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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
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Escherichia coli K-12 substr. MG1655 Transporter: ferric enterobactin outer membrane transport complex

Component of: ferric enterobactin transport system (summary available)

Subunit composition of ferric enterobactin outer membrane transport complex = [(TonB)(ExbB)(ExbD)][FepA]
         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)
         ferric enterobactin / colicin B / colicin D outer membrane porin FepA = FepA (summary available)

Gene-Reaction Schematic: ?


Enzymatic reaction of: transport of ferric enterobactin (ferric enterobactin outer membrane transport complex)


Subunit of: ferric enterobactin transport system

Subunit composition of ferric enterobactin transport system = [(FepC)2(FepD)(FepG)(FepB)][([TonB][ExbB][ExbD])(FepA)]
         ferric enterobactin ABC transporter = (FepC)2(FepD)(FepG)(FepB) (extended summary available)
                 ferric enterobactin ABC transporter - ATP binding subunit = FepC (extended summary available)
                 ferric enterobactin ABC transporter - membrane subunit = FepD
                 ferric enterobactin ABC transporter - membrane subunit = FepG
                 ferric enterobactin ABC transporter - periplasmic binding protein = FepB
         ferric enterobactin outer membrane transport complex = ([TonB][ExbB][ExbD])(FepA)
                 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)
                 ferric enterobactin / colicin B / colicin D outer membrane porin FepA = FepA (summary available)

Summary:
FepA is a 22-stranded membrane-spanning beta barrel protein in the outer membrane. FepA is a TonB dependent active transporter that recognizes ferric enterobactin and translocates the molecule across the outer membrane into the periplasm. FepB is a periplasmic binding protein that binds ferric enterobactin for transport across the inner membrane by the FepCDG ABC transporter.

Locations: outer membrane, inner membrane, periplasmic space

GO Terms:

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


Enzymatic reaction of: ferric enterobactin transport


Subunit of ferric enterobactin 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 [UniProtGOA11, GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
GO:0015891 - siderophore transport Author statement [Braun95]
GO:0042914 - colicin transport Author statement [Braun95]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11]
GO:0044718 - siderophore transmembrane transport Inferred by computational analysis [GOA01]
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 [GOA01, Letain97, Bassford76]
GO:0015343 - siderophore transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Postle88]
GO:0031233 - intrinsic component of external side of plasma membrane Inferred from experiment [Skare93]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [GOA01, 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 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

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 [UniProtGOA11, GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11]
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 [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05, Letain97]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

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 4]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

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 [UniProtGOA11, GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
GO:0043213 - bacteriocin transport Inferred by computational analysis [UniProtGOA11]
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 [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Letain97]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

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 4]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Subunit of ferric enterobactin outer membrane transport complex: ferric enterobactin / colicin B / colicin D outer membrane porin FepA

Synonyms: Fep, Cbt, Cbr, FeuB, FepA

Gene: fepA Accession Numbers: EG10293 (EcoCyc), b0584, ECK0576

Locations: outer membrane

Sequence Length: 746 AAs

Molecular Weight: 82.107 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0015685 - ferric-enterobactin transport Inferred from experiment [Armstrong90]
GO:0042914 - colicin transport Inferred from experiment [Armstrong90]
GO:0055085 - transmembrane transport Inferred from experiment [Rutz92]
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:0005515 - protein binding Inferred from experiment [Brinkman08, VakhariaRao07]
GO:0015620 - ferric-enterobactin transmembrane transporter activity Inferred from experiment [Armstrong90]
GO:0022834 - ligand-gated channel activity Inferred from experiment [Rutz92]
GO:0042912 - colicin transmembrane transporter activity Inferred from experiment [Armstrong90]
GO:0004872 - receptor activity Inferred by computational analysis [GOA01]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01]
GO:0005506 - iron ion binding 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, Han12, Molloy00]
GO:0045203 - integral component of cell outer membrane Inferred from experiment [Buchanan99a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes adaptations Fe aquisition
extrachromosomal colicin related
transport Channel-type Transporters Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)

Unification Links: DIP:DIP-9592N , EcoliWiki:b0584 , ModBase:P05825 , PR:PRO_000022600 , Pride:P05825 , Protein Model Portal:P05825 , RefSeq:NP_415116 , SMR:P05825 , String:511145.b0584 , UniProt:P05825

Relationship Links: InterPro:IN-FAMILY:IPR000531 , InterPro:IN-FAMILY:IPR010105 , InterPro:IN-FAMILY:IPR010916 , InterPro:IN-FAMILY:IPR010917 , InterPro:IN-FAMILY:IPR012910 , PDB:Structure:1FEP , Pfam:IN-FAMILY:PF00593 , Pfam:IN-FAMILY:PF07715 , Prosite:IN-FAMILY:PS00430 , Prosite:IN-FAMILY:PS01156

Summary:
FepA is a protein involved with transport of enterobactin-iron across the outer membrane [Sansom99]. Its structure consists of a 22-strand antiparallel β-barrel and an N-terminal globular domain which folds into the barrel [Buchanan99a, Ma07]. FepA interacts with a TonB, ExbB, ExbD complex, linking the movement of ferric enterobactin from the environment into the periplasm with the proton gradient of the inner membrane, making this translocation an active process [Buchanan99a]. FepA is also involved with the passage of colicins B and D through the outer membrane [Cao02].

Proteomic analyses indicate that fepA is upregulated when E. coli cells are exposed to sea water [Muela08].

Essentiality data for fepA knockouts: ?

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

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

Armstrong90: Armstrong SK, Francis CL, McIntosh MA (1990). "Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA." J Biol Chem 265(24);14536-43. PMID: 2201687

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

Barnard01: Barnard TJ, Watson ME, McIntosh MA (2001). "Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport." Mol Microbiol 2001;41(3);527-36. PMID: 11532122

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

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

Buchanan99a: Buchanan SK, Smith BS, Venkatramani L, Xia D, Esser L, Palnitkar M, Chakraborty R, van der Helm D, Deisenhofer J (1999). "Crystal structure of the outer membrane active transporter FepA from Escherichia coli." Nat Struct Biol 1999;6(1);56-63. PMID: 9886293

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

Cao02: Cao Z, Klebba PE (2002). "Mechanisms of colicin binding and transport through outer membrane porins." Biochimie 84(5-6);399-412. PMID: 12423783

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

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."

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

Han12: Han MJ, Lee SY, Hong SH (2012). "Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains." J Microbiol Biotechnol 22(4);470-8. PMID: 22534293

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

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

Ma07: Ma L, Kaserer WA, Annamalai R, Scott DC, Jin B, Jiang X, Xiao Q, Maymani H, Massia LM, Ferreira LC, Newton SM, Klebba PE (2007). "Evidence of ball-and-chain transport of ferric enterobactin through FepA." J Biol Chem 282(1):397-406. PMID: 17056600

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

Muela08: Muela A, Seco C, Camafeita E, Arana I, Orruno M, Lopez JA, Barcina I (2008). "Changes in Escherichia coli outer membrane subproteome under environmental conditions inducing the viable but nonculturable state." FEMS Microbiol Ecol 64(1);28-36. PMID: 18318713

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

Pugsley76: Pugsley AP, Reeves P (1976). "Iron uptake in colicin B-resistant mutants of Escherichia coli K-12." J Bacteriol 126(3);1052-62. PMID: 7543

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

Rutz92: Rutz JM, Liu J, Lyons JA, Goranson J, Armstrong SK, McIntosh MA, Feix JB, Klebba PE (1992). "Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane." Science 258(5081);471-5. PMID: 1411544

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

Shea91: Shea CM, McIntosh MA (1991). "Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli." Mol Microbiol 1991;5(6);1415-28. PMID: 1838574

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

Sprencel00: Sprencel C, Cao Z, Qi Z, Scott DC, Montague MA, Ivanoff N, Xu J, Raymond KM, Newton SM, Klebba PE (2000). "Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB." J Bacteriol 182(19);5359-64. PMID: 10986237

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."

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

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


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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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