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Escherichia coli K-12 substr. MG1655 Polypeptide: ferrichrome / phage / antibiotic outer membrane porin FhuA



Gene: fhuA Accession Numbers: EG10302 (EcoCyc), b0150, ECK0149

Synonyms: T1, T5rec, tonA

Regulation Summary Diagram: ?

Component of:
ferrichrome outer membrane transport complex
ferrichrome transport system

Summary:
FhuA is involved with the transport of ferrichrome across the outer membrane [Locher98]. It forms a monomeric channel consisting of a 22-strand, antiparallel β-barrel, obstructed by a "plug" formed by residues 19-159 [Locher98].

Conformational changes in outer exposed-surface loops of FhuA, brought about by TonB, promote the movement of siderophore-iron complexes across the outer membrane into the periplasm [James08, Sansom99]. TonB combined with ExbB and ExbD, also serves to couple this transport with the electrochemical gradient across the inner membrane, allowing for the accumulation of siderophore-iron against the concentration gradient, thereby making it an active process [Sansom99]. In addition to siderophore transport, FhuA also transports albomycin and rifamycin CGP 4832, and serves as a receptor for phages T5, T1, φ80, UC-1, and the peptides colicin M and microncin J25 [Braun02].

The 3 dimensional crystal structure of FhuA in both its native and siderophore associated conformation has been determined [Ferguson98, Ferguson00]. The crystal structure of FhuA associated with albomycin has been determined at 3.10Å resolution [Ferguson00].Targeting of FhuA to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].

Review: [Braun09]

Citations: [Samsonov02]

Gene Citations: [Fecker83, Koster86, Burkhardt87]

Locations: outer membrane

Map Position: [167,484 -> 169,727] (3.61 centisomes)
Length: 2244 bp / 747 aa

Molecular Weight of Polypeptide: 82.182 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000520 , CGSC:777 , DIP:DIP-9602N , EchoBASE:EB0298 , EcoGene:EG10302 , EcoliWiki:b0150 , ModBase:P06971 , OU-Microarray:b0150 , PortEco:fhuA , PR:PRO_000022609 , Pride:P06971 , Protein Model Portal:P06971 , RefSeq:NP_414692 , RegulonDB:EG10302 , SMR:P06971 , String:511145.b0150 , UniProt:P06971

Relationship Links: InterPro:IN-FAMILY:IPR000531 , InterPro:IN-FAMILY:IPR010105 , InterPro:IN-FAMILY:IPR010916 , InterPro:IN-FAMILY:IPR010917 , InterPro:IN-FAMILY:IPR012910 , PDB:Structure:1BY3 , PDB:Structure:1BY5 , PDB:Structure:1FCP , PDB:Structure:1FI1 , PDB:Structure:1QFF , PDB:Structure:1QFG , PDB:Structure:1QJQ , PDB:Structure:1QKC , PDB:Structure:2FCP , PDB:Structure:2GRX , Pfam:IN-FAMILY:PF00593 , Pfam:IN-FAMILY:PF07715 , Prosite:IN-FAMILY:PS00430 , Prosite:IN-FAMILY:PS01156

In Paralogous Gene Group: 51 (8 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0044718 - siderophore transmembrane transport Inferred by computational analysis [GOA01]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005506 - iron ion binding Inferred from experiment Inferred by computational analysis [GOA01, FaraldoGomez03]
GO:0015643 - toxic substance binding Inferred from experiment [Braun73]
GO:0046790 - virion binding Inferred from experiment [Braun73, Braun73a]
GO:0048037 - cofactor binding Inferred from experiment [FaraldoGomez03]
GO:0004872 - receptor activity Inferred by computational analysis [GOA01]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01]
GO:0015343 - siderophore transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Molloy00, LopezCampistrou05, Carmel90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: extrachromosomal colicin related
extrachromosomal prophage genes and phage related functions
transport Channel-type Transporters Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)

Essentiality data for fhuA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: ferrichrome outer membrane transport complex

Subunit composition of ferrichrome outer membrane transport complex = [(TonB)(ExbB)(ExbD)][FhuA]
         TonB energy transducing system = (TonB)(ExbB)(ExbD) (extended summary available)
                 TonB energy transducing system - TonB subunit = TonB (extended summary available)
                 TonB energy transducing system - ExbB subunit = ExbB (summary available)
                 tonB energy transducing system - ExbD subunit = ExbD (summary available)
         ferrichrome / phage / antibiotic outer membrane porin FhuA = FhuA (extended summary available)

Component of: ferrichrome transport system


Enzymatic reaction of: transport of ferrichrome (ferrichrome outer membrane transport complex)


Subunit of: ferrichrome transport system

Synonyms: iron (III) hydroxamate uptake system

Subunit composition of ferrichrome transport system = [(FhuC)2(FhuB)2(FhuD)][([TonB][ExbB][ExbD])(FhuA)]
         iron (III) hydroxamate ABC transporter = (FhuC)2(FhuB)2(FhuD) (extended summary available)
                 iron (III) hydroxamate ABC transporter - ATP binding subunit = FhuC
                 iron (III) hydroxamate ABC transporter - membrane subunit = FhuB
                 iron (III) hydroxamate ABC transporter - periplasmic binding protein = FhuD (summary available)
         ferrichrome outer membrane transport complex = ([TonB][ExbB][ExbD])(FhuA)
                 TonB energy transducing system = (TonB)(ExbB)(ExbD) (extended summary available)
                         TonB energy transducing system - TonB subunit = TonB (extended summary available)
                         TonB energy transducing system - ExbB subunit = ExbB (summary available)
                         tonB energy transducing system - ExbD subunit = ExbD (summary available)
                 ferrichrome / phage / antibiotic outer membrane porin FhuA = FhuA (extended summary available)

Citations: [Wu95]


Enzymatic reaction of: transport of ferrichrome (ferrichrome transport system)


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 33
[Coulton86, UniProt11]
.
Chain 34 -> 747
[UniProt09]
UniProt: Ferrichrome-iron receptor;
Protein-Segment 40 -> 47
[UniProt10]
UniProt: TonB box; Sequence Annotation Type: short sequence motif;
Amino-Acid-Sites-That-Bind 114
[UniProt10]
UniProt: Ferrichrome;
Amino-Acid-Sites-That-Bind 133
[UniProt10]
UniProt: Ferrichrome;
Protein-Segment 148 -> 149
[UniProt10a]
UniProt: Ferrichrome binding; Sequence Annotation Type: region of interest;
Transmembrane-Region 193 -> 201
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 207 -> 215
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 223 -> 231
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 246 -> 255
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 260 -> 268
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Sites-That-Bind 277
[UniProt10]
UniProt: Ferrichrome;
Amino-Acid-Sites-That-Bind 279
[UniProt10]
UniProt: Ferrichrome;
Transmembrane-Region 313 -> 321
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 327 -> 335
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Sites-That-Bind 346
[UniProt10]
UniProt: Ferrichrome;
Amino-Acid-Sites-That-Bind 348
[UniProt10]
UniProt: Ferrichrome;
Disulfide-Bond-Site 362, 351
[UniProt10]
Transmembrane-Region 388 -> 396
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 405 -> 413
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Sites-That-Bind 424
[UniProt10]
UniProt: Ferrichrome;
Transmembrane-Region 465 -> 473
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 478 -> 486
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 509 -> 517
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 523 -> 531
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 552 -> 560
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 566 -> 574
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 602 -> 610
[UniProt10]
UniProt: Beta stranded;
Sequence-Conflict 609 -> 610
[Fujita94, UniProt10]
Alternate sequence: AA → RP; UniProt: (in Ref. 2);
Transmembrane-Region 614 -> 622
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 646 -> 654
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 662 -> 670
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 690 -> 698
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 706 -> 714
[UniProt10]
UniProt: Beta stranded;
Disulfide-Bond-Site 731, 725
[UniProt10]
Protein-Segment 730 -> 747
[UniProt10]
UniProt: TonB C-terminal box; Sequence Annotation Type: short sequence motif;
Amino-Acid-Sites-That-Bind 735
[UniProt10]
UniProt: Ferrichrome;
Sequence-Conflict 737
[Burkhardt87, UniProt10]
Alternate sequence: R → P; UniProt: (in Ref. 6; CAA29253);
Transmembrane-Region 738 -> 746
[UniProt10]
UniProt: Beta stranded;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0150 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10302; confirmed by SwissProt match.


References

Baars06: Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW (2006). "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics." J Biol Chem 281(15);10024-34. PMID: 16352602

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Braun02: Braun M, Killmann H, Maier E, Benz R, Braun V (2002). "Diffusion through channel derivatives of the Escherichia coli FhuA transport protein." Eur J Biochem 2002;269(20);4948-59. PMID: 12383253

Braun09: Braun V (2009). "FhuA (TonA), the career of a protein." J Bacteriol 191(11);3431-6. PMID: 19329642

Braun73: Braun V, Schaller K, Wolff H (1973). "A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B." Biochim Biophys Acta 323(1);87-97. PMID: 4584483

Braun73a: Braun V, Wolff H (1973). "Characterization of the receptor protein for phage T5 and colicin M in the outer membrane of E. coli B." FEBS Lett 34(1);77-80. PMID: 4580999

Burkhardt87: Burkhardt R, Braun V (1987). "Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins." Mol Gen Genet 1987;209(1);49-55. PMID: 2823072

Carmel90: Carmel G, Hellstern D, Henning D, Coulton JW (1990). "Insertion mutagenesis of the gene encoding the ferrichrome-iron receptor of Escherichia coli K-12." J Bacteriol 172(4);1861-9. PMID: 2156805

Coulton86: Coulton JW, Mason P, Cameron DR, Carmel G, Jean R, Rode HN (1986). "Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12." J Bacteriol 1986;165(1);181-92. PMID: 3079747

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

FaraldoGomez03: Faraldo-Gomez JD, Smith GR, Sansom MS (2003). "Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states." Biophys J 85(3);1406-20. PMID: 12944258

Fecker83: Fecker L, Braun V (1983). "Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli." J Bacteriol 1983;156(3);1301-14. PMID: 6315685

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Ferguson00: Ferguson AD, Braun V, Fiedler HP, Coulton JW, Diederichs K, Welte W (2000). "Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA." Protein Sci 9(5);956-63. PMID: 10850805

Ferguson98: Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W (1998). "Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide." Science 282(5397);2215-20. PMID: 9856937

Fujita94: Fujita N, Mori H, Yura T, Ishihama A (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22(9);1637-9. PMID: 8202364

Gaspar99: Gaspar M, Santos MA, Krauter K, Winkelmann G (1999). "Molecular recognition of synthetic siderophore analogues: a study with receptor-deficient and fhu(A-B) deletion mutants of Escherichia coli." Biometals 1999;12(3);209-18. PMID: 10581683

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hantke75: Hantke K, Braun V (1975). "Membrane receptor dependent iron transport in Escherichia coli." FEBS Lett 49(3);301-5. PMID: 1089064

James08: James KJ, Hancock MA, Moreau V, Molina F, Coulton JW (2008). "TonB Induces Conformational Changes in Surface-exposed Loops of FhuA, Outer Membrane Receptor of Escherichia coli." Protein Sci NIL. PMID: 18653801

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Koster86: Koster W, Braun V (1986). "Iron hydroxamate transport of Escherichia coli: nucleotide sequence of the fhuB gene and identification of the protein." Mol Gen Genet 1986;204(3);435-42. PMID: 3020380

Koster91: Koster W (1991). "Iron(III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli." Biol Met 1991;4(1);23-32. PMID: 1830209

Locher98: Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, Moras D (1998). "Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes." Cell 1998;95(6);771-8. PMID: 9865695

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Molloy00: Molloy MP, Herbert BR, Slade MB, Rabilloud T, Nouwens AS, Williams KL, Gooley AA (2000). "Proteomic analysis of the Escherichia coli outer membrane." Eur J Biochem 267(10);2871-81. PMID: 10806384

Samsonov02: Samsonov VV, Samsonov VV, Sineoky SP (2002). "DcrA and dcrB Escherichia coli genes can control DNA injection by phages specific for BtuB and FhuA receptors." Res Microbiol 153(10);639-46. PMID: 12558182

Sansom99: Sansom MS (1999). "Membrane proteins: A tale of barrels and corks." Curr Biol 1999;9(7);R254-7. PMID: 10209114

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Wu95: Wu LF, Mandrand-Berthelot MA (1995). "A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions." Biochimie 1995;77(9);744-50. PMID: 8789466

Other References Related to Gene Regulation

Chen07: Chen Z, Lewis KA, Shultzaberger RK, Lyakhov IG, Zheng M, Doan B, Storz G, Schneider TD (2007). "Discovery of Fur binding site clusters in Escherichia coli by information theory models." Nucleic Acids Res 35(20);6762-77. PMID: 17921503

Hantke81: Hantke K (1981). "Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant." Mol Gen Genet 182(2);288-92. PMID: 7026976

Huerta03: Huerta AM, Collado-Vides J (2003). "Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals." J Mol Biol 333(2);261-78. PMID: 14529615


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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