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protein-export chaperone SecB
This family consists of preprotein translocase subunit SecB. SecB is required for the normal export of envelope proteins out of the cell cytoplasm [1]. [1]. 2656409. Characterization of the Escherichia coli protein-export gene secB. Kumamoto CA, Nault AK;. Gene 1989;75:167-175. (from Pfam)
protein-export chaperone SecB, a component of the multisubunit membrane-bound enzyme Sec protein translocase, functions as an export-specific molecular chaperone that selectively binds preproteins, maintains them in a translocation competent state and delivers them to SecA, the membrane-bound ATPase that drives the translocation reaction
This protein acts as an export-specific cytosolic chaperone. It binds the mature region of pre-proteins destined for secretion, prevents aggregation, and delivers them to SecA. This protein is tetrameric in E. coli. The archaeal Methanococcus jannaschii homolog MJ0357 has been shown (PMID:14985117) to share many properties, including chaperone-like activity, and scores between trusted and noise.
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