Conserved Protein Domain Family
PBP2_CrgA_like_2

?
cd08471: PBP2_CrgA_like_2 
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold.
This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 2. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. 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
?
PSSM-Id: 176160
View PSSM: cd08471
Aligned: 48 rows
Threshold Bit Score: 240.505
Threshold Setting Gi: 103487832
Created: 13-Oct-2009
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
 
putativeputative
Feature 1:putative dimerization interface [polypeptide binding site]
Evidence:
  • Comment:based on sequence similarity to Neisseria meningitidis CrgA

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                   ##   ## ##  #   # #######                                            
YP_001768458  92 GDLSATAPvVFGRRHLVPIVTDFLVAYPeIAVRLLLiDRSVNLVEDhIDVALRIGPLaDSALVATRVGLVRRVVCASPEY 171 Methylobacteriu...
YP_001022471  92 GLLRLTAPvEFGRRHVAPLVNAFLAAHPaMRIELTLaDRVADLLDEgLDLALRIGRLpDSSMVAVPLGRTRLVVCASPAY 171 Methylibium pet...
ACB13013      92 GRLALTAPvTFGRMHVAPLAASFLKQHPdLSVELLLlDRVVDLLEEgLDVAVRIGTLpDSSLVAVPLGTVRRVCCASPAY 171 Hydrogenophaga ...
YP_931617     92 GRVVVTAPvMFGQQHVAPALTRFVQHYGqMRVELRLhDRVVNLLEEhIDVAVRIGAIeDQSLVAHALGTLRRIVVAAPAY 171 Azoarcus sp. BH72
YP_001479319  90 GLLRITSPvQFGRKHVAPVVMAFLDLYPqMQIEMVLnDRNLDLIDEgLDVAVRIGHLqDSSRVARRLGQVSRVTVASPAY 169 Serratia protea...
YP_001354316  90 GTLKVTAPvVFGRRHVAPIVNSYLDQYPeMRVELITnDRNLDLIEEgIDVGVRIGSLaDTSMVARRVGQVQSVLVASPDY 169 Janthinobacteri...
YP_420634     91 GRLRVTAPvVFGRRHVTPIIVDFLRAYPqISIEAVFsDNNLDLIEEeLDVAVRIGTLaDSTLVARRVGEVESVLVASPGY 170 Magnetospirillu...
YP_617393     92 GQLHLTAPvMFGRLHVLPVVDAMMTKHReLGVRMMLiDRNVRIVEEgIDVAVRIGALaDSGLKAVRIGRVRQMLVASPAY 171 Sphingopyxis al...
YP_273972     92 GLLRVTAPvEFGQRYIAPLVNAFLSEHQdINVELNLnDQIVPLLDErLDLALRIGHLpDSAMVARRIGATRLVSCASPGY 171 Pseudomonas syr...
YP_615142     92 GELSITMPiEFGVRHVIPIALAFIDEYPeVTLNLITsDRLVHMVDEhVDVAIRLGHLpDSALFAVKAGEFRLIACASPAY 171 Sphingopyxis al...
Feature 1                        #                             #####      ##  #                  
YP_001768458 172 LARRGtPAAPeDLAAHDLVTFegf-paTTDWRFrrgatplsipirPRLAVNAAeaAVDAARAGlGVTRVLSYQAADEIRS 250 Methylobacteriu...
YP_001022471 172 LREAGpVAHPsALRGLACIAFap---hGRHWHFqdrgapltqtvsARLVANQVqaASLACTQGlGIARLLHYQVADELAD 248 Methylibium pet...
ACB13013     172 LRRHGtPKEPrDLLKHRCIGFkgh-gaSADWRFqvagrelkvpvrPVFVTNQVeaAMDAGIAGlGCVSLLSYQARTGLES 250 Hydrogenophaga ...
YP_931617    172 LAARGtPQHPrELAAHECIVFng--nsAGWWRFiddghefgmtvdGRLTYNHVapALDACRAGmGLGTFIAYQIADDLHA 249 Azoarcus sp. BH72
YP_001479319 170 LALRGePLEPaQLVDHDTIVGtqr-asLREWRFgpqengdrvrltPRLLLNEVetQLLAARAGkGIARLLSYQVADDLAA 248 Serratia protea...
YP_001354316 170 IERRGePKSI-ADIAHHDVIFtairekAPEWRFrhngreqivaltPRLIVNEIdaVLLAAKAGrGLARVLSYQVADELQA 248 Janthinobacteri...
YP_420634    171 IAAHGlPLAVdELAEHDVIFTsgr-pvLVEWRLieggrernvrltPRLMVNQVeaSLAAARAGlGIARALSYQVVDDLAA 249 Magnetospirillu...
YP_617393    172 LARRGaPHGIaDLKGHDLIGTmgp-rwTSEWQFarerw--rlpapPRLTVNTVdgALAAAEAGlGIANLLSYQLAEAIDA 248 Sphingopyxis al...
YP_273972    172 LRTAPlLDTPkSLPEHACITLas---hGRQWYFrhqgkeliqditPRLVCNQVraASLACIQGlGVTRLIHYQVADELAD 248 Pseudomonas syr...
YP_615142    172 LDRRGaPTSPrELSGHDGIMFgp---lPMFWGYridgedvmctprPRVSVNSAagNLAAVLSGvGVARLFDYQVSEHLQS 248 Sphingopyxis al...
Feature 1                                                  
YP_001768458 251 GALRVLLeaYEPAPLPVSFVHPErgqlplkVRAFLDWAIPRM 292 Methylobacterium sp. 4-46
YP_001022471 249 GRLLRLLpaFEPPDLPIQLVYPHarllsprVRQFIDWAAPRL 290 Methylibium petroleiphilum PM1
ACB13013     251 GALKAVLrgFEVDPLPVNILYRPdrlmstrVRALVDWLIPSL 292 Hydrogenophaga sp. PL2G6
YP_931617    250 GRLLPVLeaFELPPRPVHVAFPHarllptrTRVLVDWLRRDL 291 Azoarcus sp. BH72
YP_001479319 249 GTLVRLLpaFEPLPMPVQLVAQNsqrmplkVRTFWDYAWQEL 290 Serratia proteamaculans 568
YP_001354316 249 GTLLRVLpkLDAPDLPVQLIVPSarlmapkSRAFLDLAIDKL 290 Janthinobacterium sp. Marseille
YP_420634    250 GHLVRVLp-GSGALQPVHLVVPGgrhmaarTRAFLNFATNGL 290 Magnetospirillum magneticum AMB-1
YP_617393    249 GRLIALLeqEQPPALPVHLLFEPsraalpaVRLFVEAMQARM 290 Sphingopyxis alaskensis RB2256
YP_273972    249 GRLIRVLnnFETADLPIQLVYPHalqlsprVKAFVEWAIPQL 290 Pseudomonas syringae pv. phaseolicola 1448A
YP_615142    249 GALVRILpdADGEPRPVHIVYPRqgllplkVRAFIDWASPRL 290 Sphingopyxis alaskensis RB2256

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap