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Conserved domains on  [gi|2045876398|ref|WP_214057467|]
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TetR/AcrR family transcriptional regulator [Nocardioides aquaticus]

Protein Classification

TetR/AcrR family transcriptional regulator( domain architecture ID 11442015)

TetR/AcrR family transcriptional regulator may control genes involved in one of 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:0003700|GO:0003677|GO:0006355
PubMed:  23602932
SCOP:  4000333

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
32-191 2.60e-21

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


:

Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 86.49  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQIRDsSASATVKLR 111
Cdd:COG1309     5 EATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALA-AEDPRERLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 112 KLVVQLMCSYAEHYPFLYVYLQENMAhvdpkrkawAAEMRRVNRRYEAAVTDIIGQGIDEGSIRAVGEPWVLAYGLMGMV 191
Cdd:COG1309    84 ALLRAYLEFLAENPALARLLLAEAAE---------LPELRAALRALLRRLRALLAELLRAGGLLADVDPDALARALLALL 154
 
Name Accession Description Interval E-value
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
32-191 2.60e-21

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 86.49  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQIRDsSASATVKLR 111
Cdd:COG1309     5 EATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALA-AEDPRERLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 112 KLVVQLMCSYAEHYPFLYVYLQENMAhvdpkrkawAAEMRRVNRRYEAAVTDIIGQGIDEGSIRAVGEPWVLAYGLMGMV 191
Cdd:COG1309    84 ALLRAYLEFLAENPALARLLLAEAAE---------LPELRAALRALLRRLRALLAELLRAGGLLADVDPDALARALLALL 154
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 103-222 3.39e-20

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: 82.22  E-value: 3.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 103 SASATVKLRKLVVQLMCSYAEHYPFLYVYLQEnMAHVDPKRKAWAAEMRRvnrRYEAAVTDIIGQGIDEGSIRAVgEPWV 182
Cdd:pfam17932   1 GGSPVERLRALVRAHVRVHAERRDEAAVFLRE-LRSLSPEHRAEIRALRR---EYERLLRDLIEEGVAAGEFRDL-DPKL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2045876398 183 LAYGLMGMVSWTHRWFNPNtAEVDAKTIGESYADVLLSGL 222
Cdd:pfam17932  76 AALAILGMLNWVYRWYRPD-GPLSPEEIADQYADLLLRGL 114
septum_RefZ NF037937
forespore capture DNA-binding protein RefZ; RefZ (regulator of FtsZ), a DNA-binding protein in ...
 38-125 2.21e-11

forespore capture DNA-binding protein RefZ; RefZ (regulator of FtsZ), a DNA-binding protein in the family of TetR/AcrR family transcriptional regulators, participates in septum placement and in chromosome capture during the asymmetrical cell division in endospore formation. The five nearly palindromic DNA motifs (RBMs) to which RefZ binds affect chromosomal localization, not transcription, so RefZ is not considered a transcription factor.


Pssm-ID: 468281 [Multi-domain]  Cd Length: 195  Bit Score: 61.00  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  38 ILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQ--IRDSSASATVKLRKLVV 115
Cdd:NF037937    4 ILDAAISLFNTKGFDGTSVRDIAKKAKVNVALISYYFKGKQGLLEYLVTSFFEGYLEILEEgfEELKNLSAKECLKQLVR 83

                          90
                  ....*....|
gi 2045876398 116 QLMCSYAEHY 125
Cdd:NF037937   84 NILHYQQEHH 93
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
35-80 7.19e-09

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 53.75  E-value: 7.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2045876398  35 RAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEV 80
Cdd:NF041196    8 RRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEAL 53
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 32-82 3.95e-05

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 43.07  E-value: 3.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFD 82
Cdd:PRK10668   10 QETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFS 60
 
Name Accession Description Interval E-value
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
32-191 2.60e-21

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 86.49  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQIRDsSASATVKLR 111
Cdd:COG1309     5 EATRERILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALEEALA-AEDPRERLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 112 KLVVQLMCSYAEHYPFLYVYLQENMAhvdpkrkawAAEMRRVNRRYEAAVTDIIGQGIDEGSIRAVGEPWVLAYGLMGMV 191
Cdd:COG1309    84 ALLRAYLEFLAENPALARLLLAEAAE---------LPELRAALRALLRRLRALLAELLRAGGLLADVDPDALARALLALL 154
TetR_C_24 pfam17932
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 103-222 3.39e-20

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: 82.22  E-value: 3.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 103 SASATVKLRKLVVQLMCSYAEHYPFLYVYLQEnMAHVDPKRKAWAAEMRRvnrRYEAAVTDIIGQGIDEGSIRAVgEPWV 182
Cdd:pfam17932   1 GGSPVERLRALVRAHVRVHAERRDEAAVFLRE-LRSLSPEHRAEIRALRR---EYERLLRDLIEEGVAAGEFRDL-DPKL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2045876398 183 LAYGLMGMVSWTHRWFNPNtAEVDAKTIGESYADVLLSGL 222
Cdd:pfam17932  76 AALAILGMLNWVYRWYRPD-GPLSPEEIADQYADLLLRGL 114
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
38-82 5.94e-12

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 58.57  E-value: 5.94e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2045876398  38 ILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFD 82
Cdd:pfam00440   1 ILDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSKEELLE 45
septum_RefZ NF037937
forespore capture DNA-binding protein RefZ; RefZ (regulator of FtsZ), a DNA-binding protein in ...
 38-125 2.21e-11

forespore capture DNA-binding protein RefZ; RefZ (regulator of FtsZ), a DNA-binding protein in the family of TetR/AcrR family transcriptional regulators, participates in septum placement and in chromosome capture during the asymmetrical cell division in endospore formation. The five nearly palindromic DNA motifs (RBMs) to which RefZ binds affect chromosomal localization, not transcription, so RefZ is not considered a transcription factor.


Pssm-ID: 468281 [Multi-domain]  Cd Length: 195  Bit Score: 61.00  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  38 ILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQ--IRDSSASATVKLRKLVV 115
Cdd:NF037937    4 ILDAAISLFNTKGFDGTSVRDIAKKAKVNVALISYYFKGKQGLLEYLVTSFFEGYLEILEEgfEELKNLSAKECLKQLVR 83

                          90
                  ....*....|
gi 2045876398 116 QLMCSYAEHY 125
Cdd:NF037937   84 NILHYQQEHH 93
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
32-177 6.35e-09

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 53.79  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFDVLVTDVVKGNLAIAEQIRDsSASATVKLR 111
Cdd:COG3226     7 EERRERILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRDELLAAAFERLAEREAARLRALLA-AADDLEDAA 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045876398 112 KLVVQLMCSYAEHYPFLYVYLQENM--AHVDPKRKAWAAEMRRVNRRYEAAVTDIIGQGIDEGSIRAV 177
Cdd:COG3226    86 EALADLLAELLPADRDRLLARYELYleALRDPELRALLRRWRDRLREALARLLAALGSPDPPETARAL 153
ScbR_bind_reg NF041196
ScbR family autoregulator-binding transcription factor;
35-80 7.19e-09

ScbR family autoregulator-binding transcription factor;


Pssm-ID: 469100 [Multi-domain]  Cd Length: 191  Bit Score: 53.75  E-value: 7.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2045876398  35 RAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEV 80
Cdd:NF041196    8 RRAILEAAAEVFDERGYAAATISDILERAGVTKGALYFHFSSKEAL 53
PRK10668 PRK10668
DNA-binding transcriptional repressor AcrR; Provisional
 32-82 3.95e-05

DNA-binding transcriptional repressor AcrR; Provisional


Pssm-ID: 182632 [Multi-domain]  Cd Length: 215  Bit Score: 43.07  E-value: 3.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFD 82
Cdd:PRK10668   10 QETRQHILDAALRLFSQQGVSATSLADIAKAAGVTRGAIYWHFKNKSDLFS 60
PRK15008 PRK15008
HTH-type transcriptional regulator RutR; Provisional
 18-81 1.36e-04

HTH-type transcriptional regulator RutR; Provisional


Pssm-ID: 184970 [Multi-domain]  Cd Length: 212  Bit Score: 41.84  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045876398  18 QRRATAQGQKNAGYEDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVF 81
Cdd:PRK15008    3 QGAVKTTGKRSRAVSAKKKAILSAALDTFSQFGFHGTRLEQIAELAGVSKTNLLYYFPSKEALY 66
PRK14996 PRK14996
TetR family transcriptional regulator; Provisional
 32-191 2.90e-04

TetR family transcriptional regulator; Provisional


Pssm-ID: 184958 [Multi-domain]  Cd Length: 192  Bit Score: 40.46  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSS----KEEVFDVLvtdvVKGNLAIAEQIRDSSASAt 107
Cdd:PRK14996    7 DERREVILQAAMRVALAEGFAAMTVRRIASEAQVAAGQVHHHFSSagelKALAFIHL----IRQLLDAEQVPQTASWRE- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398 108 vklrKLVVQLMCSYAEHYPFLYVYLQ-ENMAHVDPK-RKAWAAEMrrvnRRYEAAVTDIIGQGIDEGSIRAVGEPWVLAY 185
Cdd:PRK14996   82 ----RLHAMLGSEDGRFEPYIRLWREaQILADRDPEiKDAYLLTM----QMWHQETVAIIEQGKAAGEFRSTSNATDIAW 153


                  ....*.
gi 2045876398 186 GLMGMV 191
Cdd:PRK14996  154 RLIALV 159
PRK09975 PRK09975
DNA-binding transcriptional regulator EnvR; Provisional
 19-82 2.40e-03

DNA-binding transcriptional regulator EnvR; Provisional


Pssm-ID: 182177 [Multi-domain]  Cd Length: 213  Bit Score: 37.80  E-value: 2.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045876398  19 RRATAQGQKNagyedrRAQILHAAALLFRTGGYRGTSIGKIAEEVGTDRASIYYYFSSKEEVFD 82
Cdd:PRK09975    3 KKTKAEALKT------RQELIETAIAQFALRGVSNTTLNDIADAANVTRGAIYWHFENKTQLFN 60
PRK11552 PRK11552
putative DNA-binding transcriptional regulator; Provisional
 32-101 4.47e-03

putative DNA-binding transcriptional regulator; Provisional


Pssm-ID: 236928 [Multi-domain]  Cd Length: 225  Bit Score: 37.34  E-value: 4.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045876398  32 EDRRAQILHAAALLFRTGGYRGTSiGKIAEEVGTDRASIYYYFSSKEEVFdvlvtdvvkgnLAIAEQIRD 101
Cdd:PRK11552   12 EQAKQQLIAAALAQFGEYGLHATT-RDIAAQAGQNIAAITYYFGSKEDLY-----------LAVAQWIAD 69
slmA PRK09480
division inhibitor protein; Provisional
 34-85 5.11e-03

division inhibitor protein; Provisional


Pssm-ID: 181894 [Multi-domain]  Cd Length: 194  Bit Score: 36.71  E-value: 5.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2045876398  34 RRAQILHA-AALLFRTGGYRGTSiGKIAEEVGTDRASIYYYFSSKEEVFDVLV 85
Cdd:PRK09480   11 RREQILQAlAQMLESPPGERITT-AKLAARVGVSEAALYRHFPSKARMFEGLI 62
 
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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