ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily which
uses the hydrolysis of ATP to energize diverse biological import and export
systems. ABC transporters are minimally constituted of two conserved regions:
a highly conserved ATP binding cassette (ABC) (see <PDOC00185>) and a less
conserved transmembrane domain (TMD). These regions can be found on the same
protein (mostly in eukaryotes and bacterial exporters) or on two different
ones (mostly bacterial importers) [1,2,3]. But in a subgroup of exporters, the
transmembrane region is encoded by a separated polypeptide, the ABC-2 type
transport system integral membrane protein. The molecular size of this
transmembrane protein is around 30 Kd. It is thought to contain six
transmembrane regions, it either form homooligomeric channels or associate
with another type of transmembrane protein to form heteroligomers. The
function of the integral inner-membrane protein is to translocate the
substrate across the membrane and seems to play an important role in substrate
recognition [4].
The ABC-2 type transport system integral membrane proteins with a functional
attribution are listed below:
Escherichia coli wzm (kpsM), involved in polysialic acid export.
Haemophilus influenzae bexB, involved in polyribosylribitol phosphate
capsule polysaccharide export.
Neisseria meningitidis ctrC, involved in polyneuraminic acid capsule
polysaccharide export.
Rhizobiacae nodulation protein J (gene nodJ), probably involved in
exporting a modified β-1,4-linked N-acetylglucosamine oligosaccharide.
Streptomyces peucetius drrB, involved in exporting the antibiotics
daunorubicin and Doxorubicin.
Klebsiella pneumoniae O-antigen export system protein rfbA.
Yersinia enterocolitica O-antigen export system protein rfbD.
Escherichia coli hypothetical protein yadH.
Escherichia coli hypothetical protein yhhJ.
Escherichia coli hypothetical protein yhih.
The profile we developed recognize the six transmembrane regions of ABC-2
integral membrane proteins.
Note:
These profile replaces a pattern (PS00890) whose specificity was
inadequate. Furthermore, this profile matches some eukaryotic transporters in
Drosophila melanogaster, Dictyostelium discoideum, Anopheles gambiae, and
some prokaryotic fused exporters. None of these atypical matches are detected
by other ABC TMD profiles (see <PDOC00364>).
Last update:
May 2005 / Text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
References
1
Authors
Holland I.B., Cole S.P.C., Kuchler K., Higgins C.F.
Source
(In) ABC proteins from bacteria to man, Academic Press, San Diego, (2003).
2
Authors
Holland I.B., Blight M.A.
Source
J. Mol. Biol. 293:381-399(1999).
3
Authors
Saurin W., Hofnung M., Dassa E.
Title
Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.
The NodL and NodJ proteins from Rhizobium and Bradyrhizobium strains are similar to capsular polysaccharide secretion proteins from gram-negative bacteria.
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