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Escherichia coli K-12 substr. MG1655 Transporter: The Colicin A Import System

Subunit composition of The Colicin A Import System = [BtuB][(OmpF)3][TolB]
         vitamin B12 / E colicin / bacteriophage BF23 outer membrane porin BtuB = BtuB (extended summary available)
         outer membrane protein F = (OmpF)3

Gene-Reaction Schematic: ?


Subunit of The Colicin A Import System: vitamin B12 / E colicin / bacteriophage BF23 outer membrane porin BtuB

Synonyms: Cer, Bfe, BtuB

Gene: btuB Accession Numbers: EG10126 (EcoCyc), b3966, ECK3958

Locations: outer membrane

Sequence Length: 614 AAs

Molecular Weight: 68.407 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0015889 - cobalamin transport Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Cadieux02]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0055085 - transmembrane transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004872 - receptor activity Inferred by computational analysis [GOA01]
GO:0005215 - transporter activity Inferred by computational analysis [GOA01]
GO:0015235 - cobalamin transporter activity Inferred by computational analysis [GOA06, GOA01]
GO:0015288 - porin activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009279 - cell outer membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]
GO:0046930 - pore complex Inferred by computational analysis [UniProtGOA11a]

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

Unification Links: DIP:DIP-9232N , EcoliWiki:b3966 , ModBase:P06129 , PR:PRO_000022234 , Pride:P06129 , Protein Model Portal:P06129 , RefSeq:NP_418401 , SMR:P06129 , String:511145.b3966 , UniProt:P06129

Relationship Links: InterPro:IN-FAMILY:IPR000531 , InterPro:IN-FAMILY:IPR010101 , InterPro:IN-FAMILY:IPR010916 , InterPro:IN-FAMILY:IPR010917 , InterPro:IN-FAMILY:IPR012910 , PDB:Structure:1NQE , PDB:Structure:1NQF , PDB:Structure:1NQG , PDB:Structure:1NQH , PDB:Structure:1UJW , PDB:Structure:2GSK , PDB:Structure:2GUF , PDB:Structure:2YSU , PDB:Structure:3M8B , PDB:Structure:3M8D , PDB:Structure:3RGM , PDB:Structure:3RGN , Pfam:IN-FAMILY:PF00593 , Pfam:IN-FAMILY:PF07715 , Prosite:IN-FAMILY:PS00430 , Prosite:IN-FAMILY:PS01156

Summary:
BtuB is an outer membrane porin that mediates binding and TonB-dependent active transport of vitamin B12 (cyanocobalamin) across the outer membrane. The system has a high affinity for vitamin B12 and its many derivatives including adenosylcobalamin and cobinamide [Bradbeer78, Roth96]. Calcium binding to BtuB induces high-affinity binding of cyanocobalamin. Several structures of this 22 strand beta barrel protein have been elucidated including a structure with bound calcium and cyanocobalamin [Chimento03]. The Ton box of BtuB unfolds and extends into the periplasm in the presence of substrate in order to initiate interaction with TonB so that transport can occur [Xu06a].

BtuB is also the receptor for group A colicins which enter by way of the Tol system. OmpF imports the cytotoxic domains of group A colicins E3 and N after the colicins bind to the BtuB receptor [Zakharov04, Zakharov06]. The presence of BtuB has been shown to be necessary for the cleavage of endonuclease colicin E2 (ColE2), and the associated cognate immunity protein (Im2) by OmpT [Duche09]. FRET analyses have shown that free energy for colicin unfolding is provided by binding of the R- domain to BtuB [Zakharov08]. BtuB production decreased in response to exogenous polyamines which are known to provide resistance to ColE7 [Pan06].

The crystal structure of BtuB has also been solved with the bound carboxy terminus of TonB to a resolution of 2.1 Å [Shultis06, Shultis06a], and alone to a resolution of 1.95 Å [Cherezov06].

Translation is down-regulated by coenzyme B(12) via a direct interaction between the compound and the 5'-untranslated region of the mRNA [Nahvi02].

Citations: [Cadieux03, Likhacheva96, Samsonov02]

Essentiality data for btuB 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 No 37 Aerobic 7   No [Baba06, Yamamoto09]

Component enzyme of The Colicin A Import System : outer membrane protein F

Synonyms: nfxB, tolF, cmlB, coa, cry, outer membrane porin OmpF, colB, outer membrane protein A1, outer membrane protein 1a, outer membrane protein 4, outer membrane protein b, outer membrane protein 0-9

Gene: ompF Accession Numbers: EG10671 (EcoCyc), b0929, ECK0920

Locations: outer membrane

Subunit composition of outer membrane protein F = [OmpF]3

Map Position: [985,117 <- 986,205] (21.23 centisomes)
Length: 1089 bp / 362 aa

Molecular Weight of Polypeptide: 39.333 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006855 - drug transmembrane transport Inferred from experiment [Harder81]
GO:0043213 - bacteriocin transport Inferred from experiment [Bourdineaud90]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0034220 - ion transmembrane transport Author statement [Nikaido85]
Molecular Function: GO:0015238 - drug transmembrane transporter activity Inferred from experiment [Harder81]
GO:0015288 - porin activity Inferred from experiment Author statement Inferred by computational analysis [UniProtGOA11a, GOA01, Nikaido85, Saint96]
GO:0042912 - colicin transmembrane transporter activity Inferred from experiment [Bourdineaud90]
GO:0015075 - ion transmembrane transporter activity Author statement [Nikaido85]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Han12a, Zhang07a, Molloy00, LopezCampistrou05, Palva78]
GO:0046930 - pore complex Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Cowan92]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: transport Channel-type Transporters Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)

Unification Links: DIP:DIP-10398N , EcoliWiki:b0929 , Mint:MINT-1511804 , ModBase:P02931 , PR:PRO_000023452 , Pride:P02931 , Protein Model Portal:P02931 , RefSeq:NP_415449 , SMR:P02931 , String:511145.b0929 , UniProt:P02931

Relationship Links: InterPro:IN-FAMILY:IPR001702 , InterPro:IN-FAMILY:IPR001897 , InterPro:IN-FAMILY:IPR013793 , InterPro:IN-FAMILY:IPR023614 , PDB:Structure:1BT9 , PDB:Structure:1GFM , PDB:Structure:1GFN , PDB:Structure:1GFO , PDB:Structure:1GFP , PDB:Structure:1GFQ , PDB:Structure:1HXT , PDB:Structure:1HXU , PDB:Structure:1HXX , PDB:Structure:1MPF , PDB:Structure:1OPF , PDB:Structure:2OMF , PDB:Structure:2ZFG , PDB:Structure:2ZLD , PDB:Structure:3FYX , PDB:Structure:3HW9 , PDB:Structure:3HWB , PDB:Structure:3K19 , PDB:Structure:3K1B , PDB:Structure:3POQ , PDB:Structure:3POU , PDB:Structure:3POX , PDB:Structure:4GCP , PDB:Structure:4GCQ , PDB:Structure:4GCS , Pfam:IN-FAMILY:PF00267 , Prints:IN-FAMILY:PR00182 , Prints:IN-FAMILY:PR00183 , Prosite:IN-FAMILY:PS00576

Catalyzes:
glycine betaine[extracellular space] ↔ glycine betaine[periplasmic space] ,
hydrophilic solute or ion < 600 Da[extracellular space] → hydrophilic solute or ion < 600 Da[periplasmic space]

Summary:
OmpF is a member of the General Bacterial Porin (GBP) family. X-ray crystallography has determined the three-dimensional structure of the OmpF porin to be a trimeric structure with each monomer consisting of 16 antiparallel β strands [Cowan92]. OmpF is tightly but noncovalently associated with the peptidoglycan layer [Lambert88]. Targeting of OmpF to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].

OmpF allows the passage of solutes such as sugars, ions, and amino acids which are less than 600 daltons, with a weak preference for cationic molecules [Cowan92]. Studies in which OmpF was chemically modified suggested OmpF has two separate ionic pathways preferential for either small, highly charged ions or large ions [Miedema06]. Double OmpC-OmpF mutants and OmpR mutants (incapable of synthesizing OmpC and OmpF) survive poorly in comparison to single mutants of OmpC or OmpF when suspended in filtered-autoclaved water or sea water. This suggests that these two porins are crucial for entry into survival mode [Darcan03]. OmpF is believed to be the main pathway for β-lactam antibiotics (reviewed in [Nikaido89]). OmpF has been implicated in the secretion of the extracellular protein YebF [Prehna12].

Expression of a mutant OmpF in the absence of DegP, which is normally lethal, was shown to be down-regulated post-transcriptionally in response to overexpression of ipeX, an RNA containing the 3' ends of ybcQ and nmpC [CastilloKeller06]. In E. coli K-12 the nmpC gene, encoding a qsr phage porin protein, is disrupted by an IS5 element.

OmpF imports the cytotoxic domains of group A colicins E1 and E3 after the colicins bind to the BtuB receptor [Zakharov04, Zakharov06]. The Colicin E9 (ColE9) translocon is a heptameric complex consisting of single copies of the ColE9-immunity protein complex, BtuB, the OmpF trimer and TolB [Housden13]. ColE9's unstructured N-terminal domain occupies two OmpF subunits and captures TolB on the other side of the membrane [Housden10, Housden13]. Colicin N uses only OmpF for entry [elKouhen93] - it does not require a separate receptor protein, rather it binds to lipopolysaccharide molecules adjacent to OmpF [Baboolal08, Johnson14].

OmpF production decreased in response to exogenous polyamines which are known to provide resistance to ColE7 [Pan06]. Polyamines have also been shown to inhibit antibiotic flux through polyliposome reconstituted OmpF [Kreir08, Iyer97].

Crystal structures of OmpF with and without bound N-terminal segment of colicin E3 have been solved to 3.0 Å and 1.6 Å resolution, respectively [Yamashita08].

Amounts of OmpF porin are reduced in mutants in which lon and ycgE are inactivated [Duval09]. The drug susceptibilities of the lon and ycgE mutants are associated with a decreased level of OmpF and not the result of overexpression of MarA or AcrAB [Duval09].

A description of outer membrane protein nomenclature, including early and recommended names can be found in [Osborn80].

Citations: [Nikaido85, Rosenbusch74, Schabert95, Miedema06a, Zhu09, Kumar10, Burgess08, Zakharov08]

Gene Citations: [Mizuno83]

Essentiality data for ompF 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 The Colicin A Import System: TolB

Synonyms: Lky, LkyA

Gene: tolB Accession Numbers: EG11008 (EcoCyc), b0740, ECK0729

Locations: periplasmic space, membrane

Sequence Length: 430 AAs

Molecular Weight: 45.956 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0015031 - protein transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Clavel98]
GO:0017038 - protein import Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Clavel98]
GO:0043213 - bacteriocin transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Clavel98]
GO:0006508 - proteolysis Inferred by computational analysis [GOA01]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Bonsor09, Clavel98]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Han13, Zhang07a, Molloy00, LopezCampistrou05, Isnard94, Levengood89]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01, Isnard94]
GO:0016020 - membrane Inferred by computational analysis [GOA01]

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)

Unification Links: DIP:DIP-48262N , EcoliWiki:b0740 , Mint:MINT-7888580 , ModBase:P0A855 , PR:PRO_000024079 , Pride:P0A855 , Protein Model Portal:P0A855 , RefSeq:NP_415268 , SMR:P0A855 , String:511145.b0740 , UniProt:P0A855

Relationship Links: InterPro:IN-FAMILY:IPR002469 , InterPro:IN-FAMILY:IPR007195 , InterPro:IN-FAMILY:IPR011659 , InterPro:IN-FAMILY:IPR014167 , InterPro:IN-FAMILY:IPR015943 , PDB:Structure:1C5K , PDB:Structure:1CRZ , PDB:Structure:2HQS , PDB:Structure:2IVZ , PDB:Structure:2W8B , PDB:Structure:3IAX , Pfam:IN-FAMILY:PF00930 , Pfam:IN-FAMILY:PF04052 , Pfam:IN-FAMILY:PF07676

Summary:
TolB is a periplasmic protein member of the YbgC-YbgF-TolQ-R-A-B-Pal Cell Envelope Complex, also known as the Tol-Pal system [Cascales01]. TolB has been found to interact with the outer membrane PAL lipoprotein [Bouveret95], as well as with the major outer membrane lipoprotein (LPP) and OmpA in a PAL-dependent manner [Clavel98]. Crystal structures of TolB have been determined to resolutions of 1.95 Å [Abergel99] and 2.0 Å [Yamaguchi99, Loftus06]. Targeting of TolB to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].

Yeast two-hybrid analyses of the Tol-Pal system [Walburger02] indicated that interaction between TolB and the inner membrane protein, TolA, is required for the uptake of group A colicins and for the membrane integrity. TolB is competitively recruited by the disordered translocation domain of ColE9 to energize the transport of the colicin across the outer membrane [Loftus06]. Binding of ColE9 to TolB disrupts the TolB-Pal interaction locally destabilizing the outer membrane [Loftus06].

Essentiality data for tolB 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]

References

Abergel99: Abergel C, Bouveret E, Claverie JM, Brown K, Rigal A, Lazdunski C, Benedetti H (1999). "Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution." Structure 7(10);1291-300. PMID: 10545334

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

Baboolal08: Baboolal TG, Conroy MJ, Gill K, Ridley H, Visudtiphole V, Bullough PA, Lakey JH (2008). "Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F." Structure 16(3);371-9. PMID: 18334212

Bonsor09: Bonsor DA, Hecht O, Vankemmelbeke M, Sharma A, Krachler AM, Housden NG, Lilly KJ, James R, Moore GR, Kleanthous C (2009). "Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins." EMBO J 28(18);2846-57. PMID: 19696740

Bourdineaud90: Bourdineaud JP, Fierobe HP, Lazdunski C, Pages JM (1990). "Involvement of OmpF during reception and translocation steps of colicin N entry." Mol Microbiol 4(10);1737-43. PMID: 1706457

Bouveret95: Bouveret E, Derouiche R, Rigal A, Lloubes R, Lazdunski C, Benedetti H (1995). "Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli." J Biol Chem 270(19);11071-7. PMID: 7744736

Bradbeer78: Bradbeer C, Kenley JS, Di Masi DR, Leighton M (1978). "Transport of vitamin B12 in Escherichia coli. Corrinoid specificities of the periplasmic B12-binding protein and of energy-dependent B12 transport." J Biol Chem 253(5);1347-52. PMID: 342526

Burgess08: Burgess NK, Dao TP, Stanley AM, Fleming KG (2008). "Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro." J Biol Chem 283(39);26748-58. PMID: 18641391

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

Cadieux03: Cadieux N, Phan PG, Cafiso DS, Kadner RJ (2003). "Differential substrate-induced signaling through the TonB-dependent transporter BtuB." Proc Natl Acad Sci U S A 100(19);10688-93. PMID: 12958215

Cascales01: Cascales E, Lloubes R, Sturgis JN (2001). "The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB." Mol Microbiol 42(3);795-807. PMID: 11722743

CastilloKeller06: Castillo-Keller M, Vuong P, Misra R (2006). "Novel mechanism of Escherichia coli porin regulation." J Bacteriol 188(2);576-86. PMID: 16385048

Cherezov06: Cherezov V, Yamashita E, Liu W, Zhalnina M, Cramer WA, Caffrey M (2006). "In meso structure of the cobalamin transporter, BtuB, at 1.95 A resolution." J Mol Biol 364(4);716-34. PMID: 17028020

Chimento03: Chimento DP, Mohanty AK, Kadner RJ, Wiener MC (2003). "Substrate-induced transmembrane signaling in the cobalamin transporter BtuB." Nat Struct Biol 10(5);394-401. PMID: 12652322

Clavel98: Clavel T, Germon P, Vianney A, Portalier R, Lazzaroni JC (1998). "TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA." Mol Microbiol 29(1);359-67. PMID: 9701827

Cowan92: Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, Rosenbusch JP (1992). "Crystal structures explain functional properties of two E. coli porins." Nature 1992;358(6389);727-33. PMID: 1380671

Darcan03: Darcan C, Ozkanca R, Flint KP (2003). "Survival of nonspecific porin-deficient mutants of Escherichia coli in black sea water." Lett Appl Microbiol 37(5);380-5. PMID: 14633108

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

Duche09: Duche D, Issouf M, Lloubes R (2009). "Immunity Protein Protects Colicin E2 from OmpT Protease." J Biochem 145(1);95-101. PMID: 18990718

Duval09: Duval V, Nicoloff H, Levy SB (2009). "Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli." Antimicrob Agents Chemother 53(11);4944-8. PMID: 19721064

elKouhen93: el Kouhen R, Fierobe HP, Scianimanico S, Steiert M, Pattus F, Pages JM (1993). "Characterization of the receptor and translocator domains of colicin N." Eur J Biochem 214(3);635-9. PMID: 8319674

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Han12a: 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

Han13: Han MJ, Kim JY, Kim JA (2013). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng. PMID: 24140104

Harder81: Harder KJ, Nikaido H, Matsuhashi M (1981). "Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin." Antimicrob Agents Chemother 20(4);549-52. PMID: 7044293

Housden10: Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, Kleanthous C (2010). "Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF." Proc Natl Acad Sci U S A 107(50);21412-7. PMID: 21098297

Housden13: Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C (2013). "Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF." Science 340(6140);1570-4. PMID: 23812713

Isnard94: Isnard M, Rigal A, Lazzaroni JC, Lazdunski C, Lloubes R (1994). "Maturation and localization of the TolB protein required for colicin import." J Bacteriol 176(20);6392-6. PMID: 7929011

Iyer97: Iyer R, Delcour AH (1997). "Complex inhibition of OmpF and OmpC bacterial porins by polyamines." J Biol Chem 272(30);18595-601. PMID: 9228026

Johnson14: Johnson CL, Ridley H, Marchetti R, Silipo A, Griffin DC, Crawford L, Bonev B, Molinaro A, Lakey JH (2014). "The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein." Mol Microbiol. PMID: 24589252

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

Kreir08: Kreir M, Farre C, Beckler M, George M, Fertig N (2008). "Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes." Lab Chip 8(4);587-95. PMID: 18369514

Kumar10: Kumar A, Hajjar E, Ruggerone P, Ceccarelli M (2010). "Molecular Simulations Reveal the Mechanism and the Determinants for Ampicillin Translocation through OmpF." J Phys Chem B 114(29);9608-16. PMID: 20590090

Lambert88: Lambert PA (1988). "Enterobacteriaceae: composition, structure and function of the cell envelope." Soc Appl Bacteriol Symp Ser 17;21S-34S. PMID: 2903556

Levengood89: Levengood SK, Webster RE (1989). "Nucleotide sequences of the tolA and tolB genes and localization of their products, components of a multistep translocation system in Escherichia coli." J Bacteriol 171(12);6600-9. PMID: 2687247

Likhacheva96: Likhacheva NA, Samsonov VV, Samsonov VV, Sineoky SP (1996). "Genetic control of the resistance to phage C1 of Escherichia coli K-12." J Bacteriol 178(17);5309-15. PMID: 8752353

Loftus06: Loftus SR, Walker D, Mate MJ, Bonsor DA, James R, Moore GR, Kleanthous C (2006). "Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9." Proc Natl Acad Sci U S A 103(33);12353-8. PMID: 16894158

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

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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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