Structure of bacterial phospholipid transporter MlaFEDB with substrate bound.
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The primary structural study places the MlaA outer-membrane interface in the three-part Mla pathway.
"This system consists of three main parts: (1) an IM ABC transporter complex, MlaFEDB; (2) an OM complex, MlaA-OmpC/F; and (3) a soluble periplasmic protein, MlaC, which has been proposed to shuttle phospholipids between MlaFEDB and MlaA-OmpC/F (Figure 1A)."
Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
UniProt record for Pseudomonas putida KT2440 VacJ/MlaA (Q88KX6)
OpenScientist functional research for PSEPK vacJ
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The report supports an outer-membrane MlaA/VacJ lipid-handling role from conserved-family and ortholog evidence, but found no direct experimental characterization of PP_2163.
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Net transport direction, N-terminal lipidation, and the identity of any KT2440 porin partner remain unresolved for this specific protein.