Escherichia coli K-12 substr. MG1655 Transporter: Colicin E9 translocon
Inferred from experiment

Subunit composition of Colicin E9 translocon = [TolB][(OmpF)3]
         TolB - periplasmic protein of the Tol-Pal system = TolB (extended summary available)
         outer membrane porin F = (OmpF)3
                 OmpF monomer = OmpF

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reaction of [a monosaccharide[periplasm] ↔ a monosaccharide[extracellular space]] (no EC#):
i2: N-acetylneuraminate[extracellular space]N-acetylneuraminate[periplasm] (no EC#)

Instance reaction of [N-acetylneuraminate[extracellular space]N-acetylneuraminate[periplasm]] (no EC#):
i1: N-acetyl-β-neuraminate[extracellular space]N-acetyl-β-neuraminate[periplasm] (no EC#)

Subunit of Colicin E9 translocon: TolB - periplasmic protein of the Tol-Pal system

Synonyms: Lky, LkyA

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

Locations: periplasmic space

Sequence Length: 430 AAs

Molecular Weight: 45.956 kD (from nucleotide sequence)

GO Terms:
Biological Process:
Inferred by computational analysisInferred from experimentGO:0015031 - protein transport [Clavel98, UniProtGOA11a, GOA01a]
Inferred by computational analysisInferred from experimentGO:0017038 - protein import [Clavel98, GOA06, GOA01a]
Inferred by computational analysisInferred from experimentGO:0043213 - bacteriocin transport [Clavel98, UniProtGOA11a]
Inferred from experimentGO:0051301 - cell division [Gerding07]
Inferred from experimentGO:0071237 - cellular response to bacteriocin [Loftus06, Walburger02]
Inferred by computational analysisGO:0006810 - transport [UniProtGOA11a]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Walburger02, Rigal97, Bouveret95, Bonsor09, Clavel98]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0030288 - outer membrane-bounded periplasmic space [DiazMejia09, Han14, Zhang07, Molloy00, LopezCampistrou05, Isnard94, Levengood89]
Inferred from experimentGO:0032153 - cell division site [Gerding07]
Inferred by computational analysisInferred from experimentGO:0042597 - periplasmic space [Isnard94, UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]

MultiFun Terms: extrachromosomalcolicin related
extrachromosomalprophage genes and phage related functions
transportChannel-type TransportersBeta 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, 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:PF04052, Pfam:IN-FAMILY:PF07676

TolB is a periplasmic component of the Tol-Pal system - a group of interacting proteins which span the cell envelope of E. coli K-12. The Tol-Pal system plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. It also has a role in facilitating phage infection and colicin uptake.

TolB is a periplasmic protein [Isnard94]; TolB interacts with the peptidoglycan associated lipoprotein, Pal in vivo [Bouveret95, Walburger02]. TolB interacts with the major outer membrane lipoprotein, Lpp and with OmpA in a Pal-dependent manner [Clavel98]. Purified TolB interacts with the trimeric outer membrane porins, OmpF, OmpC, PhoE and LamB in vitro [Rigal97]. TolB may form homodimers in vivo [Walburger02]. TolB interacts with TolA; disrupting this interaction results in cells that are hypersensitive to SDS and tolerant to colicin A [Walburger02].

TolB accumulates at the site of constriction in dividing cells; this localisation is dependent on FtsN [Gerding07].

TolB consists of two domains - an N-terminal domain with an αβ structure and a large C-terminal domain that adopts a 6-bladed β propeller structure [Abergel99, Carr00].

Colicin E9 binds to the propeller domain of TolB; colicin E9 competes with Pal for binding to TolB; colicin E9 can dislodge Pal from its complex with TolB but this requires Ca2+ or Mg2+ ions [Loftus06, Papadakos12]. Colicin A and colicin E9 interact in subtly different ways with TolB [Zhang10]. TolB, TolA and proton motive force are required for release of the immunity protein (Im9) from colicin E9 [Vankemmelbeke09]

tolB mutants release periplasmic proteins into the extracellular medium [Lazzaroni81, FogniniLefebvre87].

Targeting of TolB to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].

tol: colicin tolerant [Nagel67, Nomura67]
lky: leaky [Lazzaroni81]

Comments: [Uversky12]

Citations: [Benedetti91, Bouveret98, Duche06]

Essentiality data for tolB knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enrichedYes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Component enzyme of Colicin E9 translocon : outer membrane porin F

Synonyms: nfxB, tolF, cmlB, cry, outer membrane protein F, 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 porin F = [OmpF]3
         OmpF monomer = OmpF

Map Position: [985,117 <- 986,205] (21.23 centisomes, 76°)
Length: 1089 bp / 362 aa

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

GO Terms:
Biological Process:
Inferred from experimentGO:0006855 - drug transmembrane transport [Harder81]
Inferred from experimentGO:0043213 - bacteriocin transport [Bourdineaud90]
Inferred by computational analysisGO:0006810 - transport [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0006811 - ion transport [UniProtGOA11a]
Author statementGO:0034220 - ion transmembrane transport [Nikaido85]
Molecular Function:
Inferred from experimentGO:0015238 - drug transmembrane transporter activity [Harder81]
Inferred from experimentAuthor statementInferred by computational analysisGO:0015288 - porin activity [UniProtGOA11a, GOA01a, Nikaido85, Saint96]
Inferred from experimentGO:0042912 - colicin transmembrane transporter activity [Bourdineaud90]
Author statementGO:0015075 - ion transmembrane transporter activity [Nikaido85]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0009279 - cell outer membrane [UniProtGOA11, UniProtGOA11a, DiazMejia09, Han12a, Zhang07, Molloy00, LopezCampistrou05, Palva78]
Inferred from experimentInferred by computational analysisGO:0046930 - pore complex [UniProtGOA11a, Cowan92]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016021 - integral component of membrane [UniProtGOA11a]

MultiFun Terms: transportChannel-type TransportersBeta 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, 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, PDB:Structure:4JFB, PDB:Structure:4LSE, PDB:Structure:4LSF, PDB:Structure:4LSH, PDB:Structure:4LSI, Pfam:IN-FAMILY:PF00267, Prints:IN-FAMILY:PR00182, Prints:IN-FAMILY:PR00183, Prosite:IN-FAMILY:PS00576

S-methyl-5-thio-D-ribose[periplasm]S-methyl-5-thio-D-ribose[extracellular space],
an inositol[periplasm] ↔ an inositol[extracellular space],
an amino acid[periplasm] ↔ an amino acid[extracellular space],
a nucleobase[periplasm] ↔ a nucleobase[extracellular space],
a sugar alcohol[periplasm] ↔ a sugar alcohol[extracellular space],
a short-chain alcohol[periplasm] ↔ a short-chain alcohol[extracellular space],
a short-chain carboxylate[periplasm] ↔ a short-chain carboxylate[extracellular space],
an organosulfur compound[periplasm] ↔ an organosulfur compound[extracellular space],
H2O[periplasm] ↔ H2O[extracellular space],
CO2[periplasm] ↔ CO2[extracellular space],
an ion[periplasm] ↔ an ion[extracellular space],
a monosaccharide[periplasm] ↔ a monosaccharide[extracellular space],
glycine betaine[extracellular space] ↔ glycine betaine[periplasm],
hydrophilic solute or ion < 600 Da[extracellular space] ↔ hydrophilic solute or ion < 600 Da[periplasm]

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, Zhao15]

Gene Citations: [Mizuno83]

Essentiality data for ompF knockouts:

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


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

Benedetti91: Benedetti H, Frenette M, Baty D, Knibiehler M, Pattus F, Lazdunski C (1991). "Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement." J Mol Biol 217(3);429-39. PMID: 1704440

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

Bouveret98: Bouveret E, Rigal A, Lazdunski C, Benedetti H (1998). "Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli." Mol Microbiol 27(1);143-57. PMID: 9466263

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

Carr00: Carr S, Penfold CN, Bamford V, James R, Hemmings AM (2000). "The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9." Structure 8(1);57-66. PMID: 10673426

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

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

Duche06: Duche D, Frenkian A, Prima V, Lloubes R (2006). "Release of immunity protein requires functional endonuclease colicin import machinery." J Bacteriol 188(24);8593-600. PMID: 17012383

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

FogniniLefebvre87: Fognini-Lefebvre N, Lazzaroni JC, Portalier R (1987). "tolA, tolB and excC, three cistrons involved in the control of pleiotropic release of periplasmic proteins by Escherichia coli K12." Mol Gen Genet 209(2);391-5. PMID: 3312962

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

Gerding07: Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA (2007). "The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli." Mol Microbiol 63(4);1008-25. PMID: 17233825

GOA01a: 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

Han14: Han MJ, Kim JY, Kim JA (2014). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng 117(4);437-42. 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

Lazzaroni81: Lazzaroni JC, Portalier RC (1981). "Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12." J Bacteriol 145(3);1351-8. PMID: 7009581

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

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

Miedema06: Miedema H, Vrouenraets M, Wierenga J, Gillespie D, Eisenberg B, Meijberg W, Nonner W (2006). "Ca2+ selectivity of a chemically modified OmpF with reduced pore volume." Biophys J 91(12);4392-400. PMID: 16997866

Miedema06a: Miedema H, Vrouenraets M, Wierenga J, Eisenberg B, Schirmer T, Basle A, Meijberg W (2006). "Conductance and selectivity fluctuations in D127 mutants of the bacterial porin OmpF." Eur Biophys J 36(1);13-22. PMID: 16858566

Mizuno83: Mizuno T, Chou MY, Inouye M (1983). "A comparative study on the genes for three porins of the Escherichia coli outer membrane. DNA sequence of the osmoregulated ompC gene." J Biol Chem 1983;258(11);6932-40. PMID: 6304064

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

Nagel67: Nagel de Zwaig R, Luria SE (1967). "Genetics and physiology of colicin-tolerant mutants of Escherichia coli." J Bacteriol 94(4);1112-23. PMID: 4167587

Nikaido85: Nikaido H, Vaara M (1985). "Molecular basis of bacterial outer membrane permeability." Microbiol Rev 49(1);1-32. PMID: 2580220

Nikaido89: Nikaido H (1989). "Outer membrane barrier as a mechanism of antimicrobial resistance." Antimicrob Agents Chemother 33(11);1831-6. PMID: 2692513

Nomura67: Nomura M, Witten C (1967). "Interaction of colicins with bacterial cells. 3. Colicin-tolerant mutations in Escherichia coli." J Bacteriol 94(4);1093-111. PMID: 4860908

Osborn80: Osborn MJ, Wu HC (1980). "Proteins of the outer membrane of gram-negative bacteria." Annu Rev Microbiol 34;369-422. PMID: 6254441

Palva78: Palva ET, Randall LL (1978). "Arrangement of protein I in Escherichia coli outer membrane: cross-linking study." J Bacteriol 133(1);279-86. PMID: 338582

Pan06: Pan YH, Liao CC, Kuo CC, Duan KJ, Liang PH, Yuan HS, Hu ST, Chak KF (2006). "The critical roles of polyamines in regulating ColE7 production and restricting ColE7 uptake of the colicin-producing Escherichia coli." J Biol Chem 281(19);13083-91. PMID: 16549429

Papadakos12: Papadakos G, Housden NG, Lilly KJ, Kaminska R, Kleanthous C (2012). "Kinetic basis for the competitive recruitment of TolB by the intrinsically disordered translocation domain of colicin E9." J Mol Biol 418(5);269-80. PMID: 22310049

Prehna12: Prehna G, Zhang G, Gong X, Duszyk M, Okon M, McIntosh LP, Weiner JH, Strynadka NC (2012). "A Protein Export Pathway Involving Escherichia coli Porins." Structure 20(7);1154-66. PMID: 22658749

Rigal97: Rigal A, Bouveret E, Lloubes R, Lazdunski C, Benedetti H (1997). "The TolB protein interacts with the porins of Escherichia coli." J Bacteriol 179(23);7274-9. PMID: 9393690

Rosenbusch74: Rosenbusch JP (1974). "Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding." J Biol Chem 249(24);8019-29. PMID: 4609976

Saint96: Saint N, Lou KL, Widmer C, Luckey M, Schirmer T, Rosenbusch JP (1996). "Structural and functional characterization of OmpF porin mutants selected for larger pore size. II. Functional characterization." J Biol Chem 271(34);20676-80. PMID: 8702817

Schabert95: Schabert FA, Henn C, Engel A (1995). "Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy." Science 268(5207);92-4. PMID: 7701347

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."

Uversky12: Uversky VN (2012). "Disordered competitive recruiter: fast and foldable." J Mol Biol 418(5);267-8. PMID: 22381408

Vankemmelbeke09: Vankemmelbeke M, Zhang Y, Moore GR, Kleanthous C, Penfold CN, James R (2009). "Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation." J Biol Chem 284(28);18932-41. PMID: 19458090

Walburger02: Walburger A, Lazdunski C, Corda Y (2002). "The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB." Mol Microbiol 44(3);695-708. PMID: 11994151

Yamashita08: Yamashita E, Zhalnina MV, Zakharov SD, Sharma O, Cramer WA (2008). "Crystal structures of the OmpF porin: function in a colicin translocon." EMBO J 27(15);2171-80. PMID: 18636093

Zakharov04: Zakharov SD, Eroukova VY, Rokitskaya TI, Zhalnina MV, Sharma O, Loll PJ, Zgurskaya HI, Antonenko YN, Cramer WA (2004). "Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import." Biophys J 87(6);3901-11. PMID: 15465872

Zakharov06: Zakharov SD, Zhalnina MV, Sharma O, Cramer WA (2006). "The colicin E3 outer membrane translocon: immunity protein release allows interaction of the cytotoxic domain with OmpF porin." Biochemistry 45(34);10199-207. PMID: 16922495

Zakharov08: Zakharov SD, Sharma O, Zhalnina MV, Cramer WA (2008). "Primary Events in the Colicin Translocon: FRET Analysis of Colicin Unfolding Initiated by Binding to BtuB and OmpF." Biochemistry. PMID: 18986168

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

Zhang10: Zhang Y, Li C, Vankemmelbeke MN, Bardelang P, Paoli M, Penfold CN, James R (2010). "The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins." Mol Microbiol 75(3);623-36. PMID: 19627502

Zhao15: Zhao Z, Eberhart LJ, Orfe LH, Lu SY, Besser TE, Call DR (2015). "Genome-wide screening identifies six genes that are associated with susceptibility to Escherichia coli microcin PDI." Appl Environ Microbiol. PMID: 26209678

Zhu09: Zhu Y, Guo T, Park JE, Li X, Meng W, Datta A, Bern M, Lim SK, Sze SK (2009). "Elucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprinting." Mol Cell Proteomics. PMID: 19473960

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 19.5 on Fri Nov 27, 2015, BIOCYC13B.