Genetic organization of multiple fep genes encoding ferric enterobactin transport functions in Escherichia coli
- PMID: 2956250
- PMCID: PMC212444
- DOI: 10.1128/jb.169.8.3638-3646.1987
Genetic organization of multiple fep genes encoding ferric enterobactin transport functions in Escherichia coli
Abstract
Three genes were shown to provide functions specific for ferric enterobactin transport in Escherichia coli: fepA encoded the outer membrane receptor, fepB produced a periplasmic protein, and the fepC product was presumably a component of a cytoplasmic membrane permease system for this siderophore. A 10.6-kilobase-pair E. coli chromosomal EcoRI restriction fragment containing the fepB and fepC genes was isolated from a genomic library constructed in the vector pBR328. Both cistrons were localized on this clone (pITS24) by subcloning and deletion and insertion mutagenesis to positions that were separated by approximately 2.5 kilobases. Within this region, insertion mutations defining an additional ferric enterobactin transport gene (fepD) were isolated, and polarity effects from insertions into fepB suggested that fepD is encoded downstream on the same transcript. A 31,500-dalton FepC protein and a family of FepB polypeptides ranging from 34,000 to 37,000 daltons were identified in E. coli minicells, but the product of fepD was not detectable by this system. Another insertion mutation between entF and fepC was also shown to disrupt iron transport via enterobactin and thus defined the fepE locus; fepE weakly expressed a 43,000-dalton protein in minicells. It is proposed that these newly identified genes, fepD and fepE, provide functions which act in conjunction with the fepC product to form the ferric enterobactin-specific cytoplasmic membrane permease. An additional 44,000-dalton protein was identified and shown to be expressed from a gene that is situated between fepB and entE and that is transcribed in the direction opposite that of fepB. Although the function of this protein is uncharacterized, its membrane location suggests that it too may function in iron transport.
Similar articles
-
Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB.J Bacteriol. 2000 Oct;182(19):5359-64. doi: 10.1128/JB.182.19.5359-5364.2000. J Bacteriol. 2000. PMID: 10986237 Free PMC article.
-
Escherichia coli K-12 envelope proteins specifically required for ferrienterobactin uptake.J Bacteriol. 1986 Jun;166(3):930-6. doi: 10.1128/jb.166.3.930-936.1986. J Bacteriol. 1986. PMID: 3011753 Free PMC article.
-
Escherichia coli periplasmic protein FepB binds ferrienterobactin.Microbiology (Reading). 1995 Jul;141 ( Pt 7):1647-54. doi: 10.1099/13500872-141-7-1647. Microbiology (Reading). 1995. PMID: 7551033
-
Iron(III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli.Biol Met. 1991;4(1):23-32. doi: 10.1007/BF01135553. Biol Met. 1991. PMID: 1830209 Review.
-
Surface signaling: novel transcription initiation mechanism starting from the cell surface.Arch Microbiol. 1997 Jun;167(6):325-31. doi: 10.1007/s002030050451. Arch Microbiol. 1997. PMID: 9148773 Review.
Cited by
-
Transcriptional analysis reveals specific niche factors and response to environmental stresses of enterohemorrhagic Escherichia coli O157:H7 in bovine digestive contents.BMC Microbiol. 2021 Oct 19;21(1):284. doi: 10.1186/s12866-021-02343-7. BMC Microbiol. 2021. PMID: 34663220 Free PMC article.
-
The alternative role of enterobactin as an oxidative stress protector allows Escherichia coli colony development.PLoS One. 2014 Jan 2;9(1):e84734. doi: 10.1371/journal.pone.0084734. eCollection 2014. PLoS One. 2014. PMID: 24392154 Free PMC article.
-
A novel purification of ferric citrate receptor (FecA) from Escherichia coli UT5600 and further characterization of its binding activity.Biometals. 1993 Spring;6(1):37-44. doi: 10.1007/BF00154230. Biometals. 1993. PMID: 8471824
-
Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB.J Bacteriol. 2000 Oct;182(19):5359-64. doi: 10.1128/JB.182.19.5359-5364.2000. J Bacteriol. 2000. PMID: 10986237 Free PMC article.
-
Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA.J Bacteriol. 1989 Feb;171(2):784-90. doi: 10.1128/jb.171.2.784-790.1989. J Bacteriol. 1989. PMID: 2521621 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases