Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1862, Issue 10, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2020.183319
Keywords
SecA; Clustering protocol; Phylogenetic information; Charge of SecA sequences; Lipid binding motif; NBD1 and PBD sequence clusters
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Funding
- Excellence Initiative of the German Federal and State Governments by the Freie Universitat Berlin
- Spanish Ministry of Science [RTI2018-098983-8-10]
- Granada Excellence Network of Innovation Laboratories Strengthening through Short-Visits Fellowship (GENIL-SSV 2012)
- European Commission Marie CurieInternational Reintegration Award [FP7-PEOPLE-2010-RG-276920]
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SecA is an essential component of the Sec protein secretion pathway in bacteria. Secretory proteins targeted to the Sec pathway by their N-terminal signal peptide bind to SecA, which couples binding and hydrolysis of adenosine triphosphate with movement of the secretory protein across the membrane-embedded SecYEG protein translocon. The phylogenetic diversity of bacteria raises the important question as to whether the region of SecA where the pre-protein binds has conserved sequence features that might impact the reaction mechanism of SecA. To address this question we established a large data set of SecA protein sequences and implemented a protocol to cluster and analyze these sequences according to features of two of the SecA functional domains, the protein binding domain and the nucleotide-binding domain 1. We identify remarkable sequence diversity of the protein binding domain, but also conserved motifs with potential role in protein binding. The N-terminus of SecA has sequence motifs that could help anchor SecA to the membrane. The overall sequence length and net estimated charge of SecA sequences depend on the organism.
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