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Conserved domains on  [gi|1277463626|ref|WP_100066811|]
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TetR/AcrR family transcriptional regulator [Corynebacterium amycolatum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TetR_C_15 super family cl38975
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 71-184 9.34e-25

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 found in a number of different TetR transcription regulator proteins including SlmA proteins found in E. coli. Unlike other TetR proteins, SlmA functions not as a transcription regulator but rather as an NO (nucleoid occlusion) factor. 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.


The actual alignment was detected with superfamily member pfam17928:

Pssm-ID: 476838  Cd Length: 113  Bit Score: 92.77  E-value: 9.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  71 WPEFLSEFIDHLAKLWREDVSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYAL 150
Cdd:pfam17928   3 WWDALDRLIDRYAAMNRDEPVFRDLWFADQADPRLADIDADNNRALAARFARALAPLAPDGDGDELVRTAAVLMHLADAL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277463626 151 LNYAVDHPGSDAEReahyelTVQEIKRMTISYLM 184
Cdd:pfam17928  83 LRLAIALDPDEDDA------IVDEAKRMLRRYLA 110
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
1-125 7.69e-09

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


:

Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 52.21  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626   1 MLSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANKYVMICELDRQDTAAVIEEVSrfgERVPTLKWPEFLSEFID 80
Cdd:COG1309    11 ILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALE---EALAAEDPRERLRALLR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1277463626  81 HLAKLWREDVSRRAVWLA-VQSTPATRATAEDTKSRLVTEISKVLR 125
Cdd:COG1309    88 AYLEFLAENPALARLLLAeAAELPELRAALRALLRRLRALLAELLR 133
 
Name Accession Description Interval E-value
TetR_C_22 pfam17928
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 71-184 9.34e-25

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 the TetR Transcriptional Repressor present in sco1712 proteins from Streptomyces coelicolo which act as a regulator of antibiotic production.


Pssm-ID: 465571  Cd Length: 113  Bit Score: 92.77  E-value: 9.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  71 WPEFLSEFIDHLAKLWREDVSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYAL 150
Cdd:pfam17928   3 WWDALDRLIDRYAAMNRDEPVFRDLWFADQADPRLADIDADNNRALAARFARALAPLAPDGDGDELVRTAAVLMHLADAL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277463626 151 LNYAVDHPGSDAEReahyelTVQEIKRMTISYLM 184
Cdd:pfam17928  83 LRLAIALDPDEDDA------IVDEAKRMLRRYLA 110
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
1-125 7.69e-09

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 52.21  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626   1 MLSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANKYVMICELDRQDTAAVIEEVSrfgERVPTLKWPEFLSEFID 80
Cdd:COG1309    11 ILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALE---EALAAEDPRERLRALLR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1277463626  81 HLAKLWREDVSRRAVWLA-VQSTPATRATAEDTKSRLVTEISKVLR 125
Cdd:COG1309    88 AYLEFLAENPALARLLLAeAAELPELRAALRALLRRLRALLAELLR 133
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
2-40 8.55e-06

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 41.24  E-value: 8.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1277463626   2 LSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANK 40
Cdd:pfam00440   2 LDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSK 40
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
1-164 8.45e-05

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 41.46  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626   1 MLSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANK-----YVM--ICELDRQDTAAVIEEVSRFGERVptlkwpE 73
Cdd:COG3226    13 ILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRdellaAAFerLAEREAARLRALLAAADDLEDAA------E 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  74 FLSEFIDHLAKLWRED-VSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYALLN 152
Cdd:COG3226    87 ALADLLAELLPADRDRlLARYELYLEALRDPELRALLRRWRDRLREALARLLAALGSPDPPETARALVALIDGLTLHALL 166

                         170
                  ....*....|..
gi 1277463626 153 YAVDHPGSDAER 164
Cdd:COG3226   167 DPDPLTREELRA 178
 
Name Accession Description Interval E-value
TetR_C_22 pfam17928
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 71-184 9.34e-25

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 the TetR Transcriptional Repressor present in sco1712 proteins from Streptomyces coelicolo which act as a regulator of antibiotic production.


Pssm-ID: 465571  Cd Length: 113  Bit Score: 92.77  E-value: 9.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  71 WPEFLSEFIDHLAKLWREDVSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYAL 150
Cdd:pfam17928   3 WWDALDRLIDRYAAMNRDEPVFRDLWFADQADPRLADIDADNNRALAARFARALAPLAPDGDGDELVRTAAVLMHLADAL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277463626 151 LNYAVDHPGSDAEReahyelTVQEIKRMTISYLM 184
Cdd:pfam17928  83 LRLAIALDPDEDDA------IVDEAKRMLRRYLA 110
TetR_C_15 pfam17918
Tetracyclin repressor-like, C-terminal domain; TetR family regulators are involved in the ...
 71-183 8.83e-11

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 found in a number of different TetR transcription regulator proteins including SlmA proteins found in E. coli. Unlike other TetR proteins, SlmA functions not as a transcription regulator but rather as an NO (nucleoid occlusion) factor. 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: 465566  Cd Length: 108  Bit Score: 56.52  E-value: 8.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  71 WPEFLSEFIDHLAKLWREDVSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYAL 150
Cdd:pfam17918   2 LAEALDALVDALVAAHRENPALRRVLYAVAPSPGLLELVEALDQEIAAALAALLARRAPALPPEDLELAAFVAVEAVEAL 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1277463626 151 LNYAVDHPGSDAEReahyelTVQEIKRMTISYL 183
Cdd:pfam17918  82 LHLALEEDPADREA------LIEELKRLLLAYL 108
AcrR COG1309
DNA-binding protein, AcrR family, includes nucleoid occlusion protein SlmA [Transcription];
1-125 7.69e-09

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


Pssm-ID: 440920 [Multi-domain]  Cd Length: 156  Bit Score: 52.21  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626   1 MLSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANKYVMICELDRQDTAAVIEEVSrfgERVPTLKWPEFLSEFID 80
Cdd:COG1309    11 ILDAALELFAEKGYEGTSVRDIAARAGVSKGTLYRHFGSKEELLLAVLERLLEELLAALE---EALAAEDPRERLRALLR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1277463626  81 HLAKLWREDVSRRAVWLA-VQSTPATRATAEDTKSRLVTEISKVLR 125
Cdd:COG1309    88 AYLEFLAENPALARLLLAeAAELPELRAALRALLRRLRALLAELLR 133
TetR_N pfam00440
Bacterial regulatory proteins, tetR family;
2-40 8.55e-06

Bacterial regulatory proteins, tetR family;


Pssm-ID: 425684 [Multi-domain]  Cd Length: 47  Bit Score: 41.24  E-value: 8.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1277463626   2 LSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANK 40
Cdd:pfam00440   2 LDAARELFAERGYDATTVREIAKRAGVSKGALYRYFGSK 40
YbjK COG3226
DNA-binding transcriptional regulator YbjK [Transcription];
1-164 8.45e-05

DNA-binding transcriptional regulator YbjK [Transcription];


Pssm-ID: 442459 [Multi-domain]  Cd Length: 191  Bit Score: 41.46  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626   1 MLSSARTVLIEHGFESFTFDEVARIADIPIGTLYQFFANK-----YVM--ICELDRQDTAAVIEEVSRFGERVptlkwpE 73
Cdd:COG3226    13 ILEAALRVIARDGVRGVTHRAVAAEAGVPLGSTTYYFRTRdellaAAFerLAEREAARLRALLAAADDLEDAA------E 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277463626  74 FLSEFIDHLAKLWRED-VSRRAVWLAVQSTPATRATAEDTKSRLVTEISKVLRPLVPSSSDAELNFISDLMINATYALLN 152
Cdd:COG3226    87 ALADLLAELLPADRDRlLARYELYLEALRDPELRALLRRWRDRLREALARLLAALGSPDPPETARALVALIDGLTLHALL 166

                         170
                  ....*....|..
gi 1277463626 153 YAVDHPGSDAER 164
Cdd:COG3226   167 DPDPLTREELRA 178
 
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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