| EC |
7.6.2.9 |
| Accepted name: |
ABC-type quaternary amine transporter |
| Reaction: |
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] |
| Other name(s): |
glycine betaine ABC transporter; ProVWX; quaternary-amine ABC transporter; quaternary-amine-transporting ATPase (ambiguous) |
| Systematic name: |
ATP phosphohydrolase (ABC-type, quaternary-amine-importing) |
| Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of quaternary amine derivatives. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321] |
| 2. |
Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213–6220. [DOI] [PMID: 9335265] |
| 3. |
Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977] |
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| [EC 7.6.2.9 created 2000 as EC 3.6.3.32, transferred 2018 to EC 7.6.2.9] |
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