1IZ1,1IXC


Conserved Protein Domain Family
PBP2_CbnR

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cd08486: PBP2_CbnR 
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The C-terminal substrate binding domain of LysR-type transcriptional regulator, CbnR, involved in the chlorocatechol catabolism, contains the type 2 periplasmic binding fold.
This CD represents the substrate binding domain of LysR-type regulator CbnR which is involved in the regulation of chlorocatechol breakdown. The chlorocatechol-degradative pathway is often found in bacteria that can use chlorinated aromatic compounds as carbon and energy sources. CbnR is found in the 3-chlorobenzoate degradative bacterium Ralstonia eutropha NH9 and forms a tetramer. CbnR activates the expression of the cbnABCD genes, which are responsible for the degradation of chlorocatechol converted from 3-chlorobenzoate and are transcribed divergently from cbnR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Statistics
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PSSM-Id: 176175
View PSSM: cd08486
Aligned: 5 rows
Threshold Bit Score: 374.047
Threshold Setting Gi: 33357068
Created: 19-Oct-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
dimerizationputative
Conserved site includes 32 residues -Click on image for an interactive view with Cn3D
Feature 1:dimerization interface [polypeptide binding site]
Evidence:
  • Structure:1IZ1; interface at a dimeric unit of Cupriavidus necator CbnR, contacts at 4 A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #    ###  ##  #  #       ##             ##         #                     #
1IZ1_A     91 GELSVAYFGtPIYRSLPLLLRAFLTSTPtATVSLTHmtkdEQVEGLLAGtIHVGFSRFFPRHpgIEIVNIAQeDLYLAVH 170 Cupriavidus necator
1IXC_A     91 GELSVAYFGtPIYRSLPLLLRAFLTSTPtATVSLTHxtkdEQVEGLLAGtIHVGFSRFFPRHpgIEIVNIAQeDLYLAVH 170 Ralstonia eutropha
ABP88940   91 GELSVAYFGtPIYRSLPLLLRAFFTSTPtATVSLTHmtkdEQVEGLLAGtIHVGFSRFFPRHpgIEIVNIAQeDLYLAVH 170 Pseudomonas nitror...
ABP88941   90 GELSVAYFGtPIYRSLPLLLRAFFTSTPtATVSLTHmtkdEQVEGLLAGtIHVGFSRFFPRHpgIEIVNIAQeDLYLAVH 169 Pseudomonas aerugi...
P27102     91 GELSVAYFGtPIYRSLPLLLRAFLTSTPtATVSLTHmtkdEQVEGLLAGtIHVGFSRFFPRHpgIEIVNIAQeDLYLAVH 170 Pseudomonas sp. P51
Feature 1                                  #  ### #        ## # #  #      #  ##             ##
1IZ1_A    171 RSQsgkfGKTCKLadLRAVELTLFPrggrPSFADEVIGLFkhaGIEPRIARVVEDAtAALALTMAGaASSIVPASvaaIR 250 Cupriavidus necator
1IXC_A    171 RSQsgkfGKTCKLadLRAVELTLFPrggrPSFADEVIGLFkhaGIEPRIARVVEDAtAALALTXAGaASSIVPASvaaIR 250 Ralstonia eutropha
ABP88940  171 RSQsgkfGKTCKLadLRAVELTLFPrggrPSFADEVIGLFkhaGIEPRIARVVEDAtAALALTMAGaASSIVPASvaaIR 250 Pseudomonas nitror...
ABP88941  170 RSQsgkfGKTCKLadLRAVELTLFPrggrPSFADEVIGLFkhaGIEPRIARVVEGAtAALALTMAGaASSIVPASvaaIR 249 Pseudomonas aerugi...
P27102    171 RSQsgkfGKTCKLadLRAVELTLFPrggrPSFADEVIGLFkhaGIEPRIARVVEDAtAALALTMAGaASSIVPASvaaIR 250 Pseudomonas sp. P51
Feature 1     ##                    #               
1IZ1_A    251 WPDIAFARIVgtrvKVPISCIFRKekqpPILARFVEHV 288 Cupriavidus necator
1IXC_A    251 WPDIAFARIVgtrvKVPISCIFRKekqpPILARFVEHV 288 Ralstonia eutropha
ABP88940  251 WPDIAFARIVgtrvKVPISCIFRKekqpPILARFVEHV 288 Pseudomonas nitroreducens
ABP88941  250 WPDIAFARIVgtrvKVPISCIFRKekqpPILARFVEHV 287 Pseudomonas aeruginosa
P27102    251 WPDIAFARIVgtrvKVPISCTFRKekqpPILARFVEHV 288 Pseudomonas sp. P51

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