LPTD Antibody

1. These results demonstrate that multiple periplasmic proteases monitor outer membrane proteins at distinct points in the assembly process as in the case of degradation of the outer membrane protein LptD by the DegP, BepA and YcaL proteases. PMID: 28784813
2. the mutant protein lptD4213 is synthetically lethal with the deletion of dsbB as well as with DsbB inhibitors PMID: 28232484
3. findings suggest lptE14 causes poor plugging of the LptD beta barrel and that a reduction of ineffectively plugged LptD-LptE14 complexes in the outer membrane decreases permeability to erythromycin; lptE14 supports a proposed plug-and-barrel LptE-LptD arrangement PMID: 23316047
4. disulfide bond-dependent protein folding of LptD requires the proper assembly of a two-protein complex to promote disulfide bond rearrangement. PMID: 22936569
5. Data show that oxidation of LptD is not required for the formation of the LptD/E complex but it is essential for function. PMID: 20566849
6. LptD contains a soluble N-terminal domain and a C-terminal transmembrane domain. LptE stabilizes LptD by interacting with the C-terminal domain of LptD. LptE binds LPS specifically and may serve as a substrate recognition site at the outer membrane. PMID: 20203010
7. Results show that RlpB is essential for cell viability and that the Imp/RlpB complex is responsible for lipopolysaccharides reaching the outer surface of the outer membrane. PMID: 16861298

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KEGG: ecj:JW0053

STRING: 316385.ECDH10B_0055