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Unveiling multiple copies of MlaC highlights its multifaceted nature

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Abstract

The maintenance of the lipid asymmetry (Mla) system plays a critical role in facilitating the transport of phospholipids between the inner and outer membranes of the Gram-negative bacteria. In E. coli, the system consists of six proteins: MlaA-OmpF/C complex (outer membrane), MlaC (periplasm), and MlaFEDB complex (inner membrane). Despite extensive research on the core proteins (MlaFED) of the Mla system, the occurrence of Mla components like MlaA, MlaB, and MlaC in diderm remains uncertain. Therefore, this gap presents a significant opportunity for further investigation, particularly regarding MlaC, which serves as the sole mobile component of the Mla system. This has led to the identification of multiple copies of MlaC in 63 distinct genera of Proteobacteria and related phyla. Interestingly, amongst these genera, the genetic arrangements of the mla operon were observed to be varying and, thus, were further categorized into four distinct groups. The variations among the genetic organization of the mla operons suggest their evolution through various processes, such as duplications, losses, rearrangements, and fusions. Further, the results of this study highlight the MlaC’s substrate promiscuity, illuminating new avenues for the Mla system.

Highlights

• Multiple copies of MlaC and other Mla components were identified.

• A unique motif, “Ω-ζ-Φ/π-Φ-ζ-Φ” is located in the subdomain D1R2 of MlaC.

• The genetic arrangement of the mla operon is not conserved.

• MlaC duplicates demonstrate substrate promiscuity.

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Data availability

No datasets were generated or analysed during the current study.

Abbreviations

CTD:

C-terminal domain

LPS:

Lipopolysaccharide

Mla:

Maintenance of lipid asymmetry

MSA:

Multiple sequence alignment

NBD:

Nucleotide-binding domain

NTD:

N-terminal domain

OM:

Outer membrane

Omp:

Osmoporin

PL:

Phospholipid

SBP:

Substrate-binding protein

TMD:

Transmembrane domain

References

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Acknowledgements

The work was supported by the Science and Engineering Research Board (SERB), Department of Science and Technology (DST), Government of India (Grant number: EEQ/2021/000060). The authors acknowledge the facilities provided by the Indian Institute of Technology Guwahati, Assam, India. The authors would like to express their gratitude to the members of the Structural and Computational Biology Laboratory (SCBL) for all the timely support. RT acknowledges the Ministry of Education, Government of India, for providing the research fellowship.

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Authors

Contributions

SPK conceived the project and guided the research. RT and DA collected the data. RT performed the formal data analysis. RT and SPK analyzed the data. RT and SPK wrote the manuscript.

Corresponding author

Correspondence to Shankar Prasad Kanaujia.

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Competing interests

The authors declare no competing interests.

Additional information

Communicated by Yusuf Akhter.

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Tripathi, R., Ayekpam, D. & Kanaujia, S.P. Unveiling multiple copies of MlaC highlights its multifaceted nature. Arch Microbiol 207, 107 (2025). https://doi.org/10.1007/s00203-025-04308-0

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  • DOI: https://doi.org/10.1007/s00203-025-04308-0

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