The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain
| Autor: | Ira Herskowitz, Flora Banuett, M A Innis, K E Rudd, J A Noble, Eugene V. Koonin |
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| Rok vydání: | 1993 |
| Předmět: |
Molecular Sequence Data
Restriction Mapping Sequence alignment Biology GTP Phosphohydrolases GTP-binding protein regulators Adenosine Triphosphate Bacterial Proteins GTP-Binding Proteins Consensus Sequence Consensus sequence Escherichia coli Amino Acid Sequence Integral membrane protein Peptide sequence Lysogeny Multidisciplinary Base Sequence Sequence Homology Amino Acid Serine Endopeptidases Membrane Proteins Lambda phage biology.organism_classification Bacteriophage lambda Biochemistry Membrane protein Genes Bacterial Sequence motif Sequence Alignment Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 90(22) |
| ISSN: | 0027-8424 |
| Popis: | The hflA (high frequency of lysogenization) locus of Escherichia coli governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII 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. |
| Databáze: | OpenAIRE |
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