The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain

J. A. Noble, M. A. Innis, E. V. Koonin, K. E. Rudd, F. Banuett, I. Herskowitz

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

The hflA (high frequency of lysogenization) locus of Escherichia coli governs the lysis-lysogeny decision of bacteriophage A by controlling stability of the phage ell protein. HflA contains three genes, hflX, hflK, and hflC, encoding polypeptides of 50, 46, and 37 kDa, respectively. We have determined the nucleotide sequence of 3843 base pairs containing hflA and have found three large open reading frames corresponding to hflX, hflK, and hflC. HflX contains the three sequence motifs typical of GTP-binding proteins and appears to be a member of a distinct family of putative GTPases. HflC and HflK appear to be integral membrane proteins which show some similarity to each other and to a human membrane protein. The C-terminal region of HflC contains a domain resembling the catalytic domain of ClpP, a bacterial ATP-dependent protease. We hypothesize that HflK and HflC constitute a distinct membrane-bound protease whose activity may be modulated by HflX GTPase.

Original languageEnglish (US)
Pages (from-to)10866-10870
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number22
DOIs
StatePublished - 1993

Keywords

  • Bacteriophage λ
  • cII protein
  • Lysis-lysogeny decision
  • Proteolysis

ASJC Scopus subject areas

  • General
  • Genetics

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