Beta-barrel assembly machine protein A (BamA) (BamA)

Beta-barrel assembly machine protein A (BamA) is the central and essential component of the Beta-barrel assembly machinery (BAM) complex, which is found in the outer membrane of all Gram-negative bacteria [1, 7, 15]. It consists of a 16-stranded transmembrane beta-barrel domain and five N-terminal periplasmic polypeptide transport-associated (POTRA) domains [7, 15]. BamA's primary biological role is to catalyze the folding and insertion of nascent beta-barrel outer membrane proteins (OMPs) into the outer membrane, a process essential for maintaining the structural integrity and functional capacity of the bacterial cell envelope [4, 5, 13]. Due to its surface exposure and high conservation across diverse bacterial species, BamA has become a high-priority target for the development of novel antibiotics to combat multidrug-resistant (MDR) pathogens [3, 6, 9]. Therapeutic agents such as the natural peptide darobactin and the small molecule MRL-494 exert their bactericidal effects by binding to BamA—specifically at its lateral gate or extracellular loops—thereby inhibiting the assembly of vital OMPs and leading to lethal membrane disruption [8, 10, 11].

Other names

BamAOmp85YaetYaeTD15OMP85

Inhibition of outer membrane protein (OMP) assembly by blocking the BamA lateral gate or extracellular loops, leading to membrane instability and cell death [1, 8, 10, 11].