<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rank L</submitter><funding>NIAID NIH HHS</funding><funding>HHS | NIH | National Cancer Institute</funding><funding>NCI NIH HHS</funding><funding>HHS | NIH | National Institute of Allergy and Infectious Diseases</funding><pagination>e00685-20</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8088607</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>203(10)</volume><pubmed_abstract>Mycobacteria possess Mce transporters that import lipids and are thought to function analogously to ATP-binding cassette (ABC) transporters. However, whereas ABC transporters import substrates using a single solute-binding protein (SBP) to deliver a substrate to permease proteins in the membrane, mycobacterial Mce transporters have a potential for six SBPs (MceA to MceF) working with a pair of permeases (YrbEA and YrbEB), a cytoplasmic ATPase (MceG), and multiple Mce-associated membrane (Mam) and orphaned Mam (Omam) proteins to transport lipids. In this study, we used the model mycobacterium &lt;i>Mycobacterium smegmatis&lt;/i> to study the requirement for individual Mce, Mam, and Omam proteins in Mce4 transport of cholesterol. All of the Mce4 and Mam4 proteins we investigated were required for </pubmed_abstract><journal>Journal of bacteriology</journal><pubmed_title>Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.</pubmed_title><pmcid>PMC8088607</pmcid><funding_grant_id>P30CA016086</funding_grant_id><funding_grant_id>P30 CA016086</funding_grant_id><funding_grant_id>AI135899</funding_grant_id><funding_grant_id>R21 AI135899</funding_grant_id><pubmed_authors>Braunstein M</pubmed_authors><pubmed_authors>Herring LE</pubmed_authors><pubmed_authors>Rank L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.</name><description>Mycobacteria possess Mce transporters that import lipids and are thought to function analogously to ATP-binding cassette (ABC) transporters. However, whereas ABC transporters import substrates using a single solute-binding protein (SBP) to deliver a substrate to permease proteins in the membrane, mycobacterial Mce transporters have a potential for six SBPs (MceA to MceF) working with a pair of permeases (YrbEA and YrbEB), a cytoplasmic ATPase (MceG), and multiple Mce-associated membrane (Mam) and orphaned Mam (Omam) proteins to transport lipids. In this study, we used the model mycobacterium &lt;i>Mycobacterium smegmatis&lt;/i> to study the requirement for individual Mce, Mam, and Omam proteins in Mce4 transport of cholesterol. All of the Mce4 and Mam4 proteins we investigated were required for </description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Apr</publication><modification>2026-05-08T15:54:00.203Z</modification><creation>2024-11-21T07:36:14.104Z</creation></dates><accession>S-EPMC8088607</accession><cross_references><pubmed>33649150</pubmed><doi>10.1128/jb.00685-20</doi><doi>10.1128/JB.00685-20</doi></cross_references></HashMap>