PF04069

Substrate binding domain of ABC-type glycine betaine transport system

Pfam entry
Member databasePfam
Pfam typefamily
Short nameOpuAC
ClanPBP
Author Kerrison ND;0000-0002-1471-953X Finn RD;0000-0001-8626-2148
Sequence Ontology0100021

Description

Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis
[1]
. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine
[2]
. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA).

References

1.OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. Kempf B, Bremer E. J. Biol. Chem. 270, 16701-13, (1995). View articlePMID: 7622480

2.Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Kappes RM, Kempf B, Kneip S, Boch J, Gade J, Meier-Wagner J, Bremer E. Mol. Microbiol. 32, 203-16, (1999). View articlePMID: 10216873

Further reading

3. Identification and characterization of an ATP binding cassette L-carnitine transporter in Listeria monocytogenes. Fraser KR, Harvie D, Coote PJ, O'Byrne CP. Appl. Environ. Microbiol. 66, 4696-704, (2000). View articlePMID: 11055912

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