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PMID: 9683481 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Identification of a new site for ferrichrome transport by comparison of the FhuA proteins of Escherichia coli, Salmonella paratyphi B, Salmonella typhimurium, and Pantoea agglomerans.

Journal of bacteriology ·Vol. 180 ·No. 15 ·1998-08-00 ·Pages 3845-52

Killmann H, Herrmann C, Wolff H, Braun V

Abstract

The fhuA genes of Salmonella paratyphi B, Salmonella typhimurium, and Pantoea agglomerans were sequenced and compared with the known fhuA sequence of Escherichia coli. The highly similar FhuA proteins displayed the largest difference in the predicted gating loop, which in E. coli controls the permeability of the FhuA channel and serves as the principal binding site for the phages T1, T5, and phi80. All the FhuA proteins contained the region in the gating loops required in E. coli for ferrichrome and albomycin transport. The three subdomains required for phage binding were contained in the gating loop of S. paratyphi B which is infected by the E. coli phages, whereas two of the subdomains were deleted in S. typhimurium and P. agglomerans which are resistant to the E. coli phages. Small deletions in a surface loop adjacent to the gating loop, residues 236 to 243 and 236 to 248, inactivated E. coli FhuA with regard to transport of ferrichrome and albomycin, but sensitivity to T1 and T5 was fully retained and sensitivity to phi80 and colicin M was reduced 10-fold. Full-size FhuA hybrid proteins of S. paratyphi B and S. typhimurium displayed S. paratyphi B FhuA activity when the hybrids contained two-thirds of either the N- or the C-terminal portions of S. paratyphi B and displayed S. typhimurium FhuA activity to phage ES18 when the hybrid contained two-thirds of the N-terminal region of the S. typhimurium FhuA. The central segment of the S. paratyphi B FhuA flanked on both sides by S. typhimurium FhuA regions conferred full sensitivity only to phage T5. The data support the essential role of the gating loop for the transport of ferrichrome and albomycin, identified an additional loop for ferrichrome and albomycin uptake, and suggest that several segments and their proper conformation, determined by the entire FhuA protein, contribute to the multiple FhuA activities.

MeSH Terms
Amino Acid Sequence Bacterial Outer Membrane Proteins/chemistry,genetics,metabolism Bacteriophages/physiology Biological Transport Cell Membrane Permeability Cosmids Enterobacteriaceae/metabolism Escherichia coli/genetics,metabolism Escherichia coli Proteins Ferrichrome/metabolism Kinetics Molecular Sequence Data Plasmids Receptors, Virus/chemistry,genetics,metabolism Recombinant Proteins/chemistry,metabolism Salmonella paratyphi A/metabolism Salmonella typhimurium/metabolism Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Bacterial Outer Membrane Proteins Escherichia coli Proteins FhuA protein, E coli Receptors, Virus Recombinant Proteins Ferrichrome
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Killmann H
Mikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany. [email protected]
Herrmann C
Wolff H
Braun V
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31 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.180.15.3845-3852.1998
Email
[email protected]
Published
1998-08-00
Pages
3845-52
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC107368
Subset
IM
Databases
GENBANK
Y14025, Y14026, Y14067
External Links
PubMed source DOI: 10.1128/JB.180.15.3845-3852.1998 PMC Full Text View journal details
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