Conserved Protein Domain Family
PBP2_LTTR_like_2

?
cd08427: PBP2_LTTR_like_2 
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold.
LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. 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
?
PSSM-Id: 176118
View PSSM: cd08427
Aligned: 29 rows
Threshold Bit Score: 207.427
Threshold Setting Gi: 159046721
Created: 7-Oct-2009
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
 
putative
Feature 1:putative dimerization interface [polypeptide binding site]
Evidence:
  • Comment:based on sequence similarity to the known structures of LysR-type transcriptional regulators.
  • Comment:Most members of the LysR family of transcriptional regulators are tetrameric, while CrgA assembles into octameric rings

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                       ## ##  #   # #######                                             
NP_886148     89 LLRVGAIasvqqDLLVRALAALRAEHPdVRVRIVPGvsltLLGHVDAGeVDLAVLIRPpfalppeLEWQPLLRePMVLAV 168 Bordetella para...
YP_002137134  91 LLTLGAVptvitGSLPPALGRLRTRYQdMQVKLVSGlsteLVRKVEEGdLDAALTTEPpyavppqYEWIPYDEePFFVVA 170 Geobacter bemid...
YP_001900321  92 AVAIGAVvs-vmGSLAHAVAGLKQAHKgLDVKLITGksgeLVEQVEAGeLDGALVVEHlerlpanLVWHPLYTePLVVVA 170 Ralstonia picke...
YP_001629001 118 SLRIGTLvsslmGTFGTVLARVKHDYPdLHITLLAGqsadFAARVAAGeLDAAVVTEPphgvepaLVWAPLYQePLVLIA 197 Bordetella petr...
YP_998354     90 LLSLGVInsawtGVLPRLLKKITAGHPnLEIKVTAGisgdLVAKVDAGiVDAAIVTQPprhfsthLVAHHLYAePFVLIA 169 Verminephrobact...
YP_002501893  91 RLRLGAVqtalsGVLPEALAALNQSHPrVRVHVSAGmsaeLALRIAAGeLDAAVTTEPvrphppdLVWTPLYEdRFWLIA 170 Methylobacteriu...
NP_519215    103 RLRIGAIqtalsGPLPDALLALRRDHPlLRVHVAAGmsaeLAQRVAAGeLDAAITSQPvrphpaeLTWTTLYEdRFWLLA 182 Ralstonia solan...
YP_002947469  90 LLKLGSVhtvasGVLPLALRHLQRQGHgLEVHVTTGlthdLERAVYHRqLDVALVTEPelp-rsgLDFLPFVDeALVVIA 168 Variovorax para...
YP_917182    180 KFVIGSVrtsaiGLLPQAVSRVVANHPgLKIRLLVGnsenLVQDVYAGrLDAAIIAENsls-srdLDWSPFIRePLFLIA 258 Paracoccus deni...
YP_001542389  90 VLKLGAIrtvsmRLVPEALRGMRGRYPdLGFEMTVGmserLMADVAAGrLDAALVAEHvgv-patLSWSPVLNePLVIIA 168 Dinoroseobacter...
Feature 1                                                    ######     ## ##                    
NP_886148    169 PeaapeaPWRELLagqPFIRYdRASFGGRLVDMFLkrhrldvreAIELDEidaIANLVRHGlGVALLPhtrh---ldarG 245 Bordetella para...
YP_002137134 171 PkeaginDVALLFerfPFVRFdKMAWAGAMVDHELmlqgirpreVMEFDSlemALALVEEGlGIAVVPlsksrleqvanH 250 Geobacter bemid...
YP_001900321 171 Grht-rgRAEEVLrthPFLRFdRAVRTGALIDRALrkthmavneFIEVNSieaIVELVRQQvGVTLVPrlrraswesdpA 249 Ralstonia picke...
YP_001629001 198 AarlrhkSVASLLatePFLQFdRSLWTGHLITEALsrhgaapntILELNSieaIAELVRQDyGVAVVPllananwraskQ 277 Bordetella petr...
YP_998354    170 PaqmefsDLATSMgaaPYVAFdRSAWAGQLIDEYLgarglrvrpAMEVNSldaIIAVVSHGlGVSIVPlilganwhtspA 249 Verminephrobact...
YP_002501893 171 PpghdarSPRELLselPFIRFdSHAWAGRVIDRELrrmrldvreEMVLDSlevILRMVEKGlGVAVVPlsddv--latlR 248 Methylobacteriu...
NP_519215    183 PpqhanhDARKLLeelPFIRFdAQAWAGRMIAAELrrlgvrvreEMVLDSqeaIVRMVASGlGAAIVAlsdav-lahlpP 261 Ralstonia solan...
YP_002947469 169 HksakgaSDQEVLegtPYVRFnRSARVGNLVQEEIvrrqitvrsTMEIDNlegVIAMVANGlGASVVPargvk-nefpsT 247 Variovorax para...
YP_917182    259 PpgtpvvDVRQALsafPFVRFrSNVPLARLIETELgrmnlplndIAEMDTisaVTACVENGlGVSIVPriaai--ergvD 336 Paracoccus deni...
YP_001542389 169 PpqeawrSEVSLLrdlPFIRYaTDVPLARQIETELsglsivpreVAVANTmpaVVGLVQAGlGVAVVPriatl--hggpA 246 Dinoroseobacter...
Feature 1                                             
NP_886148    246 LRLLelddqvrfAREIGLIVRQplgqsplAQRLAQCL 282 Bordetella parapertussis 12822
YP_002137134 251 FTLTpfgt-pqlSRRVGMYQKRqhprqplTRAVLDEL 286 Geobacter bemidjiensis Bem
YP_001900321 250 LRVLplpp-qtpVRTVGMIERKehvrhgvIQAVLDAL 285 Ralstonia pickettii 12J
YP_001629001 278 LAVKplpg-paiMRRVGMLERRrhgkqaiTQTLRGVF 313 Bordetella petrii DSM 12804
YP_998354    250 LRIVrls---gfDRPVSLIERRqhlrsalTATVLASF 283 Verminephrobacter eiseniae EF01-2
YP_002501893 249 LTTLpfge-pqlIRRIVLLERQdctggrlSAALAQAV 284 Methylobacterium nodulans ORS 2060
NP_519215    262 LVRLpfgq-pqlRRAVVLLEHAsrpaqrfAQALTDAV 297 Ralstonia solanacearum GMI1000
YP_002947469 248 VRVIpfgn-ptvTRRLGMLAPKenprshlCQLLLEAL 283 Variovorax paradoxus S110
YP_917182    337 LVMLpfgd-ppvFRQIGLLQRPkgpraglIAELHEQL 372 Paracoccus denitrificans PD1222
YP_001542389 247 LHCRpfrd-gaiTRRVGLVQRQvssrsrvLTELREIL 282 Dinoroseobacter shibae DFL 12

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