1EXI


Conserved Protein Domain Family
HTH_BmrR

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cd01107: HTH_BmrR 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 133382
View PSSM: cd01107
Aligned: 60 rows
Threshold Bit Score: 112.997
Threshold Setting Gi: 42521663
Created: 30-Apr-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:DNA binding residues [nucleic acid binding site]
Evidence:
  • Structure:1EXI; Bacillus subtilis BmrR bound to DNA; defined at 3.5A contacts.
    View structure with Cn3D
  • Comment:these residues contact two consecutive major grooves

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        ###             #                 ###                                          
1EXI_A        6 YSIGEVSKLANVSIKALRYYDKIDLFKPAYVDPdtSYRYYTdSQLIHLDLIKSLKY-IGTPLEEMKKAQDLEme----eL 80  Bacillus subtilis
CAJ70522      2 FSIGMFSKINKITTKTLRYYEDIGLLKPEYVDEftKYRYYTtEQLPKLHQIITLKQ-MGLSLAEIKKAVENPe-----eV 75  Clostridium diff...
ZP_01425775   2 LRIGAFSRIAHMTIDTLRHYDAVGLLKPAVIDPttGYRYYTaDQLQAVNQIVTLKE-LGFSLEEIAHIQKGHsss--adL 78  Herpetosiphon au...
ZP_00907674   5 YTIGEVSRYMNISTKILRHYDHLNLLKPCYISPdtKYRYFSyDQLFIIDVIRYLNKtLLIPLEDIKNILDENkdy--dkL 82  Clostridium beij...
ZP_01352284  13 FKIGEVAAMFDISTKTLRIYDRIGLLKPSSIDGesGYRYYSpNQISRLEVILNLKR-VGFSLSEISLFVNGDisn--neI 89  Clostridium phyt...
NP_782073    10 YSIGKVGEICKITKKALRYYDKMDILSPDKVSDesGYRYYSkKTLLSVPMIKYYKQ-SGFKLEEMKVFLEGEty---dfF 85  Clostridium teta...
ZP_01352238   7 YSIGEVSKSCNISTKALRFYDKMGIISPDVICKenSYRYYNkESLLTVPIVKYYKQ-MGFKLEEMQGLVEGNty---fyL 82  Clostridium phyt...
YP_389780     7 YSIGDVSQICNISKKALRYYDKIGLITSQRQDYn-NYRYYThESLLAVPVIKYYKQ-MGFKLDEMREFIEGStanvyraI 84  Desulfovibrio de...
YP_245814     2 YTIGKFSGICNLPVKTLRYYDDIGLLKPSYIDPktNYRYYDyDKIEAIKIIMLLKS-LHTPLADIKEIIERVdq---vqW 77  Bacillus cereus ...
CAG29277     50 YSIGKVSTLCNVPIKTLRYYDKIGLLVPEYRKCdsNYRYYTqDQILTLFIIRKLKH-LGIPLKDISQIVCKKna---saM 125 Clostridium prop...
Feature 1                                       
1EXI_A       81 FAFYTEQERQIREKLDFLSALEQTISLVKKRM 112 Bacillus subtilis
CAJ70522     76 ENILMNKEKEMLDVIKSEEYKIIKLRNYLMNL 107 Clostridium difficile 630
ZP_01425775  79 HALLQHQLRVTEQTITAAEQRRSRIQAHLHAV 110 Herpetosiphon aurantiacus ATCC 23779
ZP_00907674  83 LTFLESHKEQLDKKIADIEYSKQLTDSMISDI 114 Clostridium beijerincki NCIMB 8052
ZP_01352284  90 ATIFRKKHTQLQSMVDSLEYNMELIEDMISSL 121 Clostridium phytofermentans ISDg
NP_782073    86 HKSFRNKIDELKELEKEINLKIRSVKDWDDLI 117 Clostridium tetani E88
ZP_01352238  83 EHNFRNKIDQLRLQEQQIHNSYIAVKDWYELI 114 Clostridium phytofermentans ISDg
YP_389780    85 RNSFLSKIQELEKEQEEIRRKHMSVKDWYDLI 116 Desulfovibrio desulfuricans G20
YP_245814    78 NSIFEQKISELEKQKEQISKEIEEIKQLQIKM 109 Bacillus cereus E33L
CAG29277    126 GACIRERLYEISNAIDSLNNQYAEGQLLLERL 157 Clostridium propionicum

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