PMID:2060763: Difference between revisions

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<span style = 'font-size: large'> '''Haydon, DJ and Guest, JR'''  (1991) A new family of bacterial regulatory proteins.''FEMS Microbiol. Lett.'' '''63''':291-5</span>
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!align=left  |Citation
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'''No author listed'''  (1991) A new family of bacterial regulatory proteins. ''FEMS Microbiol. Lett.'' '''63''':291-5
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!align=left  |Abstract
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A new family of bacterial regulatory proteins has been identified by sequence similarity. The family contains the repressor of the Bacillus subtilis gluconate operon (GntR), the regulators for histidine utilization in Pseudomonas putida (HutCPp) and Klebsiella aerogenes (HutCKa), the repressor (FadR) of fatty acid degradation in Escherichia coli, a regulator involved in the conjugal transfer of the broad host range plasmid pIJ101 (KorA), and three proteins of unidentified function in E. coli (GenA, P30 and PhnF). The proteins share amino acid sequence similarities in a 69-residue N-terminal region. A helix-turn-helix motif is predicted in the most highly-conserved segment of each protein suggesting that they are members of a new family of helix-turn-helix DNA-binding proteins.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2060763 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || A new family of bacterial regulatory proteins has been identified by sequence similarity. The family contains the repressor of the Bacillus subtilis gluconate operon (GntR), the regulators for histidine utilization in Pseudomonas putida (HutCPp) and Klebsiella aerogenes (HutCKa), the repressor (FadR) of fatty acid degradation in Escherichia coli, a regulator involved in the conjugal transfer of the broad host range plasmid pIJ101 (KorA), and three proteins of unidentified function in E. coli (GenA, P30 and PhnF). The proteins share amino acid sequence similarities in a 69-residue N-terminal region. A helix-turn-helix motif is predicted in the most highly-conserved segment of each protein suggesting that they are members of a new family of helix-turn-helix DNA-binding proteins.
!align=left  |Keywords
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Amino Acid Sequence; Bacteria/genetics; Bacterial Proteins/genetics; Base Sequence; Consensus Sequence; DNA-Binding Proteins/genetics; Databases, Factual; Genes, Regulator; Molecular Sequence Data; Plasmids; Protein Conformation; Repressor Proteins/genetics; Sequence Homology, Nucleic Acid; Transcription Factors/genetics
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2060763 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 19:10, 1 September 2013

Citation

No author listed (1991) A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 63:291-5

Abstract

A new family of bacterial regulatory proteins has been identified by sequence similarity. The family contains the repressor of the Bacillus subtilis gluconate operon (GntR), the regulators for histidine utilization in Pseudomonas putida (HutCPp) and Klebsiella aerogenes (HutCKa), the repressor (FadR) of fatty acid degradation in Escherichia coli, a regulator involved in the conjugal transfer of the broad host range plasmid pIJ101 (KorA), and three proteins of unidentified function in E. coli (GenA, P30 and PhnF). The proteins share amino acid sequence similarities in a 69-residue N-terminal region. A helix-turn-helix motif is predicted in the most highly-conserved segment of each protein suggesting that they are members of a new family of helix-turn-helix DNA-binding proteins.

Links

PubMed

Keywords

Amino Acid Sequence; Bacteria/genetics; Bacterial Proteins/genetics; Base Sequence; Consensus Sequence; DNA-Binding Proteins/genetics; Databases, Factual; Genes, Regulator; Molecular Sequence Data; Plasmids; Protein Conformation; Repressor Proteins/genetics; Sequence Homology, Nucleic Acid; Transcription Factors/genetics

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Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status
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