1IXH,1TWY,1PC3


Conserved Protein Domain Family
PBP2_phosphate_binding

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cd01006: PBP2_phosphate_binding 
Click on image for an interactive view with Cn3D
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily.
This phosphate-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 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: 270227
Aligned: 3 rows
Threshold Bit Score: 307.651
Created: 1-Nov-2000
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
chemical
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:chemical substrate binding site [chemical binding site]
Evidence:
  • Structure:1IXH; Escherichia coli phosphate-binding protein (Pbp) complexed with phosphate, contacts at 4A.
  • Citation:PMID 9228942
  • Structure:1TWY; Vibrio cholera phosphate-binding protein (Pbp) complexed with phosphate, contacts at 4A.
  • Structure:1PC3; Mycobacterium tuberculosis ABC phosphate transport receptor complexed with phosphate, contacts at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             #                                               #                       
1IXH_A      1 EASLTGAGAtfpaPVYAKWADTYQKet-gNKVNYQGigsSGGVKQIIANTvDFGASDaPLSDEKLaq-egLFQFPTViGG 78  Escherichia coli
1TWY_A     27 ASEITISGStsvaRIXDVLAEKYNQqhpeTYVAVQGvgsTAGISLLKKGVaDIAXTSrYLTESEAqn--tLHTFTLAfDG 104 Vibrio cholerae O1...
1PC3_A     26 PVTLAETGStllyPLFNLWGPAFHErypnVTITAQGtgsGAGIAQAAAGTvNIGASDaYLSEGDMaahkgLMNIALAiSA 105 Mycobacterium tube...
Feature 1                                                             #   ####                
1IXH_A     79 VVLAVNIPGlksgelvldgktlgDIYLGKIKKWDDEaiaklnpglklPSQNIAVVRRADGSGTSFVFTSYLakvneewkn 158 Escherichia coli
1TWY_A    105 LAIVVNQANpvtnlt---reqlyGIYKGQITNWKQVg---------gNDQKIAVVTREASSGTRYSFESLXgltktvkd- 171 Vibrio cholerae O1...
1PC3_A    106 QQVNYNLPGvsehlkl-ngkvlaAMYQGTIKTWDDPqiaalnpgvnlPGTAVVPLHRSDGSGDTFLFTQYLskqdpegwg 184 Mycobacterium tube...
Feature 1                           #                                                         
1IXH_A    159 n----vgtgstvkwPIGLGGkGNDGIAAFVQRLpGAIGYVEYAYAKQNn---LAYTKLisadgkpvspteenfanaak-- 229 Escherichia coli
1TWY_A    172 -------revsdvaPTALVVnSNSXXKTLVNHNtQAVGFISIGSVDKS----VKAIQFekadpts--------------- 225 Vibrio cholerae O1...
1PC3_A    185 kspgfgttvdfpavPGALGEnGNGGMVTGCAETpGCVAYIGISFLDQAsqrgLGEAQLgnssgnfllpdaqsiqaaaagf 264 Mycobacterium tube...
Feature 1                                                                      
1IXH_A    230 gadwsktfaqdltnqkgedaWPITSTTFILIHKDqkkpeqgTEVLKFFDWAYKtg--aKQANDLD 292 Escherichia coli
1TWY_A    226 -------------dniakhtYQLSRPFLILHYSDna----dEQTKEFIAFLKSes-akKLIVEYG 272 Vibrio cholerae O1 biovar eltor
1PC3_A    265 asktpanqaismidgpapdgYPIINYEYAIVNNRqkdaataQTLQAFLHWAITdgnkaSFLDQVH 329 Mycobacterium tuberculosis

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