Conserved Protein Domain Family
PBP2_BlaA

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cd08487: PBP2_BlaA 
The C-terminal substrate-binding domain of LysR-type trnascriptional regulator BlaA which involved in control of the beta-lactamase gene expression; contains the type 2 periplasmic binding fold.
This CD represents the C-terminal substrate binding domain of LysR-type transcriptional regulator, BlaA, that involved in control of the expression of beta-lactamase genes, blaA and blaB. Beta-lactamases are responsible for bacterial resistance to beta-lactam antibiotics such as penicillins. The blaA gene is located just upstream of blaB in the opposite direction and regulates the expression of the blaB. BlaA also negatively auto-regulates the expression of its own gene, blaA. BlaA (a constitutive class A penicllinase) belongs to the LysR family of transcriptional regulators, whereas 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. 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: 176176
View PSSM: cd08487
Aligned: 5 rows
Threshold Bit Score: 351.847
Threshold Setting Gi: 118587703
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              ## #                                                                      
P52660        94 VVSIAAVGTFAVGWLLPRLAEFRQLYPrIELNLRTnnnvVNLATEGLDFAIRFGEGLWplTHNKALFSAPLTVLCSSdta 173 Proteus vulgaris
BAA07083      94 VVSIAAVGTFAVGWLLPRLAEFRQLYPrIEVNLRTnnnvVNLATEGLDFAIRFGEGLWplTHNKALFSAPLTVLCSSgta 173 Proteus vulgaris
YP_001117863  97 VLTLGAVGTFAIGWLMPRLKRFGETHPfVELRLRTnnnvVDLAGEGLDFAIRFGEGNWpaTRNERLLDAPLSALCAPdia 176 Burkholderia vi...
ZP_01545113   95 VLTVGAVATFATGWLLPRLAGFAKVHPqIDLRLKTnnnrADILADGLDCFLRFGDGAWhaTNAEKLMDAPLSPICSPeaa 174 Labrenzia aggre...
YP_001887764  94 VLTVGVVGTFAVGWLMPRLKSFRDAHPfVELRLLTnnnlVDLATEGLDFAIRFGDGTWpgSLATRLLDAPLALLCTPeia 173 Burkholderia ph...
Feature 1                                                  ###                   #               
P52660       174 kplqhPTDLINETLYRSYREDEWLQWFekanmspikitGSIFDPSRLMIESAIYegGVALAPakMFSREIENGQLVQPFk 253 Proteus vulgaris
BAA07083     174 krlqhPTDLINENLYRSYREDEWLQWFekanmspikitGSIFDSSRLMIESAIYegGVALAPakMFSREIENGQLVQPFk 253 Proteus vulgaris
YP_001117863 177 rrlsrPADLTNETLLRSYRTDEWLGWFdaaqvepwtvnGPVFDSSRLMVEAAMQgaGIALAPacMFARELQLGMLARPLd 256 Burkholderia vi...
ZP_01545113  175 prlsePADLVNEPLLRSYRMDEWAMWFqaaslppprarGWMFDSSLAMVEAVTQgaGVALVPtsMFSRQLSSGAIVQPFk 254 Labrenzia aggre...
YP_001887764 174 erltkPEDLAGETLLRSYRTDDWMSWFsaagipprpirGPVFDSSRLMVEAAMQgaGIALAPalMFDHEINTGRLVRPFd 253 Burkholderia ph...
Feature 1                                     
P52660       254 ieveLGKYWLTYLKskpmtasMEIFQQWL 282 Proteus vulgaris
BAA07083     254 ieveMGKYWLTYLKskpmtasMEIFQQWL 282 Proteus vulgaris
YP_001117863 257 idvrGGAYWLTSLKskpltpaMQLFRDWI 285 Burkholderia vietnamiensis G4
ZP_01545113  255 tsvlTGSYWLTWLKsreetsaMRKFRQWM 283 Labrenzia aggregata IAM 12614
YP_001887764 254 vevhAGSYWLTWLKgkpmtpaMLLFNQWI 282 Burkholderia phytofirmans PsJN

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