English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The phosphoenolpyruvate‐dependent phosphotransferase system of Staphylococcus aureus 1. Amino‐acid sequence of the phosphocarrier protein HPr

MPS-Authors
/persons/resource/persons206340

Schrecker,  Otto
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons206099

Hengstenberg,  Wolfgang
Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Beyreuther, K., Raufuss, H., Schrecker, O., & Hengstenberg, W. (1977). The phosphoenolpyruvate‐dependent phosphotransferase system of Staphylococcus aureus 1. Amino‐acid sequence of the phosphocarrier protein HPr. European Journal of Biochemistry, 75(1), 275-286. doi:10.1111/j.1432-1033.1977.tb11527.x.


Cite as: https://hdl.handle.net/21.11116/0000-0002-D9E5-7
Abstract

The primary structure of the histidine‐containing phosphocarrier protein HPr of the phosphoenol‐pyruvate‐dependent phosphotransferase system from Staphylococcus 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, thermolytic and cyanogen bromide peptides as obtained by automated Edman degradation in a solid‐phase sequencer of Laursen. The amino‐acid sequence was found to be 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 molecular weight of 7685.

The one histidine involved in the phosphotransfer reaction of this protein was found at position 15 as part of a region of the sequence which has no predictable secondary structure. It is suggested that this protein belongs to the group of male proteins with the active center located on a protrusion rather than a cleft.