2R6G,3DHW,3DHW,2R6G,2ONK,2ONK,3D31,3D31


Conserved Protein Domain Family
TM_PBP2

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cd06261: TM_PBP2 
Click on image for an interactive view with Cn3D
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Statistics
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PSSM-Id: 119394
View PSSM: cd06261
Aligned: 252 rows
Threshold Bit Score: 33.0209
Threshold Setting Gi: 81780698
Created: 8-Jan-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:putative PBP binding loops
Evidence:
  • Structure:2R6G_E/F/G; Escherichia coli maltose transporter, interface of the TMs (MalG and MalF) with maltose binding protein, contacts at 3.5 A.
    View structure with Cn3D
  • Structure:2ONK_C/D/E; Archaeoglobus fulgidus ModBC, interface of ModB TMs with (ModA) PBP subunits, contacts at 3.5 A.
    View structure with Cn3D
  • Comment: the highlights delimit the borders of two regions involved in PBP binding which includes three loops.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                 #                     
2R6G_F      281 FVWTVVFSLITVFLTVAVGMVLACLVQWealr--gkavYRVLLILPYAVPSFISILIFKglfnqsfgeinmmlsalfgvk 358
gi 2501387   70 LLVSFVVSIGSLIIASYIGVRTSIFLVYrckpr-irkkLLLVIDILSGIPSVIFGLFATqilssifrd------------ 136
gi 1709881   70 LLVSFIVSIGALIIASYIGVRTSFFLVYrckpk-irkkLSLIIDILSGIPSVIFGLFASqilsiffrd------------ 136
gi 131443    83 LAGSGLLILWATVFGTPLGIMAGIYLAEygrkswlaevIRFINDILLSAPSIVVGLFVYtivvaq--------------- 147
gi 20139814  71 FFGSAIMCLLAIVIGTPLGIAAGTWLAEygntsktsavVRFVNDILLSAPSIVLGLFVYtlyvmht-------------- 136
gi 20139438  85 LYGSLVQAVVAAIMAVPLGSMTAVYLVEygsgp-fvrvTTFMVDVLAGVPSIVAALFIFclwiatl-------------- 149
gi 47606718  89 LYGTLVQAGVAAVLAVPLGLMTAVYLVEygtgr-msrvTTFTVDVLAGVPSIVAALFVFslwiatl-------------- 153
gi 3024475   68 IVGTLMLTFLATLIGLPLAFLAGAYAYEfpnsf-igraTKMLLQIMLEFPTILVGTFVMgmlvvp--------------- 131
gi 61230172  83 IIGTAVLAIGVILVGGTVSVLTGIYLSEfatgk-trsiLRGAYEVLSGIPSIVLGYVGYlalvvyf-------------- 147
gi 2501387  413 LVNTLVIILVAIGITFPIALLIAIWLNEytksriakntFSFVIDSLSSMPSIIYGLFGLsfflrtlqls----------- 481
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                    #                                                                  
2R6G_F      359 pawfsdpttaRTMLIIVNTWLgYPYMMILCMGLLKAIpDDLYEASAMDGAGPfqNFFKItLPLLIKPLTPLMIASFAFNF 438
gi 2501387  137 -vlhlpplslLNVIVMLSFMI-IPIVISLTTNALLHVeSSLMTVAISLGENKtsVIYKViKKEIKAQLVVILVLAFGRAI 214
gi 1709881  137 -ilklpplslLNVIAMLSFMI-IPIVISLTTNTLTYVnNDLISVVVSLGENKtsAIYKIiKKEIKPQLTVILTLAFARAI 214
gi 131443   148 ----mehfsgWAGVIALALLQ-VPIVIRTTENMLKLVpYSLREAAYALGTPKwkMISAItLKASVSGIMTGILLAIARIA 222
gi 20139814 137 ----gghfsaFSGALALVFIV-LPIVVRTTDEMLRLVpGQMREAALSLGIPQwkMIIQVlYRSASAGILTGILLALARIS 211
gi 20139438 150 ----gfqqsaFAVSLALVLLM-LPVVVRSTEEILRLVpDELREACYALGIPKwkTIVRIvFPIATPGIISGVLLSIARVI 224
gi 47606718 154 ----gfqqsaFAVALALVLLM-LPVVVRAGEEMLRLVpDELREASYALGVPKwkTIVRIvAPIAMPGIVSGILLSIARVV 228
gi 3024475  132 ----mgtfsaLAGALALALIL-TPYVAVYTEEAMAEVpKIYKEGGYALGCTRaqVIFKViTKMAKKGILTGILIGMAKVA 206
gi 61230172 148 ----dwgfslAAGVLVLSVMS-IPYIAKATESALAQVpTSYREAAEALGLPAgwALRKIvLKTAMPGIVTGMLVALALAI 222
gi 2501387  482 -aggangtslMAGILTISVVV-LPFLIRTCQEALNNVsWDLRVSAYALGVSKreVIWKIvLPGALKGLIIALILTINRII 559
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
Feature 1             #                         #  #                    #                
2R6G_F      439 NNFVLIQLltnggpdrlgt--ttpagytdllvNYTYRIafeg----------gggqDFGLAAAIATLIFLLVG 499
gi 2501387  215 SETMAVNFilqsvnyqevi--andrfftsdlkTLGSVIstfifsengdeqvsgvlyTFGIIIFVLISFLNFFA 285
gi 1709881  215 SETMAVNFvlqsvnyqevi--nnnrfftsdlkTLGSVIstfifsengdeqingvlyIFGIIILILVSLLNFFA 285
gi 131443   223 GETAPLLFtalsnqfwstd---mmqpianlpvTIFKFAmspfae-------wqqlaWAGVLIITLCVLLLNIL 285
gi 20139814 212 GETAPLLFtafgnqywssn---ifqpiaslplVMNQFAsspyks-------wqllaWSGALVLTVFVLLVSLG 274
gi 20139438 225 GETAPVLVlvgysrsinfd---ifdgnmaslpLLIYTEltnpey-------agflrVWGAALTLIILVAGINL 287
gi 47606718 229 GETAPVLVlvgyshsinld---vfhgnmaslpLLIYTEltnpeh-------agflrVWGAALTLIIVVATINL 291
gi 3024475  207 GETAPLLFtagglyevypt---nplepvgaipLLIYTLvqspsi-------edhqmAWGAALVMLIIFLAIFV 269
gi 61230172 223 GETAPLLYtagwsnspptgqltdspvgyltypIWTFYNqpsksa------qdlsydAALLLIVFLLLLIFIGR 289
gi 2501387  560 AETAPFFItaglassnlf----dlslpgqtltTRIYGQlfstnst-----avdvmlETALVSIVFLMFLIFLS 623

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