MerR family transcriptional regulator [Mycolicibacterium monacense]
Protein Classification
MerR family transcriptional regulator( domain architecture ID 10140973)
MerR family transcriptional regulator activates transcription through protein-dependent DNA distortion and the majority of regulators in the family respond to environmental stimuli, such as oxidative stress, heavy metals or antibiotics
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| HTH_MerR-like_sg2 | cd04778 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
5-220 | 1.28e-81 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 2). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. : Pssm-ID: 133405 [Multi-domain] Cd Length: 219 Bit Score: 243.45 E-value: 1.28e-81
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| Name | Accession | Description | Interval | E-value | ||||
| HTH_MerR-like_sg2 | cd04778 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
5-220 | 1.28e-81 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 2). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133405 [Multi-domain] Cd Length: 219 Bit Score: 243.45 E-value: 1.28e-81
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| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
6-69 | 7.15e-17 | ||||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 72.59 E-value: 7.15e-17
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| SoxR | COG0789 | DNA-binding transcriptional regulator, MerR family [Transcription]; |
10-94 | 7.16e-11 | ||||
DNA-binding transcriptional regulator, MerR family [Transcription]; Pssm-ID: 440552 [Multi-domain] Cd Length: 100 Bit Score: 57.22 E-value: 7.16e-11
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| HTH_MERR | smart00422 | helix_turn_helix, mercury resistance; |
6-72 | 5.87e-10 | ||||
helix_turn_helix, mercury resistance; Pssm-ID: 197716 Cd Length: 70 Bit Score: 54.06 E-value: 5.87e-10
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| CueR | TIGR02044 | Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and ... |
8-70 | 2.27e-05 | ||||
Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue. [Regulatory functions, DNA interactions] Pssm-ID: 131099 [Multi-domain] Cd Length: 127 Bit Score: 42.82 E-value: 2.27e-05
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| PRK10227 | PRK10227 | HTH-type transcriptional regulator CueR; |
8-114 | 6.32e-05 | ||||
HTH-type transcriptional regulator CueR; Pssm-ID: 182320 Cd Length: 135 Bit Score: 41.56 E-value: 6.32e-05
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| Name | Accession | Description | Interval | E-value | ||||
| HTH_MerR-like_sg2 | cd04778 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
5-220 | 1.28e-81 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 2). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133405 [Multi-domain] Cd Length: 219 Bit Score: 243.45 E-value: 1.28e-81
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| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
6-69 | 7.15e-17 | ||||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 72.59 E-value: 7.15e-17
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| HTH_MerR-like | cd00592 | Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ... |
6-86 | 1.04e-12 | ||||
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133378 [Multi-domain] Cd Length: 100 Bit Score: 62.26 E-value: 1.04e-12
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| SoxR | COG0789 | DNA-binding transcriptional regulator, MerR family [Transcription]; |
10-94 | 7.16e-11 | ||||
DNA-binding transcriptional regulator, MerR family [Transcription]; Pssm-ID: 440552 [Multi-domain] Cd Length: 100 Bit Score: 57.22 E-value: 7.16e-11
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| HTH_TipAL-Mta | cd01106 | Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; ... |
6-94 | 3.63e-10 | ||||
Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; Helix-turn-helix (HTH) TipAL, Mta, and SkgA transcription regulators, and related proteins, N-terminal domain. TipAL regulates resistance to and activation by numerous cyclic thiopeptide antibiotics, such as thiostrepton. Mta is a global transcriptional regulator; the N-terminal DNA-binding domain of Mta interacts directly with the promoters of mta, bmr, blt, and ydfK, and induces transcription of these multidrug-efflux transport genes. SkgA has been shown to control stationary-phase expression of catalase-peroxidase in Caulobacter crescentus. These proteins are comprised of distinct domains that harbor an N-terminal active (DNA-binding) site and a regulatory (effector-binding) site. The conserved N-terminal domain of these transcription regulators contains winged HTH motifs that mediate DNA binding. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Unique to this family, is a TipAL-like, lineage specific Bacilli subgroup, which has five conserved cysteines in the C-terminus of the protein. Pssm-ID: 133381 [Multi-domain] Cd Length: 103 Bit Score: 55.57 E-value: 3.63e-10
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| HTH_MERR | smart00422 | helix_turn_helix, mercury resistance; |
6-72 | 5.87e-10 | ||||
helix_turn_helix, mercury resistance; Pssm-ID: 197716 Cd Length: 70 Bit Score: 54.06 E-value: 5.87e-10
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| HTH_MerR2 | cd04769 | Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix ... |
10-72 | 2.89e-09 | ||||
Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MerR2 and related proteins. MerR2 in Bacillus cereus RC607 regulates resistance to organomercurials. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133397 [Multi-domain] Cd Length: 116 Bit Score: 53.52 E-value: 2.89e-09
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| HTH_MerR-SF | cd04761 | Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ... |
6-54 | 4.41e-08 | ||||
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133389 [Multi-domain] Cd Length: 49 Bit Score: 48.36 E-value: 4.41e-08
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| HTH_MerR-like_sg3 | cd01282 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
7-77 | 5.05e-08 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 3). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133388 Cd Length: 112 Bit Score: 49.91 E-value: 5.05e-08
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| HTH_MerR-like_sg5 | cd04780 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
6-79 | 5.29e-07 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 5), N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133407 Cd Length: 95 Bit Score: 46.55 E-value: 5.29e-07
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| HTH_GlnR-like | cd01105 | Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix ... |
6-69 | 5.79e-07 | ||||
Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator GlnR and related proteins, N-terminal domain. The GlnR and TnrA (also known as ScgR) proteins have been shown to regulate expression of glutamine synthetase as well as several genes involved in nitrogen metabolism. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133380 Cd Length: 88 Bit Score: 46.45 E-value: 5.79e-07
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| HTH_HMRTR | cd04770 | Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ... |
6-72 | 2.16e-06 | ||||
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133398 [Multi-domain] Cd Length: 123 Bit Score: 45.63 E-value: 2.16e-06
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| HTH_CadR-PbrR | cd04784 | Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; ... |
6-59 | 3.64e-06 | ||||
Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; Helix-turn-helix (HTH) CadR and PbrR transcription regulators including Pseudomonas aeruginosa CadR and Ralstonia metallidurans PbrR that regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which form a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Pssm-ID: 133411 Cd Length: 127 Bit Score: 44.87 E-value: 3.64e-06
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| CueR | TIGR02044 | Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and ... |
8-70 | 2.27e-05 | ||||
Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue. [Regulatory functions, DNA interactions] Pssm-ID: 131099 [Multi-domain] Cd Length: 127 Bit Score: 42.82 E-value: 2.27e-05
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| HTH_MerR-like_sg6 | cd04781 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
10-72 | 2.48e-05 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 6) with at least two conserved cysteines present in the C-terminal portion of the protein. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133408 Cd Length: 120 Bit Score: 42.66 E-value: 2.48e-05
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| HTH_MerR-like_sg4 | cd04779 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
6-71 | 2.57e-05 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 4). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133406 [Multi-domain] Cd Length: 134 Bit Score: 42.88 E-value: 2.57e-05
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| HTH_CueR | cd01108 | Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ... |
9-72 | 3.40e-05 | ||||
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Pssm-ID: 133383 [Multi-domain] Cd Length: 127 Bit Score: 42.16 E-value: 3.40e-05
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| HTH_TioE_rpt1 | cd04772 | First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ... |
6-59 | 4.40e-05 | ||||
First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD contains the N-terminal or first repeat (rpt1) of these tandem MerR-like domain proteins. Pssm-ID: 133399 Cd Length: 99 Bit Score: 41.22 E-value: 4.40e-05
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| MerR | pfam00376 | MerR family regulatory protein; |
10-36 | 4.57e-05 | ||||
MerR family regulatory protein; Pssm-ID: 425647 [Multi-domain] Cd Length: 38 Bit Score: 39.71 E-value: 4.57e-05
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| PRK10227 | PRK10227 | HTH-type transcriptional regulator CueR; |
8-114 | 6.32e-05 | ||||
HTH-type transcriptional regulator CueR; Pssm-ID: 182320 Cd Length: 135 Bit Score: 41.56 E-value: 6.32e-05
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| HTH_MlrA-CarA | cd01104 | Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; ... |
6-69 | 6.61e-05 | ||||
Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA- and CarA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins. Pssm-ID: 133379 Cd Length: 68 Bit Score: 39.92 E-value: 6.61e-05
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| zntR | PRK09514 | Zn(2+)-responsive transcriptional regulator; |
6-69 | 1.50e-04 | ||||
Zn(2+)-responsive transcriptional regulator; Pssm-ID: 181924 [Multi-domain] Cd Length: 140 Bit Score: 40.72 E-value: 1.50e-04
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| HTH_YfmP | cd04774 | Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) ... |
6-80 | 2.30e-04 | ||||
Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) transcription regulator, YfmP, and related proteins; N-terminal domain. YfmP regulates the multidrug efflux protein, YfmO, and indirectly regulates the expression of the Bacillus subtilis copZA operon encoding a metallochaperone, CopZ, and a CPx-type ATPase efflux protein, CopA. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133401 [Multi-domain] Cd Length: 96 Bit Score: 39.42 E-value: 2.30e-04
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| HTH_BmrR-like | cd04768 | Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix ... |
6-69 | 3.32e-04 | ||||
Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix (HTH) BmrR-like transcription regulators (TipAL, Mta, SkgA, BmrR, and BltR), N-terminal domain. These proteins have been shown to regulate expression of specific regulons in response to various toxic substances, antibiotics, or oxygen radicals in Bacillus subtilis, Streptomyces, and Caulobacter crescentus. They are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Pssm-ID: 133396 [Multi-domain] Cd Length: 96 Bit Score: 38.87 E-value: 3.32e-04
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| HTH_MlrA-like | cd04763 | Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix ... |
6-72 | 6.13e-04 | ||||
Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A) and related proteins, N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins. Pssm-ID: 133391 Cd Length: 68 Bit Score: 37.51 E-value: 6.13e-04
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| HTH_BmrR | cd01107 | Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) ... |
10-88 | 7.77e-04 | ||||
Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Pssm-ID: 133382 [Multi-domain] Cd Length: 108 Bit Score: 37.88 E-value: 7.77e-04
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| HTH_YyaN | cd01109 | Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; ... |
6-77 | 8.84e-03 | ||||
Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133384 [Multi-domain] Cd Length: 113 Bit Score: 35.13 E-value: 8.84e-03
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| HTH_MerR-like_sg7 | cd04786 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
7-90 | 9.15e-03 | ||||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 7) with a conserved cysteine present in the C-terminal portion of the protein. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133413 [Multi-domain] Cd Length: 131 Bit Score: 35.57 E-value: 9.15e-03
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