Conserved Protein Domain Family
PBP2_AmpR

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cd08488: PBP2_AmpR 
The C-terminal substrate domain of LysR-type transcriptional regulator AmpR that involved in control of the expression of beta-lactamase gene ampC, contains the type 2 periplasmic binding fold.
AmpR acts as a transcriptional activator by binding to a DNA region immediately upstream of the ampC promoter. In the absence of a beta-lactam inducer, AmpR represses the synthesis of beta-lactamase, whereas expression is induced in the presence of a beta-lactam inducer. The AmpD, AmpG, and AmpR proteins are involved in the induction of AmpC-type beta-lactamase (class C) which produced by enterobacterial strains and many other gram-negative bacilli. The activation of ampC by AmpR requires ampG for induction or high-level expression of AmpC. It is probable that the AmpD and AmpG work together to modulate the ability of AmpR to activate ampC expression. This substrate-binding domain shows significant homology to 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: 176177
View PSSM: cd08488
Aligned: 5 rows
Threshold Bit Score: 340.278
Threshold Setting Gi: 157403315
Created: 21-Oct-2009
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putativeputative
Feature 1:putative substrate binding pocket [chemical binding site]
Evidence:
  • Comment:based on the sequence-structure comparison with Vibrio Parahaemolyticus GcdR-like structure (2QSX_A).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           ## #                                                                      
CAC04521   95 ILRVGAVGTLAVGWLLPRLRDFQNRYPfIDLRLSTnnnrVDIAAEGLDYAIRFGsgaWHGIDATRLLEAPLSPLCIPela 174 Ochrobactrum anthropi
NP_357520  95 LLFLGVVGTFAVGWLLPRLAAFQKRHPfIDVRVSTnnnrVDMAAEGLDFAIRFGqgsWHGTDAFRLFEAPLSPLCTPkla 174 Agrobacterium tume...
YP_261150  95 VLTVGAVGTFAVGWLLPRLEDFQARHPyVDLRLSTnnnrVDVAAEGLDYAIRFGtgaWHGIEALALLQAPLSVLCVPela 174 Pseudomonas fluore...
ACO76005   95 PLHVGVVGTFATGWLLPRLPGFVNSHPrIDLRLSThnnrVDIAAEGLDYAVKFGsgaWQDLDATPLFEAPLSPLCTPela 174 Laribacter hongkon...
EDO69407   51 VVHVGAVGTFACGWLLPRLAEFARLHPsVDVRLSThnnrVDPAAEGLDYAVRFGrgtWPGMESRFLMGAPLAPLCTPaia 130 Dehalococcoides sp...
Feature 1                                                 ###                   #             
CAC04521  175 relrtPVDLARHTLLRSYRADEWTQWFvaagvtgdmplprSIMFDSSLAMMEAAMQgaGIALAPplMFSRQLLSETIVQP 254 Ochrobactrum anthropi
NP_357520 175 emlkePADLMDATLLRSYRADEWSTWFaaagvspaaqvnaGIVFDTSLGMMEAALQglGVALAPpsMFSRHLTSGAVMQP 254 Agrobacterium tume...
YP_261150 175 rqlhsPADLLGQTLLRSYRTDEWPQWFqaaglgansllpqSVVFDSSLGMLEAALQglGVALAPplMFQRQLASGAVVQP 254 Pseudomonas fluore...
ACO76005  175 rtlsqPADVLAHTLLRSYRADEWPQWLreagvghpvfirnSIMFDSSIGMIEAARQgaGIALAPpaMFTRALARGELVQP 254 Laribacter hongkon...
EDO69407  131 qqlrePAELARFALLRSYFVDDWRLWFeaaqav-pcgpinGTIFDSSLTMVQCALQnlGVALAPpsMFAREIAQGLLVQP 209 Dehalococcoides sp...
Feature 1                                    
CAC04521  255 FettvtMGSYWLTRLQsrtetqaMAAFRDWL 285 Ochrobactrum anthropi
NP_357520 255 FpvtisLGSYWLTRLQskpqtsaMQAFSDWL 285 Agrobacterium tumefaciens str. C58
YP_261150 255 FdigivTGSYWLTRLQsraetpaMGAFKAWL 285 Pseudomonas fluorescens Pf-5
ACO76005  255 FspglsTGQYWLVKLQsrqdspaMLVFSQWL 285 Laribacter hongkongensis HLHK9
EDO69407  210 FattldAGGYWLTRLAlkpagdgASAFAAWL 240 Dehalococcoides sp. VS

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