Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris and Escherichia coli; site-directed mutagenesis causing impairment of export function.
The hlyB secretion genes of Proteus vulgaris and Escherichia coli showed 81% nucleotide homology and similar E. coli-atypical codon usage. The deduced protein sequences differed in 54 of 707 residues and shared a previously unreported sequence which corresponds to the ATP-binding motif characteristic of protein kinases. The motif was also conserved in the HlyB of Morganella morganii. Of 4 oligonucleotide-directed substitutions introduced into the putative E. coli HlyB motif, 2 non-conservative changes caused radical reductions in the export of active haemolysin protein.
Koronakis
V
V
Department of Pathology, Cambridge University, England.
Koronakis
E
E
Hughes
C
C
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D011494:Protein Kinases / Q000235:genetics; D011514:Proteus vulgaris / Q000235:genetics* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D006460:Hemolysin Proteins; C050837:Hlyb protein, Bacteria; D011494:Protein Kinases