Secretion of most polypeptides across the bacterial plasma membrane is cata
lyzed by the Sec protein translocase. This complex molecular machine compri
ses a flexible transmembrane conduit coupled to a motor-like component and
displays four activities: (a) it is a specific receptor at its cytoplasmic
side for all secretory polypeptides, (b) it converts metabolic energy from
ATP and proton gradients into mechanical motion, (c) it prevents substrates
from folding in statu translocanti and (d) it binds and releases short seg
ments of the polymeric substrate sequentially. Combination of these activit
ies allows translocase to move processively along the length of the substra
te. Substrates are thus gradually expelled from the membrane and are releas
ed for subsequent extracytoplasmic folding. (C) 2000 Federation of European
Biochemical Societies. Published by Elsevier Science B.V. All rights reser
ved.