Conserved Protein Domain Family
HTH_HspR

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cd04766: HTH_HspR 
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator
Helix-turn-helix (HTH) transcription regulator HspR, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. 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 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.
Statistics
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PSSM-Id: 133394
View PSSM: cd04766
Aligned: 18 rows
Threshold Bit Score: 113.514
Threshold Setting Gi: 111020554
Created: 26-Jan-2007
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
DNA bindingputative dimer
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         ###             #                         ###                                 
CAB08585     12 TFLISVAAELAGMHAQTLRTYDRLGLVSPRRTSG----------GGRRYSlHDVELLRQVQHLSQdEGVNLAGIKRIIEl 81  Mycobacterium tu...
NP_787875     6 FFTVTVAAALSGMHPQTLRKLDRLGLLSPKRTLG----------GDRRYTaQDVEGLRAISSMVS-SGLTLEGIKHIAR- 73  Tropheryma whipp...
YP_703526    17 VYSISVAAELSGFGIAALRLYEEYGLITPLRTGG----------GTRRYSdHDLARLERVAELID-SGVNLVGIGRVLDl 85  Rhodococcus sp. ...
YP_714230    12 VYGISVAADLVGMDPQSLRAYERRGLLDPARTGG----------GTRRYSsDDLARLQRIGHLLA-AGLNLAGIARVLE- 79  Frankia alni ACN14a
BAC90804     12 VYIISVAAELVGMHPQTLRQYERAGLVHPYRMPGrgegkggkerETRLYSeHDIEQLRYIKRLTQeLKVNLEGVKQIAL- 90  Gloeobacter viol...
NP_294658   133 VYVISIAAELVDMHPQTLRLYERKQLIHPGRSSG----------KTRLYSeRDIEHLREIRRLTQeLGVNLAGVEEIMR- 201 Deinococcus radi...
YP_643567     8 VFMIGVAAELIGVHPQTLRMYEQKGLLRPRKSLK----------NTRLYSqEDIELGRYIQRLTQeMGMNLAGVKKILE- 76  Rubrobacter xyla...
AAD08067      8 LYLISVVAKILGVHPQTLRQYEKEGLIEPSRTDG----------KMRLYSqRDMDKIKTILRLTRdMGVNLAGVDIILR- 76  Helicobacter pyl...
AAC06883      7 YYTIGVVAKMYNIHPQTLRLYEREGLLKPSRSEG----------NTRLYTdEDLERLEFILFLTReLGVNLAGVDIILN- 75  Aquifex aeolicus...
ZP_01356458   5 YYTIKAAAALCGMHEQSLRLYERRGLIRPQRTPG----------NIRRYSeSDIEQIRFIKRLIDdLGVNLAGVEVILH- 73  Roseiflexus sp. ...
Feature 1                                   
CAB08585     82 tsqveaLQSRLQEMAEELAVLRANQRRE 109 Mycobacterium tuberculosis H37Rv
NP_787875    74 ------LEKELASLKAENHLLRQKLKND 95  Tropheryma whipplei str. Twist
YP_703526    86 ehrtgeLERDNRRLAADNAQLRAEQTPA 113 Rhodococcus sp. RHA1
YP_714230    80 ------LETENARLRAALELTQAADVKP 101 Frankia alni ACN14a
BAC90804     91 ------LKEELDLRQRELDKQKQKMQQE 112 Gloeobacter violaceus PCC 7421
NP_294658   202 ------LRHELDASRAHLEGNVRRLQDD 223 Deinococcus radiodurans R1
YP_643567    77 ------LEREIQSLRAENSRLRQEMERR 98  Rubrobacter xylanophilus DSM 9941
AAD08067     77 ------LKEKLDELDNLNKELQDALHKH 98  Helicobacter pylori 26695
AAC06883     76 ------LKEQMEQMQKQIDQLMEFIQNE 97  Aquifex aeolicus VF5
ZP_01356458  74 ------LRQQLIEVQRELEELRSRMPVD 95  Roseiflexus sp. RS-1

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