Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Transporter: 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)

Gene-Reaction Schematic: ?

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


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


Component enzyme of ferric coprogen transport system : iron (III) hydroxamate ABC transporter

Catalyzes:
ATP + a ferric hydroxamate complex[periplasmic space] + H2O → ADP + a ferric hydroxamate complex[cytosol] + phosphate

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].


Subunit of iron (III) hydroxamate ABC transporter: iron (III) hydroxamate ABC transporter - ATP binding subunit

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

Locations: inner membrane

Sequence Length: 265 AAs

Molecular Weight: 28.886 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01a]
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 [GOA01]
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, GOA01a]
GO:0015623 - iron-chelate-transporting ATPase activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a]
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

Unification Links: EcoliWiki:b0151 , ModBase:P07821 , PR:PRO_000022611 , Pride:P07821 , Protein Model Portal:P07821 , RefSeq:NP_414693 , 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

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: iron (III) hydroxamate ABC transporter - membrane subunit

Gene: fhuB Accession Numbers: EG10303 (EcoCyc), b0153, ECK0152

Locations: inner membrane

Sequence Length: 660 AAs

Molecular Weight: 70.423 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005215 - transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
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, membrane component

Unification Links: DIP:DIP-9603N , EcoliWiki:b0153 , Mint:MINT-1304500 , ModBase:P06972 , PR:PRO_000022610 , Pride:P06972 , Protein Model Portal:P06972 , RefSeq:NP_414695 , SMR:P06972 , String:511145.b0153 , UniProt:P06972

Relationship Links: InterPro:IN-FAMILY:IPR000522 , Pfam:IN-FAMILY:PF01032

Essentiality data for fhuB 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: iron (III) hydroxamate ABC transporter - periplasmic binding protein

Gene: fhuD Accession Numbers: EG10305 (EcoCyc), b0152, ECK0151

Locations: periplasmic space

Sequence Length: 296 AAs

Molecular Weight: 32.998 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processes adaptations Fe aquisition
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, periplasmic binding component

Unification Links: EcoliWiki:b0152 , ModBase:P07822 , PR:PRO_000022612 , Pride:P07822 , Protein Model Portal:P07822 , RefSeq:NP_414694 , SMR:P07822 , String:511145.b0152 , UniProt:P07822

Relationship Links: InterPro:IN-FAMILY:IPR002491 , InterPro:IN-FAMILY:IPR008091 , PDB:Structure:1EFD , PDB:Structure:1ESZ , PDB:Structure:1K2V , PDB:Structure:1K7S , Pfam:IN-FAMILY:PF01497 , Prints:IN-FAMILY:PR01715 , Prosite:IN-FAMILY:PS50983 , Prosite:IN-FAMILY:PS51318

Summary:
Fhu D is the periplasmic siderophore binding component of the iron III hydroxamate ABC transporter. The crystal structure of E.coli FhuD bound to gallichrome has been determined at 1.9Å resolution [Clarke00, Clarke02].

Essentiality data for fhuD 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]

Component enzyme of ferric coprogen transport system : ferric coprogen outer membrane transport complex

Locations: periplasmic space, outer membrane, inner membrane

GO Terms:

Cellular Component: GO:0005886 - plasma membrane
GO:0009279 - cell outer membrane
GO:0030288 - outer membrane-bounded periplasmic space

Catalyzes:
ferric coprogen[extracellular space] → ferric coprogen[periplasmic space]


Subunit of ferric coprogen outer membrane transport complex: ferric coprogen outer membrane porin FhuE

Synonyms: FhuE

Gene: fhuE Accession Numbers: EG10306 (EcoCyc), b1102, ECK1088

Locations: outer membrane

Sequence Length: 729 AAs

Molecular Weight: 81.232 kD (from nucleotide sequence)

Molecular Weight: 76.0 kD (experimental) [Sauer87]

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0044718 - siderophore transmembrane transport Inferred by computational analysis [GOA01a]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004872 - receptor activity Inferred by computational analysis [GOA01a]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01a]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA01a]
GO:0015343 - siderophore transmembrane transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Molloy00, Hantke83]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes adaptations Fe aquisition
metabolism central intermediary metabolism incorporation of metal ions
transport Channel-type Transporters Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)

Unification Links: EcoliWiki:b1102 , ModBase:P16869 , PR:PRO_000022613 , Pride:P16869 , Protein Model Portal:P16869 , RefSeq:NP_415620 , SMR:P16869 , String:511145.b1102 , UniProt:P16869

Relationship Links: InterPro:IN-FAMILY:IPR000531 , InterPro:IN-FAMILY:IPR010105 , InterPro:IN-FAMILY:IPR010916 , InterPro:IN-FAMILY:IPR010917 , InterPro:IN-FAMILY:IPR012910 , Pfam:IN-FAMILY:PF00593 , Pfam:IN-FAMILY:PF07715 , Prosite:IN-FAMILY:PS00430 , Prosite:IN-FAMILY:PS01156

Summary:
FhuE is a protein which serves as a receptor for ferric-coprogen (a hydroxamate-type iron chelator) and ferric-rhodotorulic acid [Sauer87]. Mutants lacking FhuE are unable to grow with coprogen, ferrioxamine B, ferrioxamine D1 or rhodotorulic acid [Hantke83]. Uptake into the periplasm is facilitated by TonB coupling of inner membrane energy to power specific uptake across the outer membrane [Bitter94]. Coprogen iron uptake is dependent on tonB, exbB and fhuCDB [Hantke83]. FhuE appears to have a preference for Δ-absolute configuration metal complexes [Matzanke84].

Essentiality data for fhuE 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 ferric coprogen outer membrane transport complex: TonB energy transducing system

Locations: inner membrane, periplasmic space

GO Terms:

Biological Process: GO:0015682 - ferric iron transport Inferred from experiment [Gresock11]
GO:0015889 - cobalamin transport Inferred from experiment [Bassford76]
Molecular Function: GO:0031992 - energy transducer activity Inferred from experiment [Letain97]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Skare93]
GO:0042597 - periplasmic space Inferred from experiment [Postle88]

Summary:
TonB is a cytoplasmic membrane protein which transduces the proton motive force (pmf) of the cytoplasmic membrane to the outer membrane active transporters thus providing the energy source required for the import of iron-siderophore complexes and vitamin B12 across the outer membrane [Letain97]. The amino-terminal signal sequence of TonB is thought to span the cytoplasmic membrane, with the rest of the protein residing within the periplasmic space [Karlsson93]. TonB has been shown to come into close contact with proteins located in both membranes [Skare93]. Sucrose density gradient centrifugation studies found that TonB is distributed approximately equally in the inner and outer membrane fractions [Letain97]. In conjunction with cytoplasmic membrane proteins ExbB and ExbD, TonB forms an energy transduction complex which interacts with a variety of outer membrane active transporter proteins [Braun02]. When complexed with ExbB and ExbD, TonB is thought to adopt an energized conformation which is subsequently released from the cytoplasmic membrane to the outer membrane whereupon it interacts with an array of outer membrane proteins [Higgs02]. TonB is then thought to respond to the conformational changes induced in the active transport proteins upon substrate binding [Moeck97], releasing its stored energy to the active transporters and reassociating with ExbB and ExbD at the cytoplasmic membrane to be re-energized [Larsen03].


Subunit of TonB energy transducing system: TonB energy transducing system - TonB subunit

Synonyms: ExbA, TonB

Gene: tonB Accession Numbers: EG11012 (EcoCyc), b1252, ECK1246

Locations: periplasmic space, inner membrane

Sequence Length: 239 AAs

Molecular Weight: 26.094 kD (from nucleotide sequence)

Molecular Weight: 25.0 kD (experimental) [James09]

GO Terms:

Biological Process: GO:0015889 - cobalamin transport Inferred from experiment [Cadieux02, Bassford76]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0015891 - siderophore transport Author statement [Braun95]
GO:0042914 - colicin transport Author statement [Braun95]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11a]
GO:0044718 - siderophore transmembrane transport Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Ollis12, Ollis12a, Ollis11, Brinkman08, VakhariaRao07, James09]
GO:0031992 - energy transducer activity Inferred from experiment Inferred by computational analysis [GOA01a, Letain97, Bassford76]
GO:0015343 - siderophore transmembrane transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Postle88]
GO:0031233 - intrinsic component of external side of plasma membrane Inferred from experiment [Skare93]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [GOA01a, DiazMejia09]

MultiFun Terms: cell structure membrane
extrachromosomal prophage genes and phage related functions

Unification Links: DIP:DIP-11010N , DIP:DIP-48111N , DisProt:DP00043 , EcoliWiki:b1252 , ModBase:P02929 , PR:PRO_000024083 , Pride:P02929 , Protein Model Portal:P02929 , RefSeq:NP_415768 , SMR:P02929 , UniProt:P02929

Relationship Links: InterPro:IN-FAMILY:IPR003538 , InterPro:IN-FAMILY:IPR006260 , PDB:Structure:1IHR , PDB:Structure:1QXX , PDB:Structure:1U07 , PDB:Structure:1XX3 , PDB:Structure:2GRX , PDB:Structure:2GSK , Pfam:IN-FAMILY:PF03544 , Prints:IN-FAMILY:PR01374

Summary:
TonB is a cytoplasmic membrane protein which transduces the proton motive force (pmf) of the cytoplasmic membrane to the outer membrane active transporters thus providing the energy source required for the import of iron-siderophore complexes and vitamin B12 across the outer membrane [Letain97]. TonB functions as part of an energy transduction complex with ExbB and ExbD [Braun02].

TonB induces conformational changes in outer exposed-surface loops of the outer-membrane receptor FhuA, which promotes binding to and transport of hydroxamate-type siderophores into the periplasm [James08]. TonB also interacts with the periplasmic binding protein BtuF. This interaction has a stoichiometry of 1:1 and is independent of cyanocobalamin binding by BtuF [James09].

Hybrid protein studies indicate that the TonB N terminus remains associated with the inner membrane, while the downstream region bridges the cell envelope due to the affinity of the C terminus for peptidoglycan. This suggests that TonB searches for occupied receptor proteins from underneath the peptidoglycan-associated outer membrane proteins [Kaserer08].

The crystal structure of a 92-residue fragment of TonB (TonB-92) has been determined to 1.13 Å resolution [Kodding04].

Essentiality data for tonB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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 TonB energy transducing system: TonB energy transducing system - ExbB subunit

Synonyms: ExbB

Gene: exbB Accession Numbers: EG10271 (EcoCyc), b3006, ECK2999

Locations: inner membrane

Sequence Length: 244 AAs

Molecular Weight: 26.287 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0050821 - protein stabilization Inferred from experiment [Ahmer95]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Ollis12, Ollis11, Brinkman08, VakhariaRao07, Higgs98]
GO:0031992 - energy transducer activity Inferred from experiment [Letain97]
GO:0008565 - protein transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05, Letain97]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes adaptations Fe aquisition
cell structure membrane
transport Electrochemical potential driven transporters Ion-gradient-driven energizers

Unification Links: DIP:DIP-47841N , EcoliWiki:b3006 , PR:PRO_000022554 , Pride:P0ABU7 , Protein Model Portal:P0ABU7 , RefSeq:NP_417479 , String:511145.b3006 , UniProt:P0ABU7

Relationship Links: InterPro:IN-FAMILY:IPR002898 , InterPro:IN-FAMILY:IPR014164 , Pfam:IN-FAMILY:PF01618

Summary:
ExbB and ExbD proteins function as part of the TonB-dependent energy transduction system for the import of iron-siderophore complexes and vitamin B12 across the outer membrane. ExbB and ExbD are encoded by the exb operon in Escherichia coli [Held02].

Essentiality data for exbB 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 TonB energy transducing system: tonB energy transducing system - ExbD subunit

Synonyms: ExbD

Gene: exbD Accession Numbers: EG10272 (EcoCyc), b3005, ECK2998

Locations: inner membrane

Sequence Length: 141 AAs

Molecular Weight: 15.527 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0050821 - protein stabilization Inferred from experiment [Ahmer95]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Ollis12, Ollis12a, Ollis11]
GO:0031992 - energy transducer activity Inferred from experiment [Letain97]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Ollis12, Ollis11]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Letain97]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes adaptations Fe aquisition
transport Electrochemical potential driven transporters Ion-gradient-driven energizers

Unification Links: DIP:DIP-47973N , EcoliWiki:b3005 , PR:PRO_000022555 , Protein Model Portal:P0ABV2 , RefSeq:NP_417478 , SMR:P0ABV2 , String:511145.b3005 , UniProt:P0ABV2

Relationship Links: InterPro:IN-FAMILY:IPR003400 , InterPro:IN-FAMILY:IPR014170 , PDB:Structure:2PFU , Pfam:IN-FAMILY:PF02472

Summary:
ExbB and ExbD proteins function as part of the TonB-dependent energy transduction system for the import of iron-siderophore complexes and vitamin B12 across the outer membrane. ExbB and ExbD are encoded by the exb operon in Escherichia coli [Held02].

Essentiality data for exbD 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]

References

Ahmer95: Ahmer BM, Thomas MG, Larsen RA, Postle K (1995). "Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability." J Bacteriol 1995;177(16);4742-7. PMID: 7642501

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

Bassford76: Bassford PJ, Bradbeer C, Kadner RJ, Schnaitman CA (1976). "Transport of vitamin B12 in tonB mutants of Escherichia coli." J Bacteriol 128(1);242-7. PMID: 135755

Bitter94: Bitter W, van Leeuwen IS, de Boer J, Zomer HW, Koster MC, Weisbeek PJ, Tommassen J (1994). "Localization of functional domains in the Escherichia coli coprogen receptor FhuE and the Pseudomonas putida ferric-pseudobactin 358 receptor PupA." Mol Gen Genet 1994;245(6);694-703. PMID: 7830717

Braun02: Braun V, Braun M (2002). "Active transport of iron and siderophore antibiotics." Curr Opin Microbiol 5(2);194-201. PMID: 11934617

Braun95: Braun V (1995). "Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins." FEMS Microbiol Rev 16(4);295-307. PMID: 7654405

Brinkman08: Brinkman KK, Larsen RA (2008). "Interactions of the energy transducer TonB with noncognate energy-harvesting complexes." J Bacteriol 190(1);421-7. PMID: 17965155

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

Cadieux02: Cadieux N, Bradbeer C, Reeger-Schneider E, Koster W, Mohanty AK, Wiener MC, Kadner RJ (2002). "Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli." J Bacteriol 2002;184(3);706-17. PMID: 11790740

Clarke00: Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW (2000). "The structure of the ferric siderophore binding protein FhuD complexed with gallichrome." Nat Struct Biol 7(4);287-91. PMID: 10742172

Clarke02: Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ (2002). "X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin." J Biol Chem 277(16);13966-72. PMID: 11805094

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

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

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

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Gresock11: Gresock MG, Savenkova MI, Larsen RA, Ollis AA, Postle K (2011). "Death of the TonB Shuttle Hypothesis." Front Microbiol 2;206. PMID: 22016747

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

Held02: Held KG, Postle K (2002). "ExbB and ExbD do not function independently in TonB-dependent energy transduction." J Bacteriol 184(18);5170-3. PMID: 12193634

Higgs02: Higgs PI, Letain TE, Merriam KK, Burke NS, Park H, Kang C, Postle K (2002). "TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli." J Bacteriol 184(6);1640-8. PMID: 11872715

Higgs98: Higgs PI, Myers PS, Postle K (1998). "Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers." J Bacteriol 180(22);6031-8. PMID: 9811664

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

James09: James KJ, Hancock MA, Gagnon JN, Coulton JW (2009). "TonB Interacts with BtuF, the Escherichia coli periplasmic binding protein for cyanocobalamin." Biochemistry 48(39);9212-20. PMID: 19708689

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

Karlsson93: Karlsson M, Hannavy K, Higgins CF (1993). "A sequence-specific function for the N-terminal signal-like sequence of the TonB protein." Mol Microbiol 8(2);379-88. PMID: 8316087

Kaserer08: Kaserer WA, Jiang X, Xiao Q, Scott DC, Bauler M, Copeland D, Newton SM, Klebba PE (2008). "Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane." J Bacteriol 190(11);4001-16. PMID: 18390658

Kodding04: Kodding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W (2004). "Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments." J Biol Chem 280(4):3022-8. PMID: 15522863

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

Larsen03: Larsen RA, Letain TE, Postle K (2003). "In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli." Mol Microbiol 49(1);211-8. PMID: 12823822

Letain97: Letain TE, Postle K (1997). "TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli." Mol Microbiol 24(2);271-83. PMID: 9159515

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

Matzanke84: Matzanke BF, Muller GI, Raymond KN (1984). "Hydroxamate siderophore mediated iron uptake in E. coli: stereospecific recognition of ferric rhodotorulic acid." Biochem Biophys Res Commun 1984;121(3);922-30. PMID: 6234892

Moeck97: Moeck GS, Coulton JW, Postle K (1997). "Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor fhua promotes interaction with the energy-transducing protein TonB." J Biol Chem 272(45);28391-7. PMID: 9353297

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

Ollis11: Ollis AA, Postle K (2011). "The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers." J Bacteriol 193(24);6852-63. PMID: 21984795

Ollis12: Ollis AA, Kumar A, Postle K (2012). "The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization." J Bacteriol 194(12);3069-77. PMID: 22493019

Ollis12a: Ollis AA, Postle K (2012). "Identification of functionally important TonB-ExbD periplasmic domain interactions in vivo." J Bacteriol 194(12);3078-87. PMID: 22493017

Postle88: Postle K, Skare JT (1988). "Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus." J Biol Chem 263(22);11000-7. PMID: 2839513

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Sauer87: Sauer M, Hantke K, Braun V (1987). "Ferric-coprogen receptor FhuE of Escherichia coli: processing and sequence common to all TonB-dependent outer membrane receptor proteins." J Bacteriol 1987;169(5);2044-9. PMID: 3032906

Skare93: Skare JT, Ahmer BM, Seachord CL, Darveau RP, Postle K (1993). "Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA." J Biol Chem 268(22);16302-8. PMID: 8344918

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."

VakhariaRao07: Vakharia-Rao H, Kastead KA, Savenkova MI, Bulathsinghala CM, Postle K (2007). "Deletion and substitution analysis of the Escherichia coli TonB Q160 region." J Bacteriol 189(13);4662-70. PMID: 17483231

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

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111


Report Errors or Provide Feedback
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 Nov 27, 2014, biocyc13.