Protein Domain : IPR017666

Type:  Family Name:  2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT2
Description:  ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs.ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations. Some eukaryotic exporters encode the four domains on the same polypeptide chain [].The ABC module (approximately two hundred amino acid residues) is known to bind and hydrolyse ATP, thereby coupling transport to ATP hydrolysis in a large number of biological processes. The cassette is duplicated in several subfamilies. Its primary sequence is highly conserved, displaying a typical phosphate-binding loop: Walker A, and a magnesium binding site: Walker B. Besides these two regions, three other conserved motifs are present in the ABC cassette: the switch region which contains a histidine loop, postulated to polarise the attaching water molecule for hydrolysis, the signature conserved motif (LSGGQ) specific to the ABC transporter, and the Q-motif (between Walker A and the signature), which interacts with the gamma phosphate through a water bond. The Walker A, Walker B, Q-loop and switch region form the nucleotide binding site [, , ].The 3D structure of a monomeric ABC module adopts a stubby L-shape with two distinct arms. ArmI (mainly beta-strand) contains Walker A and Walker B. The important residues for ATP hydrolysis and/or binding are located in the P-loop. The ATP-binding pocket is located at the extremity of armI. The perpendicular armII contains mostly the alpha helical subdomain with the signature motif. It only seems to be required for structural integrity of the ABC module. ArmII is in direct contact with the TMD. The hinge between armI and armII contains both the histidine loop and the Q-loop, making contact with the gamma phosphate of the ATP molecule. ATP hydrolysis leads to a conformational change that could facilitate ADP release. In the dimer the two ABC cassettes contact each other through hydrophobic interactions at the antiparallel beta-sheet of armI by a two-fold axis [, , , , , ].The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions []. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [, ]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [, , ]; (for further information see http://www.tcdb.org/tcdb/index.php?tc=3.A.1).The enzyme phosphonatase catalyses the degradation of 2-aminoethylphosphonate (AEP) in bacteria. This allows them to metabolise a range of organophosphonate compounds, including 2-aminoethylphosphonate, as a sole source of carbon, energy and phosphorus for growth []. The C-P bond in phosphonoacetaldehyde (Pald) is hydrolysed and a bi-covalent Lys53ethylenamine/Asp12 aspartylphosphate intermediate is formed []. This step can also be catalysed by C-P lyase [], with some bacteria having the genes for both pathways and some only for one of them. The 2-aminoethylphosphonate ABC transport system functions in the transport of 2-aminoethylphosphonate across the membrane for utilisation in the bacterial cell.This entry represents the ATP-binding component PhnT2 of the 2-aminoethylphosphonate ABC transport system. Short Name:  AminoethylPonate_ABC_PhnT2
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0 Child Features

3 Contains

DB identifier Type Name
IPR003439 Domain ABC transporter-like
IPR013611 Domain Transport-associated OB, type 2
IPR017871 Conserved_site ABC transporter, conserved site

1 Cross References

Identifier
TIGR03265

0 Found In

1 GO Annotation

GO Term Gene Name
GO:0005524 IPR017666

1 Ontology Annotations

GO Term Gene Name
GO:0005524 IPR017666

0 Parent Features

4 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Pp3s34_610V3.1.p PAC:32948312 Physcomitrium patens 2078  
Brdisv1pangenome1007522m.p PAC:33619295 Brachypodium distachyon Pangenome 288  
Brdisv1pangenome1007772m.p PAC:33640884 Brachypodium distachyon Pangenome 475  
Brdisv1BdTR11A1042828m.p PAC:35693385 Brachypodium distachyon BdTR11a 475  

14 Publications

First Author Title Year Journal Volume Pages PubMed ID
            9872322
            9873074
            11421269
            1282354
            9640644
            11402022
            11080142
            11532960
            11421270
            11470432
            11988180
            7592415
            17070898
            16842370