PR00909

SPERMDNBNDNG

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameSPERMDNBNDNG

Description
Imported from IPR001188

Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. The protein components of these traffic systems include one or two transmembrane protein components, one or two membrane-associated ATP-binding proteins and a high affinity periplasmic solute-binding protein. In Gram-positive bacteria, which are surrounded by a single membrane and therefore have no periplasmic region, the equivalent proteins are bound to the membrane via an N-terminal lipid anchor. These homologue proteins do not play an integral role in the transport process per se, but probably serve as receptors to trigger or initiate translocation of the solute through the membrane by binding to external sites of the integral membrane proteins of the efflux system. In addition at least some solute-binding proteins function in the initiation of sensory transduction pathways.

The bacterial Spermidine/putrescine-binding periplasmic protein (PotD) is involved in the polyamine transport system. It is required for the activity of the bacterial periplasmic transport system of putrescine and spermidine
[1, 2]
. This protein has two domains connected through two β-strands, which form a hinge at the bottom of the central cleft, and this hinge lies and one short peptide segment
[5]
.

Similar proteins with specificities for putrecine and spermidine are also included in this family, such as Putrescine-binding periplasmic protein PotF from Escherichia coli, more specifically involved in putrescine uptake
[4, 6, 3]
and Spermidine-binding periplasmic protein SpuE from Pseudomonas aeruginosa
[8]
respectively.

Putrescine/cadaverine-binding protein and Putrescine/agmatine-binding protein from P. aeruginosa also belong to this entry
[7]
.

References
Imported from IPR001188

1.Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K. J. Biol. Chem. 266, 20928-33, (1991). View articlePMID: 1939142

2.Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. Pistocchi R, Kashiwagi K, Miyamoto S, Nukui E, Sadakata Y, Kobayashi H, Igarashi K. J. Biol. Chem. 268, 146-52, (1993). View articlePMID: 8416922

3.A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF. Kroger P, Shanmugaratnam S, Ferruz N, Schweimer K, Hocker B. Structure 29, 433-443.e4, (2021). PMID: 33406388

4.Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity. Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K. J. Biol. Chem. 273, 17604-9, (1998). View articlePMID: 9651355

5.The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Sugiyama S, Matsuo Y, Maenaka K, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K. Protein Sci. 5, 1984-90, (1996). View articlePMID: 8897598

6.Properties of putrescine uptake by PotFGHI and PuuP and their physiological significance in Escherichia coli. Terui Y, Saroj SD, Sakamoto A, Yoshida T, Higashi K, Kurihara S, Suzuki H, Toida T, Kashiwagi K, Igarashi K. Amino Acids 46, 661-70, (2014). PMID: 23719730

7.Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins. Fernandez M, Rico-Jimenez M, Ortega A, Daddaoua A, Garcia Garcia AI, Martin-Mora D, Torres NM, Tajuelo A, Matilla MA, Krell T. Int J Mol Sci 20, (2019). PMID: 31627455

8.Structural basis of substrate binding specificity revealed by the crystal structures of polyamine receptors SpuD and SpuE from Pseudomonas aeruginosa. Wu D, Lim SC, Dong Y, Wu J, Tao F, Zhou L, Zhang LH, Song H. J. Mol. Biol. 416, 697-712, (2012). View articlePMID: 22300763

Supplementary References

1. Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K. J. Biol. Chem. 271, 9519-25, (1996). View articlePMID: 8621624

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