<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Riedel S</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>406</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6424863</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10</volume><pubmed_abstract>The mitochondrial ATP-binding cassette (ABC) transporters ABCB7 in humans, Atm1 in yeast and ATM3 in plants, are highly conserved in their overall architecture and particularly in their glutathione binding pocket located within the transmembrane spanning domains. These transporters have attracted interest in the last two decades based on their proposed role in connecting the mitochondrial iron-sulfur (Fe-S) cluster assembly with its cytosolic Fe-S cluster assembly (CIA) counterpart. So far, the specific compound that is transported across the membrane remains unknown. In this report we characterized the ABCB7-like transporter Rcc02305 in &lt;i>Rhodobacter capsulatus&lt;/i>, which shares 47% amino acid sequence identity with its mitochondrial counterpart. The constructed interposon mutant strain </pubmed_abstract><journal>Frontiers in microbiology</journal><pubmed_title>The ABCB7-Like Transporter PexA in &lt;i>Rhodobacter capsulatus&lt;/i> Is Involved in the Translocation of Reactive Sulfur Species.</pubmed_title><pmcid>PMC6424863</pmcid><funding_grant_id>LE1171/15-1</funding_grant_id><funding_grant_id>LE1171/6-2</funding_grant_id><funding_grant_id>SCHU 1251/17-1</funding_grant_id><pubmed_authors>Leimkuhler S</pubmed_authors><pubmed_authors>Muller CS</pubmed_authors><pubmed_authors>Riedel S</pubmed_authors><pubmed_authors>Watanabe M</pubmed_authors><pubmed_authors>Schunemann V</pubmed_authors><pubmed_authors>Siemiatkowska B</pubmed_authors><pubmed_authors>Hoefgen R</pubmed_authors></additional><is_claimable>false</is_claimable><name>The ABCB7-Like Transporter PexA in &lt;i>Rhodobacter capsulatus&lt;/i> Is Involved in the Translocation of Reactive Sulfur Species.</name><description>The mitochondrial ATP-binding cassette (ABC) transporters ABCB7 in humans, Atm1 in yeast and ATM3 in plants, are highly conserved in their overall architecture and particularly in their glutathione binding pocket located within the transmembrane spanning domains. These transporters have attracted interest in the last two decades based on their proposed role in connecting the mitochondrial iron-sulfur (Fe-S) cluster assembly with its cytosolic Fe-S cluster assembly (CIA) counterpart. So far, the specific compound that is transported across the membrane remains unknown. In this report we characterized the ABCB7-like transporter Rcc02305 in &lt;i>Rhodobacter capsulatus&lt;/i>, which shares 47% amino acid sequence identity with its mitochondrial counterpart. The constructed interposon mutant strain </description><dates><release>2019-01-01T00:00:00Z</release><publication>2019</publication><modification>2026-04-07T14:24:55.658Z</modification><creation>2019-06-06T21:00:49Z</creation></dates><accession>S-EPMC6424863</accession><cross_references><pubmed>30918498</pubmed><doi>10.3389/fmicb.2019.00406</doi></cross_references></HashMap>