ABC transporters - Phaeosphaeria nodorum

The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).

Environmental Information Processing; Membrane transport

Phaeosphaeria nodorum [GN:pno]

PMID:9799792

Tomii K, Kanehisa M.

A comparative analysis of ABC transporters in complete microbial genomes.

Genome Res 8:1048-59 (1998)

PMID:18424520

Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, Deho G, Silhavy TJ, Polissi A

Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli.

J Bacteriol 190:4460-9 (2008)

PMID:18375759

Ruiz N, Gronenberg LS, Kahne D, Silhavy TJ

Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli.

Proc Natl Acad Sci U S A 105:5537-42 (2008)

PMID:10557362

Omata T, Price GD, Badger MR, Okamura M, Gohta S, Ogawa T

Identification of an ATP-binding cassette transporter involved in bicarbonate uptake in the cyanobacterium Synechococcus sp. strain PCC 7942.

Proc Natl Acad Sci U S A 96:13571-6 (1999)

PMID:11731493

Quintero MJ, Montesinos ML, Herrero A, Flores E

Identification of genes encoding amino acid permeases by inactivation of selected ORFs from the Synechocystis genomic sequence.

Genome Res 11:2034-40 (2001)

PMID:16135226

Picossi S, Montesinos ML, Pernil R, Lichtle C, Herrero A, Flores E

ABC-type neutral amino acid permease N-I is required for optimal diazotrophic growth and is repressed in the heterocysts of Anabaena sp. strain PCC 7120.

Mol Microbiol 57:1582-92 (2005)

PMID:11929526

Valladares A, Montesinos ML, Herrero A, Flores E.

An ABC-type, high-affinity urea permease identified in cyanobacteria.

Mol Microbiol 43:703-15 (2002)

PMID:18326572

Richard-Fogal CL, Frawley ER, Kranz RG

Topology and function of CcmD in cytochrome c maturation.

J Bacteriol 190:3489-93 (2008)

PMID:16109926

Suzuki H, Koyanagi T, Izuka S, Onishi A, Kumagai H

The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette.

J Bacteriol 187:5861-7 (2005)

PMID:17873039

Novikova M, Metlitskaya A, Datsenko K, Kazakov T, Kazakov A, Wanner B, Severinov K

The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C.

J Bacteriol 189:8361-5 (2007)

PMID:17214741

Tikhonova EB, Devroy VK, Lau SY, Zgurskaya HI

Reconstitution of the Escherichia coli macrolide transporter: the periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB.

Mol Microbiol 63:895-910 (2007)

PMID:18805970

Yamanaka H, Kobayashi H, Takahashi E, Okamoto K

MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II.

J Bacteriol 190:7693-8 (2008)