Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Fe(III)-mediated cellular toxicity.
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The PmrA/PmrB system protects Enterobacteriaceae from Fe(III)-mediated outer-membrane toxicity, providing the regulatory context for arn induction rather than direct evidence that ArnE senses Fe(III).
"Fe(III) exhibits microbicidal activity towards strains of Salmonella enterica, Escherichia coli and Klebsiella pneumoniae defective in the Fe(III)-responding PmrA/PmrB signal transduction system"
A Genome-wide view of the Escherichia coli BasS-BasR two-component system implicated in iron-responses.
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External iron induces the E. coli yfbE/arn operon through the BasS-BasR two-component system.
"First we showed that the hypothetical yfbE operon that appears to be implicated in the modification of lipopolysaccharides is regulated at the level of transcription in response to external iron"
Global topology analysis of the Escherichia coli inner membrane proteome.
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ArnE's inner-membrane topology is covered by the E. coli C-terminal GFP/PhoA topology map.
"Using C-terminal tagging with the alkaline phosphatase and green fluorescent protein, we established the periplasmic or cytoplasmic locations of the C termini for 601 inner membrane proteins"
An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.
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Inactivating arnE/pmrL causes a loss of L-Ara4N-modified lipid A species.
"In the pmrL or pmrM deletion mutants, over 95% of each of the L-Ara4N-modified lipid A species was missing"
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ArnE is required for periplasmic accessibility of undecaprenyl phosphate-alpha-L-Ara4N, the lipid-linked L-Ara4N donor.
"At the 4-h time point, there was a 4-5-fold reduction in ratio of the monoisotopic peak areas for biotinylated undecaprenyl phosphate-alpha-L-Ara4N compared with unmodified undecaprenyl phosphate-alpha-L-Ara4N"
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ArnE/PmrL and ArnF/PmrM were proposed as subunits of the undecaprenyl phosphate-alpha-L-Ara4N flippase.
"PmrL and PmrM could specifically function to flip undecaprenyl phosphate-alpha-L-Ara4N from the cytosolic to the periplasmic side of the inner membrane, possibly functioning as a heterodimer"