rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1996-3-14
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pubmed:databankReference |
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1411544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1508046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1534324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1640832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1651239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1657869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1662760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1702781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1717434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1721242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1787788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-1848301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2066336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2075184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2139651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2156805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2162465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2201687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2257496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2536681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2551782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2914949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2963952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-2974033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3025450,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3079747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3294107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3294800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3340533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-3714490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-4358940,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-7688295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-8021177,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8576065-8596459
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ferric Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/FhuA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/FoxA protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/FoxB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Siderophores,
http://linkedlifedata.com/resource/pubmed/chemical/chrysobactin,
http://linkedlifedata.com/resource/pubmed/chemical/enterobactin receptor,
http://linkedlifedata.com/resource/pubmed/chemical/ferric uptake regulating proteins...,
http://linkedlifedata.com/resource/pubmed/chemical/tonB protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/tonB protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0021-9193
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
178
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1227-31
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pubmed:dateRevised |
2010-10-19
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pubmed:meshHeading |
|