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. 1985 Sep;4(9):2287–2293. doi: 10.1002/j.1460-2075.1985.tb03928.x

Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems.

E Dassa, M Hofnung
PMCID: PMC554499  PMID: 3000770

Abstract

The MalG protein is needed for the transport of maltose in Escherichia coli K12. We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and is thus presumably an integral inner membrane protein which could span the membrane through six hydrophobic segments. We provide direct evidence from fusion proteins for the translation frame and we also identified the in vitro made MalG protein. We have found a sequence which is highly conserved between MalG and MalF, the other integral inner membrane protein of the maltose transport system. This conserved sequence is also present in all known integral membrane proteins of binding protein-dependent transport systems, always at the same distance (approximately 90 residues) from their COOH terminus. We discuss briefly this finding.

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Selected References

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