| EC |
7.6.2.14 |
| Accepted name: |
ABC-type aliphatic sulfonate transporter |
| Reaction: |
ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein][side 1] = ADP + phosphate + aliphatic sulfonate[side 2] + [sulfonate-binding protein][side 1] |
| Other name(s): |
aliphatic sulfonate transporting ATPase; alkane sulfonate ABC transporter; aliphatic sulfonate ABC transporter; ssuACB (gene names) |
| Systematic name: |
ATP phosphohydrolase (ABC-type, aliphatic sulfonate-importing) |
| Comments: |
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli K-12 interacts with an extracytoplasmic substrate binding protein and imports a broad range of aliphatic sulfonates for use as a source of sulfur. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
van Der Ploeg, J.R., Iwanicka-Nowicka, R., Bykowski, T., Hryniewicz, M.M. and Leisinger, T. The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl. J. Biol. Chem. 274 (1999) 29358–29365. [PMID: 10506196] |
| 2. |
Kertesz, M.A. Bacterial transporters for sulfate and organosulfur compounds. Res. Microbiol. 152 (2001) 279–290. [PMID: 11421275] |
| 3. |
Davidson, A.L., Dassa, E., Orelle, C. and Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72 (2008) 317–364. [PMID: 18535149] |
|
| [EC 7.6.2.14 created 2019] |
| |
|
| |
|
Printable version