Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS.
Protein abundance profiling of the Escherichia coli cytosol.
An ABC transport system that maintains lipid asymmetry in the gram-negative outer membrane.
Escherichia coli genes that reduce the lethal effects of stress.
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A yrbB::Tn5 insertion confers hyperlethality to nalidixic acid without altering MIC; the authors attribute yrbB to outer-membrane-related function.
"These data indicate that the yrbB mutation does not change the permeablility to most compounds, which is consistent with our finding that the yrbB mutation did not change the bacteriostatic effects of nalidixic acid."
Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry.
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MlaB is required for MlaFEDB assembly and activity, likely via MlaF structure and stability.
"Finally, we establish that MlaB is necessary for both the assembly and activity of the ABC transporter, likely by modulating MlaF structure and stability."
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MlaB T52A leaves assembly intact but abolishes ATPase activity.
"We have also established a separate role for MlaB in the activity of the complex; a single T52A mutation in the STAS domain protein does not affect complex assembly but abolishes ATPase activity"
Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.
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MlaB is the STAS-domain protein encoded in the mla operon.
"The mla operon also encodes an ABC-type (ATP binding cassette) ATPase (MlaF), a periplasmic protein MlaC, and a STAS domain protein, MlaB"
Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.
Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation.
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MlaB binds the MlaF NBD and is required for MlaF stability.
"MlaB, a STAS domain protein, binds the ABC nucleotide binding domain, MlaF, and is required for its stability."
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MlaF over-expression suppresses loss of MlaB.
"This suggests that MlaB may have no essential function in Mla lipid transport apart from its role in promoting MlaF stability and/or association with the MlaFEDB complex."
Structural insights into outer membrane asymmetry maintenance in Gram-negative bacteria by MlaFEDB.
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Reconstituted MlaFEDB transport system and cryo-EM structures.
"establish a proteoliposome-based transport system that includes MlaFEDB, MlaC and MlaA-OmpF to monitor the transport direction of phospholipids"
Structure of bacterial phospholipid transporter MlaFEDB with substrate bound.
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MlaB binds each MlaF on the cytoplasmic side; the lipid pathway runs through MlaE and MlaD.
"On the cytoplasmic side, each of the MlaF ATPase subunits is bound to MlaB"
UniProt record for Escherichia coli K-12 MlaB (P64602)