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PMID: 6392295 Published · ppublish English Journal Article

The primary structure of Salmonella typhimurium HPr, a phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system. A correction.

The Journal of biological chemistry ·Vol. 259 ·No. 24 ·1984-12-25 ·Pages 15212-4

Powers DA, Roseman S

Abstract

The protein HPr is a low-molecular-weight phosphocarrier protein of the bacterial phosphoenolpyruvate:glycose phosphotransferase system. We have recently reported the complete primary amino acid sequence of HPr isolated from Salmonella typhimurium (Weigel, N., Powers, D.A., and Roseman, S. (1982) J. Biol. Chem. 257, 14499-14509). This sequence is incorrect at certain residues; the correct primary structure of the protein is presented in this report. The corrected structure generally agrees with the primary sequence predicted for HPr from Escherichia coli (based on the nucleotide sequence of the corresponding ptsH gene). The one apparent ambiguity is at the carboxyl terminus.

MeSH Terms
Amino Acid Sequence Bacterial Proteins Peptide Fragments/analysis Phosphoenolpyruvate Sugar Phosphotransferase System/isolation & purification Salmonella typhimurium/enzymology
Chemicals
Bacterial Proteins Peptide Fragments Phosphoenolpyruvate Sugar Phosphotransferase System phosphocarrier protein HPr
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Powers D A
Roseman S
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1984-12-25
Pages
15212-4
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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