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TonB C-terminal domain-containing protein
This family contains TonB members that are not captured by Pfam:PF03544. (from Pfam)
cell envelope integrity TolA C-terminal domain-containing protein
This family consists of several bacterial TolA proteins as well as two eukaryotic proteins of unknown function. Tol proteins are involved in the translocation of group A colicins. Colicins are bacterial protein toxins, which are active against Escherichia coli and other related species (See Pfam:PF01024). TolA is anchored to the cytoplasmic membrane by a single membrane spanning segment near the N-terminus, leaving most of the protein exposed to the periplasm [1]. [1]. 12423782. The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins. Lazzaroni JC, Dubuisson JF, Vianney A;. Biochimie 2002;84:391-397. (from Pfam)
cell envelope integrity protein TolA
cell envelope integrity protein TolA is part of the Tol-Pal system that plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity
TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB.
Inner membrane component of 7 member Tol-Pal envelope-spanning complex; involved in maintaining cell envelope integrity; utilized by colicins and filamentous phages for import; interacts with TolB, Pal, and through TolB to various outer membrane porins
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