Protein Domain : IPR001626

Type:  Family Name:  ABC-3
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).A number of bacterial transport systems have been found to contain integral membrane components that have similar sequences []: these systems fit thecharacteristics of ATP-binding cassette transporters []. Theproteins form homo- or hetero-oligomeric channels, allowing ATP-mediated transport. Hydropathy analysis of the proteins has revealed the presenceof 6 possible transmembrane regions. These proteins belong to family 3 of ABC transporters. Short Name:  ABC_3

1 Child Features

DB identifier Type Name
IPR022392 Family Anchored repeat-type ABC transporter, permease subunit

0 Contains

1 Cross References

Identifier
PF00950

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0005524 IPR001626
GO:0042626 IPR001626
GO:0006810 IPR001626
GO:0016020 IPR001626

4 Ontology Annotations

GO Term Gene Name
GO:0005524 IPR001626
GO:0042626 IPR001626
GO:0006810 IPR001626
GO:0016020 IPR001626

0 Parent Features

13 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0051.1.p PAC:28856429 Arabidopsis halleri 243  
Brdisv1pangenome1008746m.p PAC:33659210 Brachypodium distachyon Pangenome 279  
Brdisv1pangenome1009881m.p PAC:33608166 Brachypodium distachyon Pangenome 269  
Brdisv1pangenome1009579m.p PAC:33656773 Brachypodium distachyon Pangenome 271  
Brdisv1pangenome1011023m.p PAC:33640809 Brachypodium distachyon Pangenome 335  
Brdisv1pangenome1011190m.p PAC:33623588 Brachypodium distachyon Pangenome 284  
Brdisv1pangenome1010547m.p PAC:33640901 Brachypodium distachyon Pangenome 262  
Brdisv1BdTR11A1048566m.p PAC:35690823 Brachypodium distachyon BdTR11a 262  
Brdisv1BdTR11A1047467m.p PAC:35689618 Brachypodium distachyon BdTR11a 269  
Brdisv1BdTR11A1049158m.p PAC:35693344 Brachypodium distachyon BdTR11a 442  
Brdisv1BdTR11A1039949m.p PAC:35696136 Brachypodium distachyon BdTR11a 279  
Brdisv1BdTR11A1040647m.p PAC:35692585 Brachypodium distachyon BdTR11a 271  
Brdisv1BdTR11A1041113m.p PAC:35693154 Brachypodium distachyon BdTR11a 284  

13 Publications

First Author Title Year Journal Volume Pages PubMed ID
            9872322
            9873074
            11421269
            1282354
            9640644
            11402022
            11080142
            11532960
            11421270
            11470432
            11988180
            1659649
            1303751