biostudies-literatureMurthy ACNational Science Foundatione0003323https://www.ebi.ac.uk/biostudies/studies/S-EPMC10294652biostudies-literatureUnknown205(6)Conjugation is a major form of horizontal gene transfer, contributing to bacterial evolution and the acquisition of new traits. During conjugation, a donor cell transfers DNA to a recipient through a specialized DNA translocation channel classified as a type IV secretion system (T4SS). Here, we focused on the T4SS of ICE<i>Bs1</i>, an integrative and conjugative element in Bacillus subtilis. ConE, encoded by ICE<i>Bs1</i>, is a member of the VirB4 family of ATPases, the most conserved component of T4SSs. ConE is required for conjugation and localizes to the cell membrane, predominantly at the cell poles. In addition to Walker A and B boxes, VirB4 homologs have conserved ATPase motifs C, D, and E. Here, we created alanine substitutions in five conserved residues within or near ATPase motifsJournal of bacteriologyCharacterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICE<i>Bs1</i> of Bacillus subtilis.PMC10294652NSF-RUI 1157878NSF-RUI 1613920Ragucci AESwerdlow KJKalashyan MBui MNNBerkmen MBBroulidakis MPAleksanyan NMorton GMChen SToyoda HCMuccioli MMurthy ACfalseCharacterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICE<i>Bs1</i> of Bacillus subtilis.Conjugation is a major form of horizontal gene transfer, contributing to bacterial evolution and the acquisition of new traits. During conjugation, a donor cell transfers DNA to a recipient through a specialized DNA translocation channel classified as a type IV secretion system (T4SS). Here, we focused on the T4SS of ICE<i>Bs1</i>, an integrative and conjugative element in Bacillus subtilis. ConE, encoded by ICE<i>Bs1</i>, is a member of the VirB4 family of ATPases, the most conserved component of T4SSs. ConE is required for conjugation and localizes to the cell membrane, predominantly at the cell poles. In addition to Walker A and B boxes, VirB4 homologs have conserved ATPase motifs C, D, and E. Here, we created alanine substitutions in five conserved residues within or near ATPase motifs2023-01-01T00:00:00Z2023 Jun2026-06-08T06:41:50.592Z2025-04-04T20:37:34.534ZS-EPMC102946523721945710.1128/jb.00033-23