Conserved Protein Domain Family
PBP2_LTTR_beta_lactamase

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cd08484: PBP2_LTTR_beta_lactamase 
The C-terminal substrate-domain of LysR-type transcriptional regulators for beta-lactamase genes, contains the type 2 periplasmic binding fold.
This CD includes the C-terminal substrate binding domain of LysR-type transcriptional regulators, BlaA and AmpR, that are involved in control of the expression of beta-lactamase genes. Beta-lactamases are responsible for bacterial resistance to beta-lactam antibiotics such as penicillins. BlaA (a constitutive class A penicillinase) belongs to the LysR family of transcriptional regulators, while BlaB (an inducible class C cephalosporinase or AmpC) can be referred to as a penicillin-binding protein, but it does not act as a beta-lactamase. AmpR regulates the expression of beta-lactamases in many enterobacterial strains and many other gram-negative bacilli. In contrast to BlaA, AmpR acts an activator only in the presence of the beta-lactam inducer. In the absence of the inducer, AmpR acts as a repressor. The 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: 176173
View PSSM: cd08484
Aligned: 11 rows
Threshold Bit Score: 335.88
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 an...
P14145        95 VLKVGVNTTFAMCWLMPRLEAFRQAHPqIDLRISTnnnrVEILREGLDMAIRFGtggwtgHDAIPLAEAPMAPLCAPgla 174 Rhodobacter cap...
BAA07083      94 VVSIAAVGTFAVGWLLPRLAEFRQLYPrIEVNLRTnnnvVNLATEGLDFAIRFGeglwplTHNKALFSAPLTVLCSSgta 173 Proteus vulgaris
P52660        94 VVSIAAVGTFAVGWLLPRLAEFRQLYPrIELNLRTnnnvVNLATEGLDFAIRFGeglwplTHNKALFSAPLTVLCSSdta 173 Proteus vulgaris
NP_357520     95 LLFLGVVGTFAVGWLLPRLAAFQKRHPfIDVRVSTnnnrVDMAAEGLDFAIRFGqgswhgTDAFRLFEAPLSPLCTPkla 174 Agrobacterium t...
YP_261150     95 VLTVGAVGTFAVGWLLPRLEDFQARHPyVDLRLSTnnnrVDVAAEGLDYAIRFGtgawhgIEALALLQAPLSVLCVPela 174 Pseudomonas flu...
YP_001887764  94 VLTVGVVGTFAVGWLMPRLKSFRDAHPfVELRLLTnnnlVDLATEGLDFAIRFGdgtwpgSLATRLLDAPLALLCTPeia 173 Burkholderia ph...
ACO76005      95 PLHVGVVGTFATGWLLPRLPGFVNSHPrIDLRLSThnnrVDIAAEGLDYAVKFGsgawqdLDATPLFEAPLSPLCTPela 174 Laribacter hong...
EDO69407      51 VVHVGAVGTFACGWLLPRLAEFARLHPsVDVRLSThnnrVDPAAEGLDYAVRFGrgtwpgMESRFLMGAPLAPLCTPaia 130 Dehalococcoides...
YP_001117863  97 VLTLGAVGTFAIGWLMPRLKRFGETHPfVELRLRTnnnvVDLAGEGLDFAIRFGegnwpaTRNERLLDAPLSALCAPdia 176 Burkholderia vi...
ZP_01545113   95 VLTVGAVATFATGWLLPRLAGFAKVHPqIDLRLKTnnnrADILADGLDCFLRFGdgawhaTNAEKLMDAPLSPICSPeaa 174 Labrenzia aggre...
Feature 1                                                    ###                   #             
CAC04521     175 relrtPVDLARHTLLRSYRADEWTQWFvaagvtgdmplprSIMFDSSLAMMEAAMQgaGIALAPplMFSRQLLSETIVQP 254 Ochrobactrum an...
P14145       175 srllhPSDLGQVTLLRSYRSAEWPGWFeaagvp--cppvtGPVFDSSVALAELATSgaGVALLPisMFESYIAQGRLAQP 252 Rhodobacter cap...
BAA07083     174 krlqhPTDLINENLYRSYREDEWLQWFekanms--pikitGSIFDSSRLMIESAIYegGVALAPakMFSREIENGQLVQP 251 Proteus vulgaris
P52660       174 kplqhPTDLINETLYRSYREDEWLQWFekanms--pikitGSIFDPSRLMIESAIYegGVALAPakMFSREIENGQLVQP 251 Proteus vulgaris
NP_357520    175 emlkePADLMDATLLRSYRADEWSTWFaaagvspaaqvnaGIVFDTSLGMMEAALQglGVALAPpsMFSRHLTSGAVMQP 254 Agrobacterium t...
YP_261150    175 rqlhsPADLLGQTLLRSYRTDEWPQWFqaaglgansllpqSVVFDSSLGMLEAALQglGVALAPplMFQRQLASGAVVQP 254 Pseudomonas flu...
YP_001887764 174 erltkPEDLAGETLLRSYRTDDWMSWFsaagip--prpirGPVFDSSRLMVEAAMQgaGIALAPalMFDHEINTGRLVRP 251 Burkholderia ph...
ACO76005     175 rtlsqPADVLAHTLLRSYRADEWPQWLreagvghpvfirnSIMFDSSIGMIEAARQgaGIALAPpaMFTRALARGELVQP 254 Laribacter hong...
EDO69407     131 qqlrePAELARFALLRSYFVDDWRLWFeaaqav-pcgpinGTIFDSSLTMVQCALQnlGVALAPpsMFAREIAQGLLVQP 209 Dehalococcoides...
YP_001117863 177 rrlsrPADLTNETLLRSYRTDEWLGWFdaaqve--pwtvnGPVFDSSRLMVEAAMQgaGIALAPacMFARELQLGMLARP 254 Burkholderia vi...
ZP_01545113  175 prlsePADLVNEPLLRSYRMDEWAMWFqaaslp--pprarGWMFDSSLAMVEAVTQgaGVALVPtsMFSRQLSSGAIVQP 252 Labrenzia aggre...
Feature 1                                       
CAC04521     255 FettvtMGSYWLTRLQsrtetqaMAAFRDWL 285 Ochrobactrum anthropi
P14145       253 FgvtvsVGRYYLAWPSdrpatsaMSTFSRWL 283 Rhodobacter capsulatus
BAA07083     252 FkieveMGKYWLTYLKskpmtasMEIFQQWL 282 Proteus vulgaris
P52660       252 FkieveLGKYWLTYLKskpmtasMEIFQQWL 282 Proteus vulgaris
NP_357520    255 FpvtisLGSYWLTRLQskpqtsaMQAFSDWL 285 Agrobacterium tumefaciens str. C58
YP_261150    255 FdigivTGSYWLTRLQsraetpaMGAFKAWL 285 Pseudomonas fluorescens Pf-5
YP_001887764 252 FdvevhAGSYWLTWLKgkpmtpaMLLFNQWI 282 Burkholderia phytofirmans PsJN
ACO76005     255 FspglsTGQYWLVKLQsrqdspaMLVFSQWL 285 Laribacter hongkongensis HLHK9
EDO69407     210 FattldAGGYWLTRLAlkpagdgASAFAAWL 240 Dehalococcoides sp. VS
YP_001117863 255 LdidvrGGAYWLTSLKskpltpaMQLFRDWI 285 Burkholderia vietnamiensis G4
ZP_01545113  253 FktsvlTGSYWLTWLKsreetsaMRKFRQWM 283 Labrenzia aggregata IAM 12614

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