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Complete Amino Acid Sequence and Comparative Molecular Modeling of HPR from Streptococcus mutans Ingbritt

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Abstract

The heat-stable phosphocarrier protein (HPr) of Streptococcus mutans was extracted from whole cells using sodium lauroylsarcosinate/EDTA and purified to homogeneity by a single-step, ion-exchange chromatographic procedure. The complete amino acid sequence of the protein was determined from peptides generated by trypsin, α-chymotrypsin, endoproteinase Glu-C, and cyanogen bromide treatment. The HPr from S. mutans contains 86 or 87 amino acyl residues, depending on removal of the N-terminal Met and the protein shows high sequence homology with HPr from other Gram-positive bacteria. The predicted tertiary structure of the S. mutans HPr, from model building by homology, is an open-faced β-sandwich consisting of two α-helices and a four-stranded antiparallel β-sheet.

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Cited by (3)

  • HPr(His~P)-mediated phosphorylation differently affects counterflow and proton motive force-driven uptake via the lactose transport protein of Streptococcus thermophilus

    2000, Journal of Biological Chemistry
    Citation Excerpt :

    The N terminus of purified HPr from S. thermophilus was analyzed, and the sequence of the first 51 amino acids was determined:1MASKDFHIVAETGIHARPATLLVQTASKFASDITLEYKGKAVNLKSIMGVM51. This amino acid sequence is identical to the N-terminal sequence of HPr from Streptococcas mutans and S. salivarius except for the glutamate residue at position 36, which is variable among HPr proteins purified from Gram-positive bacteria (15, 16). The predicted Enzyme I and HPr(Ser) kinase phosphorylation sites, His-15 and Ser-46, are both present in the HPr protein fromS.

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