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Escherichia coli K-12 substr. MG1655 Transporter: outer membrane porin E



Gene: phoE Accession Numbers: EG10729 (EcoCyc), b0241, ECK0242

Synonyms: ompE, outer membrane pore protein E (E,Ic,NmpAB)

Regulation Summary Diagram: ?

Subunit composition of outer membrane porin E = [PhoE]3

Summary:
PhoE is a member of the General Bacterial Porin (GBP) family. These proteins are present in the outer membranes of Gram negative bacteria, mitochondria, and plastids. Induced by phosphate limitation, PhoE facilitates efficient diffusion of phosphate and phosphorus-containing compounds across the outer membrane [Korteland82].

PhoE is believed to be a pore with specificity defined by the pore's composition. In this case, PhoE is believed to have a preference for small anions due to a collection of positively charged amino acids near the pore entrance [Phoenix96, Benz84]. Therefore, PhoE is not a specific transport system; rather, it is just a water filled channel allowing for passive diffusion of small molecules (~600 Da). The structure of PhoE, determined at 4.0 Å resolution, is a trimer of 16-stranded β-barrel monomers with large loops that fold inside the β-barrel, and the amino terminus faces the periplasm [Cowan92, Van97, Van96, Tommassen84, Angus83]. Amino acid substitution studies show charged residues within the constriction zone of the pore act as voltage gating sensors [Navis97]. PhoE activity is inhibited by ATP which blocks ion flow through the porin [Samartzidou99].

Targeting of PhoE to the Sec-translocase for transport across the inner membrane is SecB-dependent [deCock92, Baars06]. Protein cross-linking studies indicate the transmembrane form of PhoE interacts with Skp at the periplasmic side of the inner membrane [Harms01]. Protein assembly has been studied identifying intermediates in the assembly process [Jansen00], and LPS has been identified as being important in PhoE folding [deCock99, deCock96]. TolB has been shown to interact with trimeric PhoE [Rigal97]. The C-terminal phenylalanine is essential for proper assembly of PhoE in the outer membrane [Struyve91, deCock97].

Expression of phoE is inhibited by σS [Taschner04]. High NaCl induces phoE-mediated acid sensitivity [Lazim96]. Adaptation to high osmolarity results in reduced levels of PhoE [Meyer90].

PhoE has been shown to bind human lactoferrin [Sallmann99].

Gene Citations: [Yamada89]

Locations: outer membrane

Map Position: [258,269 <- 259,324] (5.57 centisomes)
Length: 1056 bp / 351 aa

Molecular Weight of Polypeptide: 38.922 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000823 , CGSC:396 , DIP:DIP-10498N , EchoBASE:EB0722 , EcoGene:EG10729 , EcoliWiki:b0241 , Mint:MINT-1285942 , ModBase:P02932 , OU-Microarray:b0241 , PortEco:phoE , PR:PRO_000023542 , Pride:P02932 , Protein Model Portal:P02932 , RefSeq:NP_414776 , RegulonDB:EG10729 , SMR:P02932 , String:511145.b0241 , UniProt:P02932

Relationship Links: InterPro:IN-FAMILY:IPR001702 , InterPro:IN-FAMILY:IPR001897 , InterPro:IN-FAMILY:IPR013793 , InterPro:IN-FAMILY:IPR017690 , InterPro:IN-FAMILY:IPR023614 , PDB:Structure:1PHO , Pfam:IN-FAMILY:PF00267 , Prints:IN-FAMILY:PR00182 , Prints:IN-FAMILY:PR00183 , Prosite:IN-FAMILY:PS00576

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11a]
GO:0055085 - transmembrane transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0015288 - porin activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0046930 - pore complex Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Hagge02]
GO:0009279 - cell outer membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
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)

Essentiality data for phoE 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]

Credits:
Created 11-Apr-2007 by Johnson A , TIGR


Enzymatic reaction of: transport of hydrophilic solute or ion < 600 Da (outer membrane porin E)


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 21
[Overbeeke83]
 
Chain 22 -> 351
[UniProt09]
UniProt: Outer membrane pore protein E;
Mutagenesis-Variant 351
[Struyve91, UniProt11]
Alternate sequence: F → V; UniProt: Less resistant to trypsin.
Alternate sequence: F → S; UniProt: Less resistant to trypsin.
Alternate sequence: F → N; UniProt: Less resistant to trypsin.
Alternate sequence: F → Y; UniProt: Less resistant to trypsin.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0241 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10729; confirmed by SwissProt match.


References

Angus83: Angus BL, Hancock RE (1983). "Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers." J Bacteriol 155(3);1042-51. PMID: 6309736

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

Benz84: Benz R, Darveau RP, Hancock RE (1984). "Outer-membrane protein PhoE from Escherichia coli forms anion-selective pores in lipid-bilayer membranes." Eur J Biochem 140(2);319-24. PMID: 6325185

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

deCock92: de Cock H, Overeem W, Tommassen J (1992). "Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein." J Mol Biol 224(2);369-79. PMID: 1313884

deCock96: de Cock H, Tommassen J (1996). "Lipopolysaccharides and divalent cations are involved in the formation of an assembly-competent intermediate of outer-membrane protein PhoE of E.coli." EMBO J 15(20);5567-73. PMID: 8896450

deCock97: de Cock H, Struyve M, Kleerebezem M, van der Krift T, Tommassen J (1997). "Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12." J Mol Biol 269(4);473-8. PMID: 9217252

deCock99: de Cock H, Brandenburg K, Wiese A, Holst O, Seydel U (1999). "Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli." J Biol Chem 274(8);5114-9. PMID: 9988760

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

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

Hagge02: Hagge SO, de Cock H, Gutsmann T, Beckers F, Seydel U, Wiese A (2002). "Pore formation and function of phosphoporin PhoE of Escherichia coli are determined by the core sugar moiety of lipopolysaccharide." J Biol Chem 277(37);34247-53. PMID: 12091383

Harms01: Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H (2001). "The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane." J Biol Chem 276(22);18804-11. PMID: 11278858

Jansen00: Jansen C, Heutink M, Tommassen J, de Cock H (2000). "The assembly pathway of outer membrane protein PhoE of Escherichia coli." Eur J Biochem 267(12);3792-800. PMID: 10848998

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

Korteland82: Korteland J, Tommassen J, Lugtenberg B (1982). "PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate." Biochim Biophys Acta 690(2);282-9. PMID: 6289897

Lazim96: Lazim Z, Humphrey TJ, Rowbury RJ (1996). "Induction of the PhoE porin by NaCl as the basis for salt-induced acid sensitivity in Escherichia coli." Lett Appl Microbiol 23(4);269-72. PMID: 8987702

Meyer90: Meyer SE, Granett S, Jung JU, Villarejo MR (1990). "Osmotic regulation of PhoE porin synthesis in Escherichia coli." J Bacteriol 172(9);5501-2. PMID: 2168386

Navis97: Navis G, de Zeeuw D, de Jong PE (1997). "ACE-inhibitors: panacea for progressive renal disease." Lancet 349(9069);1852-3. PMID: 9217751

Overbeeke83: Overbeeke N, Bergmans H, van Mansfeld F, Lugtenberg B (1983). "Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12." J Mol Biol 163(4);513-32. PMID: 6341601

Phoenix96: Phoenix DA (1996). "On the targeting and membrane assembly of the Escherichia coli outer membrane porin, PhoE." FEMS Immunol Med Microbiol 1996;16(2);77-82. PMID: 8988389

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

Sallmann99: Sallmann FR, Baveye-Descamps S, Pattus F, Salmon V, Branza N, Spik G, Legrand D (1999). "Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin. Binding characteristics and biological effects." J Biol Chem 274(23);16107-14. PMID: 10347162

Samartzidou99: Samartzidou H, Delcour AH (1999). "Distinct sensitivities of OmpF and PhoE porins to charged modulators." FEBS Lett 444(1);65-70. PMID: 10037149

Struyve91: Struyve M, Moons M, Tommassen J (1991). "Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein." J Mol Biol 218(1);141-8. PMID: 1848301

Taschner04: Taschner NP, Yagil E, Spira B (2004). "A differential effect of sigmaS on the expression of the PHO regulon genes of Escherichia coli." Microbiology 150(Pt 9);2985-92. PMID: 15347756

Tommassen84: Tommassen J, Lugtenberg B (1984). "Amino terminus of outer membrane PhoE protein: localization by use of a bla-phoE hybrid gene." J Bacteriol 157(1);327-9. PMID: 6361002

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

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

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

Van96: Van Gelder P, Tommassen J (1996). "Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo." J Bacteriol 178(17);5320-2. PMID: 8752355

Van97: Van Gelder P, Saint N, van Boxtel R, Rosenbusch JP, Tommassen J (1997). "Pore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3." Protein Eng 10(6);699-706. PMID: 9278284

Yamada89: Yamada M, Makino K, Amemura M, Shinagawa H, Nakata A (1989). "Regulation of the phosphate regulon of Escherichia coli: analysis of mutant phoB and phoR genes causing different phenotypes." J Bacteriol 1989;171(10);5601-6. PMID: 2676981

Other References Related to Gene Regulation

Holmqvist12: Holmqvist E, Unoson C, Reimegard J, Wagner EG (2012). "A mixed double negative feedback loop between the sRNA MicF and the global regulator Lrp." Mol Microbiol 84(3);414-27. PMID: 22324810

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Tommassen87: Tommassen J, Koster M, Overduin P (1987). "Molecular analysis of the promoter region of the Escherichia coli K-12 phoE gene. Identification of an element, upstream from the promoter, required for efficient expression of phoE protein." J Mol Biol 1987;198(4);633-41. PMID: 2828642


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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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