Protein Domain : IPR013525

Type:  Domain Name:  ABC-2 type transporter
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 2 of ABC transporters. Short Name:  ABC_2_trans
Paste the following link

0 Child Features

0 Contains

1 Cross References

Identifier
PF01061

10 Found Ins

DB identifier Type Name
IPR005284 Family Pigment precursor permease
IPR000412 Family ABC-2 transporter
IPR022403 Family Alcohol ABC transporter, permease protein
IPR004377 Family ABC transporter, permease protein DrrB/DrrC
IPR005981 Family ABC-2 type transporter, NodJ
IPR020064 Family ABC transporter, G1
IPR005285 Family Pleiotropic drug resistance protein PDR/CDR
IPR017501 Domain Phage infection protein, YhgE, C-terminal
IPR005943 Family Daunorubicin resistance protein C
IPR005942 Family Daunorubicin resistance ABC transporter membrane protein

1 GO Annotation

GO Term Gene Name
GO:0016020 IPR013525

1 Ontology Annotations

GO Term Gene Name
GO:0016020 IPR013525

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
93017 D8RG54 PAC:15418217 Selaginella moellendorffii 695  
171321 D8RHS6 PAC:15408019 Selaginella moellendorffii 681  
93898 D8RGW5 PAC:15402194 Selaginella moellendorffii 611  
171782 D8RIJ5 PAC:15411374 Selaginella moellendorffii 644  
172580 D8RLA2 PAC:15412742 Selaginella moellendorffii 1424  
412710 D8RL86 PAC:15413851 Selaginella moellendorffii 1781  
412699 D8RL77 PAC:15413246 Selaginella moellendorffii 1446  
441722 D8RL97 PAC:15410157 Selaginella moellendorffii 1700  
441720 D8RL81 PAC:15410156 Selaginella moellendorffii 1687  
441717 D8RL73 PAC:15410131 Selaginella moellendorffii 1379  
96758 D8RL93 PAC:15410129 Selaginella moellendorffii 1413  
96729 D8RLA4 PAC:15410062 Selaginella moellendorffii 1450  
173584 D8RRL8 PAC:15415705 Selaginella moellendorffii 1421  
99541 D8RRM0 PAC:15417312 Selaginella moellendorffii 1425  
101338 D8RT52 PAC:15402365 Selaginella moellendorffii 1426  
267739 D8RT58 PAC:15413570 Selaginella moellendorffii 1336  
415867 D8RXH6 PAC:15423305 Selaginella moellendorffii 619  
417272 D8S2P1 PAC:15402323 Selaginella moellendorffii 1387  
417266 D8S2N6 PAC:15402308 Selaginella moellendorffii 1389  
417263 D8S2N3 PAC:15402303 Selaginella moellendorffii 1725  
230259 D8QYN0 PAC:15412361 Selaginella moellendorffii 651  
111419 D8S940 PAC:15410387 Selaginella moellendorffii 616  
111389 D8S926 PAC:15409708 Selaginella moellendorffii 612  
111338 D8S930 PAC:15409614 Selaginella moellendorffii 614  
419486 D8S938 PAC:15409753 Selaginella moellendorffii 397  
419476 D8S928 PAC:15409719 Selaginella moellendorffii 488  
419484 D8S936 PAC:15409749 Selaginella moellendorffii 202  
82705 D8R2M2 PAC:15413472 Selaginella moellendorffii 1441  
115821 D8SFU8 PAC:15402703 Selaginella moellendorffii 1459  
234186 D8SIP9 PAC:15423241 Selaginella moellendorffii 673  

13 Publications

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