| pubmed-article:8576065 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0085486 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C1335671 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0033413 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C1706937 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:8576065 | lifeskim:mentions | umls-concept:C0178696 | lld:lifeskim |
| pubmed-article:8576065 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8576065 | pubmed:dateCreated | 1996-3-14 | lld:pubmed |
| pubmed-article:8576065 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8576065 | pubmed:abstractText | The fct cbsCEBA operon from the Erwinia chrysanthemi 3937 chrysobactin-dependent iron assimilation system codes for transport and biosynthetic functions. The sequence of the fct outer membrane receptor gene was determined. The fct promoter region displays a strong resemblance to the Escherichia coli bidirectional intercistronic region controlling the expression of the fepA-entD and fes-entF operons. An apparent Fur-binding site was shown to confer iron regulation on an fct::lac fusion expressed on a low-copy-number plasmid in a Fur-proficient E. coli strain. The fct gene consists of an open reading frame encoding a 735-amino-acid polypeptide with a signal sequence of 38 residues. The Fct protein has 36% sequence homology with the E. coli ferrichrome receptor FhuA and the Yersinia enterocolitica ferrioxamine receptor FoxA. On the basis of secondary-structure predictions and these homologies, we propose a two-dimensional folding model for Fct. | lld:pubmed |
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| pubmed-article:8576065 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8576065 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8576065 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8576065 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8576065 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8576065 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:8576065 | pubmed:author | pubmed-author:SauvageCC | lld:pubmed |
| pubmed-article:8576065 | pubmed:author | pubmed-author:ExpertDD | lld:pubmed |
| pubmed-article:8576065 | pubmed:author | pubmed-author:FranzaTT | lld:pubmed |
| pubmed-article:8576065 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8576065 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:8576065 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8576065 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8576065 | pubmed:pagination | 1227-31 | lld:pubmed |
| pubmed-article:8576065 | pubmed:dateRevised | 2010-10-19 | lld:pubmed |
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