Conserved Protein Domain Family
PBP2_AlsR

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cd08452: PBP2_AlsR 
The C-terminal substrate binding domain of LysR-type trnascriptional regulator AlsR, which regulates acetoin formation under stationary phase growth conditions; contains the type 2 periplasmic binding fold.
AlsR is responsible for activating the expression of the acetoin operon (alsSD) in response to inducing signals such as glucose and acetate. Like many other LysR family proteins, AlsR is transcribed divergently from the alsSD operon. The alsS gene encodes acetolactate synthase, an enzyme involved in the production of acetoin in cells of stationary-phase. AlsS catalyzes the conversion of two pyruvate molecules to acetolactate and carbon dioxide. Acetolactate is then converted to acetoin at low pH by acetolactate decarboxylase which encoded by the alsD gene. Acetoin is an important physiological metabolite excreted by many microorganisms grown on glucose or other fermentable carbon sources. 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: 176143
View PSSM: cd08452
Aligned: 5 rows
Threshold Bit Score: 328.692
Threshold Setting Gi: 150378253
Created: 26-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 sequeuce similarity to CatM from Acinetobacter baylyi ADP1

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                    #                                                #                        
Q04778              92 LLVIGFVGsatYEFLPPIVREYRKKFPsVKIELREisssrQQEELLKGnIDIGILHPplqhtaLHIETAQSsPCVLALPK 171 Bacillus ...
CAB07788            92 LLVIGFVGsatYEFLPPIVREYRKKFPsVKIELREisssrQQEELLKGnIDIGILHPplqhtaLHIETAQSsPCVLALPK 171 Bacillus ...
goetting:RBAM33180  92 RLVVGFVGsatYEFLPPIIREFREKFPsVKLDLREissfrQQEELLKGnIDIGILHPplqhsaLHMEKVQSsPCILALPK 171 Bacillus ...
NP_979999           92 SLSIGFVGaaiYDILPSIVREYRKKFPrVSVALHElstpdQVYALHDNrIDIGFLRPpiptqlLELEPIQKlSCTLCLPK 171 Bacillus ...
YP_001314848        92 HLAVGFIDaaiYSLVPNVVECFTRSYPhVTVELADlripdQVRGVSEGrLDVGFIHPpirgeqLAIETVLVePLVVAVPQ 171 Sinorhizo...
Feature 1                                    ##      #                                                 
Q04778             172 QHPLtskesitiedLRDEPIITVAkeawPTLYMDFIQFCeqaGFRPNIVQEATEyqMVIGLVSAGiGMTFVPSSakklfn 251 Bacillus ...
CAB07788           172 QHPLtskesitiedLRDEPIITVAkeawPTLYMDFIQFCeqaGFRPNIVQEATEyqMVIGLVSAGiGMTFVPSSakklfn 251 Bacillus ...
goetting:RBAM33180 172 QHPLtakqtidiqdLKNEPIITLSketwPTLYLEFVNYCeqaGFKPKIVQEATEyqMVIGLVSAGiGVTFVPSSakklfn 251 Bacillus ...
NP_979999          172 AHPLaekdeihiedLRDEPFVFITrpvwPALYDTILSLCrdvGFSPRIVQEATEyqTVMGLVAAGiGITVIPVSanklyk 251 Bacillus ...
YP_001314848       172 RHRLasraeiplaeLANEALIQFPrsinPTLYDEIIGLCqssGFNPKIVREATPkqTIIGLVSVGlGVSLLPRClenlkr 251 Sinorhizo...
Feature 1                                                   
Q04778             252 lDVTYRKMDqiqlNAEWVIAYRKdnhnplIKHFIHIS 288 Bacillus subtilis subsp. subtilis str. SMY
CAB07788           252 lDVTYRKMDqiqlNAEWVIAYRKdnhnplIKHFIHIS 288 Bacillus subtilis subsp. subtilis str. 168
goetting:RBAM33180 252 lEVAYRGINqvqlTAEWVIAYRKdnqnpiLKHFLDIM 288 Bacillus amyloliquefaciens FZB42
NP_979999          252 tEVVYKELYdsnfVAEMSVAYKKmnsnpeLLEFLKIA 288 Bacillus cereus ATCC 10987
YP_001314848       252 dGVAYRPISgpnlSIDTSIIYRSdrlrpaTKAFINVV 288 Sinorhizobium medicae WSM419

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