Conserved Protein Domain Family
HTH_MlrA-like

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cd04763: HTH_MlrA-like 
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.
Statistics
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PSSM-Id: 133391
Aligned: 3 rows
Threshold Bit Score: 99.1462
Created: 8-Dec-2006
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
DNA binding
Feature 1:DNA binding residues [nucleic acid binding site]
Evidence:
  • Comment:Based on sequence similarity to BmrR and the structure of Bacillus subtilis BmrR bound to DNA (1EXI).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        ###             #                ###                                
P33358        4 YTIGEVALLCDINPVTLRAWQRRYGLlkPQRTDgGHRLFNdADIDRIREIKRWId-nGVQVSKVKMLLS 71  Escherichia coli
ZP_01361430   8 YSISQVAEYTGFKPHVIRFYEKEFNLn-IPRSEnARRYFTkKEINLFLYIKSLQe-kGSSNKEIKKLLK 74  Clostridium sp. OhILAs
YP_356841    11 FKIGEVAQLTGVKPHVLRYWESEFRQirPVKSQgKQRLYRrDDIEFVLNLKDILygqGYTIAGAKKILA 79  Pelobacter carbinolicus DSM...

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