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Escherichia coli K-12 substr. MG1655 Polypeptide: iron (III) hydroxamate ABC transporter - ATP binding subunit



Gene: fhuC Accession Numbers: EG10304 (EcoCyc), b0151, ECK0150

Regulation Summary Diagram: ?

Component of:
iron (III) hydroxamate ABC transporter (extended summary available)
ferric coprogen transport system
ferrichrome transport system

Gene Citations: [Fecker83, Koster86, Burkhardt87]

Locations: inner membrane

Map Position: [169,778 -> 170,575] (3.66 centisomes)
Length: 798 bp / 265 aa

Molecular Weight of Polypeptide: 28.886 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000522 , CGSC:11187 , EchoBASE:EB0300 , EcoGene:EG10304 , EcoliWiki:b0151 , ModBase:P07821 , OU-Microarray:b0151 , PortEco:fhuC , PR:PRO_000022611 , Pride:P07821 , Protein Model Portal:P07821 , RefSeq:NP_414693 , RegulonDB:EG10304 , SMR:P07821 , String:511145.b0151 , UniProt:P07821

Relationship Links: InterPro:IN-FAMILY:IPR003439 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR017871 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF00005 , Prosite:IN-FAMILY:PS00211 , Prosite:IN-FAMILY:PS50893 , Smart:IN-FAMILY:SM00382

In Paralogous Gene Group: 23 (75 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0015688 - iron chelate transport Inferred by computational analysis [GOA01a]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0015623 - iron-chelate-transporting ATPase activity Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily ATP binding cytoplasmic component

Essentiality data for fhuC 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: iron (III) hydroxamate ABC transporter

Subunit composition of iron (III) hydroxamate ABC transporter = [FhuC]2[FhuB]2[FhuD]
         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)

Component of:
ferric coprogen transport system
ferrichrome transport system

Summary:
The FhuCDB ATP-dependent iron (III) hydroxamate transporter is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Wu95]. FhuCDB catalyzes transport of iron (III)-hydroxamate compounds across the inner membrane into the cytoplasm of E. coli. Hydroxamates or siderophores are used to increase the solubility of iron (III), which is normally insoluble at pH 7 [Burkhardt87]. Based on sequence similarity, FhuB is the transmembrane component [Mademidis97], FhuC is the ATP-binding subunit [Coulton87], and FhuD is the periplasmic siderophore-binding component of the ABC transporter [Mademidis98]. A mutant with overproduced periplasmic FhuD protein was shown to bind to radioactively labeled iron (III) ferrichrome [Koster91]. Resistance of FhuD to protease K in the presence of ferrichrome, aerobactin, and coprogen also indicated binding of these substrates to FhuD [Koster91]. In E. coli, hydroxamate transport across the outer membrane (via FhuA and the TonB-ExbB-ExbD complex), coupled with the FhuBCD-mediated hydroxamate transport across the cytoplasmic membrane completes the uptake of iron (III) hydroxamates into the cell. fhuA-fhuB mutants exhibited completely abolished growth promotion by natural hydroxamates [Gaspar99].


Enzymatic reaction of: transport of iron (III) hydroxamate (iron (III) hydroxamate ABC transporter)

EC Number: 3.6.3.34


Subunit of: ferric coprogen transport system

Subunit composition of ferric coprogen transport system = [(FhuC)2(FhuB)2(FhuD)][(FhuE)([TonB][ExbB][ExbD])]
         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)
         ferric coprogen outer membrane transport complex = (FhuE)([TonB][ExbB][ExbD])
                 ferric coprogen outer membrane porin FhuE = FhuE (summary available)
                 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)

Credits:
Created 30-Oct-2011 by Mackie A , Macquarie University


Enzymatic reaction of: transport of ferric coprogen (ferric coprogen transport system)


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
Conserved-Region 12 -> 248
[UniProt09]
UniProt: ABC transporter;
Sequence-Conflict 31
[Burkhardt87, UniProt10]
Alternate sequence: S → C; UniProt: (in Ref. 2; CAA29254);
Nucleotide-Phosphate-Binding-Region 44 -> 51
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Nucleotide-Phosphate-Binding-Region 168 -> 179
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 226 -> 249
[Coulton87, Fujita94, UniProt10]
Alternate sequence: MIAQGTPAEIMRGETLEMIYGIPM → SDCSGNACGNYARRNPRNDLWHPD; UniProt: (in Ref. 1 and 3);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0151 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10304; confirmed by SwissProt match.


References

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

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

Coulton87: Coulton JW, Mason P, Allatt DD (1987). "fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12." J Bacteriol 1987;169(8);3844-9. PMID: 3301821

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

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."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Hantke83: Hantke K (1983). "Identification of an iron uptake system specific for coprogen and rhodotorulic acid in Escherichia coli K12." Mol Gen Genet 191(2);301-6. PMID: 6353165

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

Mademidis97: Mademidis A, Killmann H, Kraas W, Flechsler I, Jung G, Braun V (1997). "ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping." Mol Microbiol 1997;26(5);1109-23. PMID: 9426146

Mademidis98: Mademidis A, Koster W (1998). "Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake." Mol Gen Genet 1998;258(1-2);156-65. PMID: 9613584

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.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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

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

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
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc13.