Protein Domain : IPR010129

Type:  Family Name:  Type I secretion membrane fusion protein, HlyD
Description:  Type I secretion is an ABC transporter that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C terminus of the transported protein. This entry represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This entry selects a group of sequences closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins.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). Short Name:  T1SS_HlyD
Paste the following link

0 Child Features

1 Contains

DB identifier Type Name
IPR006144 Conserved_site Secretion protein HlyD, conserved site

2 Cross Referencess

Identifier
PTHR30386:SF3
TIGR01843

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0015031 IPR010129
GO:0016021 IPR010129

2 Ontology Annotations

GO Term Gene Name
GO:0015031 IPR010129
GO:0016021 IPR010129

1 Parent Features

DB identifier Type Name
IPR003997 Family RTX secretion protein D, Gram-negative bacteria

7 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
30333.m000035 B9TG05 PAC:16824350 Ricinus communis 291  
27739.m000027 B9TCF4 PAC:16799044 Ricinus communis 305  
Brdisv1pangenome1009039m.p PAC:33608090 Brachypodium distachyon Pangenome 957  
Brdisv1pangenome1009394m.p PAC:33620248 Brachypodium distachyon Pangenome 1012  
Brdisv1BdTR11A1040492m.p PAC:35694268 Brachypodium distachyon BdTR11a 1016  
Brdisv1BdTR11A1040603m.p PAC:35689136 Brachypodium distachyon BdTR11a 1012  
Brdisv1BdTR11A1041741m.p PAC:35693052 Brachypodium distachyon BdTR11a 919  

11 Publications

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