cdd:PRK14996 148 ATDIA 152
PRK09975 PRK09975
DNA-binding transcriptional regulator EnvR; Provisional
 4-63 5.30e-05

DNA-binding transcriptional regulator EnvR; Provisional


Pssm-ID: 182177 [Multi-domain]  Cd Length: 213  Bit Score: 42.42  E-value: 5.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   4 KVTKEHKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRI 63
Cdd:PRK09975   3 KKTKAEALKTRQELIETAIAQFALRGVSNTTLNDIADAANVTRGAIYWHFENKTQLFNEM 62
 
Name Accession Description Interval E-value
TetR_C_17 pfam17922
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 87-186 1.10e-42

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. This entry represents the C-terminal domain present in Yfir transcription regulator proteins found in Bacillus subtilus. 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.


Pssm-ID: 436144  Cd Length: 100  Bit Score: 138.95  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   87 AISIYLDELTEGLRDVADTLAPVQFEYLVTAWRNEERRQYLEKRYDLFVERFSKLLQKGIDQGEFQPLQPLATIAKFFLN 166
Cdd:pfam17922   1 QIESWLDSQEEEIEEIDDSLLPVAYEYFVTSWREKERRAYLQNRYERAVKVFKAFLQKGVDRGEFKPVLPLESIARFFIS 80

                          90       100
                  ....*....|....*....|
gi 857324850  167 MNDGIIQNALYFDEEKADVS 186
Cdd:pfam17922  81 FIDGLILNALVLGPETVKVS 100
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
7-170 1.80e-19

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 81.10  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   7 KEHKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIETGLDEGLRKLDKSAEHQSVWS 86
Cdd:COG1309    1 RRRREATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALAAEDPRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  87 AISIYLDELTEGLRDVADTLAPVqfeyLVTAWRNEERRQYLEKRYDLFVERFSKLLQkgidQGEFQPLQPLATIAKFFLN 166
Cdd:COG1309   81 RLRALLRAYLEFLAENPALARLL----LAEAAELPELRAALRALLRRLRALLAELLR----AGGLLADVDPDALARALLA 152


                 ....
gi 857324850 167 MNDG 170
Cdd:COG1309  153 LLDG 156
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
17-63 2.62e-12

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 58.96  E-value: 2.62e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 857324850   17 ILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRI 63
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLEAL 47
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
13-65 1.19e-08

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 52.60  E-value: 1.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 857324850  13 RQAkILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIE 65
Cdd:NF041196   8 RRA-ILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEALARAVLE 59
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
11-176 8.54e-08

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 50.32  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  11 DKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEM----FRRIIETGLDEGLRKLDKSAEHQSVWS 86
Cdd:COG3226    7 EERRERILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRDELlaaaFERLAEREAARLRALLAAADDLEDAAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  87 AISIYLDELTEGLRDvaDTLApvQFEYLVTAWRNEERRQYLEKRYDLFVERFSKLLQKGidqGEFQPlqplATIAKFFLN 166
Cdd:COG3226   87 ALADLLAELLPADRD--RLLA--RYELYLEALRDPELRALLRRWRDRLREALARLLAAL---GSPDP----PETARALVA 155

                        170
                 ....*....|
gi 857324850 167 MNDGIIQNAL 176
Cdd:COG3226  156 LIDGLTLHAL 165
PRK14996 PRK14996
TetR family transcriptional regulator; Provisional
 9-161 9.03e-06

TetR family transcriptional regulator; Provisional


Pssm-ID: 184958 [Multi-domain]  Cd Length: 192  Bit Score: 44.31  E-value: 9.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   9 HKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEM----FRRIIETGLDeglrkLDKSAEHQSV 84
Cdd:PRK14996   5 NRDERREVILQAAMRVALAEGFAAMTVRRIASEAQVAAGQVHHHFSSAGELkalaFIHLIRQLLD-----AEQVPQTASW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  85 WSAISIYLDELTEGlrdvadtlapvqFEYLVTAWRNE----ERRQYLEKRYDLFVERFSK----LLQKGIDQGEFQPLQP 156
Cdd:PRK14996  80 RERLHAMLGSEDGR------------FEPYIRLWREAqilaDRDPEIKDAYLLTMQMWHQetvaIIEQGKAAGEFRSTSN 147


                 ....*
gi 857324850 157 LATIA 161
Cdd:PRK14996 148 ATDIA 152
PRK09975 PRK09975
DNA-binding transcriptional regulator EnvR; Provisional
 4-63 5.30e-05

DNA-binding transcriptional regulator EnvR; Provisional


Pssm-ID: 182177 [Multi-domain]  Cd Length: 213  Bit Score: 42.42  E-value: 5.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850   4 KVTKEHKDKRQAKILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRI 63
Cdd:PRK09975   3 KKTKAEALKTRQELIETAIAQFALRGVSNTTLNDIADAANVTRGAIYWHFENKTQLFNEM 62
PRK15008 PRK15008
HTH-type transcriptional regulator RutR; Provisional
 12-101 3.69e-04

HTH-type transcriptional regulator RutR; Provisional


Pssm-ID: 184970 [Multi-domain]  Cd Length: 212  Bit Score: 39.91  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  12 KRQAkILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIETGLDEGLRKLDKSAEHQSVWSAISIY 91
Cdd:PRK15008  19 KKKA-ILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALYIAVLRQILDIWLAPLKAFREDFAPLAAIKEY 97

                         90
                 ....*....|
gi 857324850  92 LDELTEGLRD 101
Cdd:PRK15008  98 IRLKLEVSRD 107
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 10-96 4.77e-03

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 36.52  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857324850  10 KDKRQA-----KILEAAKTVFKRKGFELTTMKDVVEESGFSRGGVYLYFSSTEEMFRRIIETGlDEGLRKLDKsaEHQ-- 82
Cdd:PRK10668   4 KTKQQAqetrqHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFSEIWELS-ESKIGELEL--EYQak 80

                         90       100
                 ....*....|....*....|
gi 857324850  83 ------SVWSAISIYLDELT 96
Cdd:PRK10668  81 fpddplSVLREILIYILEAT 100
 
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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