The Phosphoenolpyruvate-Dependent Phosphotransferase System of Staphylococcus aureus. 1. Amino-Acid Sequence of the Phosphocarrier Protein HPr

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Abstract
The primary structure of the histidine-containing phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system from S. aureus was determined by automated Edman degradation. The complete sequence was deduced from the direct analysis of the protein by automated Edman degradation in a liquid-phase sequencer of Edman and from the sequence of tryptic [EC 3.4.21.4], thermolytic [EC 3.4.24.4] and CNBr peptides as obtained by automated Edman degradation in a solid-phase sequencer. The amino-acid sequence was Met-Glu-Gln-Asn-Ser-Tyr-Val-Ile-Ile-Asp-Glu-Thr-Gly-Ile-His-Ala-Arg-Pro-Ala-Thr-Met-Leu-Val-Gln-Thr-Ala-Ser-Lys-Phe-Asp-Ser-Ile-Asp-Gln-Gly-Gly-Tyr-Asp-Ser-Met-Gln-Leu-Lys-Ser-Leu-Gly-Val-Gly-Lys-Asp-Glu-Glu-Ile-Thr-Ile-Tyr-Ser-Ala-Asp-Lys-Lys-Glu-Gly-Leu-Thr-Lys-Met-Ser-Ile-Val. The 70 residues correspond to a MW of 7685. The 1 histidine involved in the phosphotransfer reaction of this protein was at position 15 as part of a region of the sequence which has no predictable secondary structure. This protein probably belongs to the group of male proteins with the active center located on a protrusion rather than a cleft.