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Escherichia coli K-12 substr. MG1655 Polypeptide: alkyl hydroperoxide reductase, AhpC component

Gene: ahpC Accession Numbers: EG11384 (EcoCyc), b0605, ECK0599

Synonyms: tpx, ssi8, alkyl hydroperoxide reductase, C22 subunit

Regulation Summary Diagram

Regulation summary diagram for ahpC

Component of: alkyl hydroperoxide reductase (extended summary available)

AhpC is the peroxidase component of alkyl hydroperoxide reductase belonging to the family of typical 2-Cys peroxiredoxins with two conserved redox-active cysteines.

By similarity to the enzyme from Salmonella typhimurium, AhpC carries out the actual reduction of the hydroperoxide substrate.

Under reduced conditions, AhpC forms a decameric ring composed of five homodimers that interact in a head-to-tail configuration, with intermolecular disulfide bonds between Cys47 of one subunit and Cys177 of the second subunit forming the active site [Dip14, Dip14a]. The C terminus is required for the dimer-to-decamer transition, anchors the AhpC-AhpF interaction, and undergoes redox-modulated structural rearrangements [Dip14].

A proteomics screen showed that AhpC interacts with ATP [Chang12]. AhpC has been found to interact with thioredoxin [Kumar04] and the peptidyl-prolyl cis-trans isomerase PpiC [Malesevic10]. AhpC is 38% oxidatively modified in exponentially growing cells; this increases to 63.2% after hypochlorite treatment [Faulkner08].

A G142V mutation in ahpC leads to increased activity in the reduction of tetralin hydroperoxide to 1,2,3,4-tetrahydro-1-naphthol [Ferrante95]. Addition of a single phenylalanine residue converts AhpC from a peroxidase to a disulfide reductase [Ritz01] that generates reduced glutathione [Yamamoto08a]. Other point mutants confer disulfide reductase activity without eliminating the peroxidase activity of AhpC [Yamamoto08a]. Surprisingly, different mutant versions of AhpC can channel electrons into disulfide-reducing pathways via different protein substrates [Faulkner08].

Protein abundance is increased by aerobic growth in acidic medium [Blankenhorn99], sulfate starvation [Quadroni96], and indole [Garbe00] and decreased in the presence of the antifouling agent zosteric acid [Villa12]. Overexpression of ahpC confers furfural tolerance [Glebes15].

An ahpC deletion mutant secretes less enterobactin and shows reduced growth and reduced accumulation of iron when grown in low iron media. The defect may be due to an effect of AhpC on the activity of EntC or on the availability of chorismate [Ma12a].

Ssi8: "sulfate starvation-induced" [Quadroni96]

Citations: [Smillie92, Jung03, Lu05, Campos07, Kwon08a, SchurigBriccio09, Wang09]

Locations: cytosol, membrane

Map Position: [638,168 -> 638,731] (13.75 centisomes, 50°)
Length: 564 bp / 187 aa

Molecular Weight of Polypeptide: 20.761 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002090, CGSC:31190, DIP:DIP-36164N, EchoBASE:EB1357, EcoGene:EG11384, EcoliWiki:b0605, Mint:MINT-1241588, ModBase:P0AE08, OU-Microarray:b0605, PortEco:ahpC, PR:PRO_000022070, Pride:P0AE08, Protein Model Portal:P0AE08, RefSeq:NP_415138, RegulonDB:EG11384, SMR:P0AE08, String:511145.b0605, Swiss-Model:P0AE08, UniProt:P0AE08

Relationship Links: InterPro:IN-FAMILY:IPR000866, InterPro:IN-FAMILY:IPR012336, InterPro:IN-FAMILY:IPR017559, InterPro:IN-FAMILY:IPR019479, InterPro:IN-FAMILY:IPR024706, Panther:IN-FAMILY:PTHR10681:SF7, PDB:Structure:4O5R, PDB:Structure:4QL7, PDB:Structure:4QL9, Pfam:IN-FAMILY:PF00578, Pfam:IN-FAMILY:PF10417, Prosite:IN-FAMILY:PS51352

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for ahpC

GO Terms:
Biological Process:
Inferred from experimentGO:0009970 - cellular response to sulfate starvation [Quadroni96]
Inferred from experimentGO:0033194 - response to hydroperoxide [Tsuji95]
Inferred from experimentGO:0033195 - response to alkyl hydroperoxide [Storz89]
Inferred from experimentGO:0033214 - iron assimilation by chelation and transport [Ma12a]
Inferred by computational analysisGO:0006979 - response to oxidative stress [GOA01a]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0004601 - peroxidase activity [UniProtGOA11a, Seaver01a]
Inferred from experimentGO:0005515 - protein binding [Kumar04, Malesevic10]
Inferred from experimentGO:0016684 - oxidoreductase activity, acting on peroxide as acceptor [Ferrante95]
Inferred from experimentGO:0032843 - hydroperoxide reductase activity [Ferrante95]
Inferred from experimentGO:0042802 - identical protein binding [Rajagopala14, Lasserre06]
Inferred by computational analysisGO:0016209 - antioxidant activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0051920 - peroxiredoxin activity [GOA01, GOA01a]
Cellular Component:
Inferred from experimentGO:0005737 - cytoplasm [Cha95]
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
Inferred from experimentGO:0009321 - alkyl hydroperoxide reductase complex [Dip14a]
Inferred from experimentGO:0016020 - membrane [Lasserre06]

MultiFun Terms: cell processesprotectiondetoxification

Essentiality data for ahpC 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]

Last-Curated 18-Nov-2014 by Keseler I, SRI International

Subunit of: alkyl hydroperoxide reductase

Subunit composition of alkyl hydroperoxide reductase = [AhpC]10[AhpF]4
         alkyl hydroperoxide reductase, AhpC component = AhpC (extended summary available)
         alkyl hydroperoxide reductase, AhpF component = AhpF (extended summary available)

Alkyl hydroperoxide reductase converts alkyl hydroperoxides to their corresponding alcohols. By similarity to the enzyme from Salmonella typhimurium, the AhpC component catalyzes the peroxide reductase reaction, while the AhpF component restores the reduced state of AhpC by transferring electrons from NADH to AhpC. Based on structural data, a model of the catalytic cycle has been proposed [Dip14a].

Alkyl hydroperoxide reductase is responsible for scavenging H2O2 at low concentrations, while catalase is responsible for scavenging H2O2 at high concentrations [Seaver01a, Seaver01].

Overexpression of alkyl hydroperoxide reductase leads to increased resistance to cumene hydroperoxide and other redox-cycling agents [Greenberg88]. An ahpCF mutant is more sensitive to the increased endogenous production of peroxides during phosphate starvation [Moreau01] and has a severe growth defect when grown on phenylethylamine [Ravindra13]. An insertion mutant in the ahpC promoter region is cold sensitive [Serina04]. Oxidative stress-related proteins, including AhpC and AhpF, are upregulated when germfree mice inoculated with E. coli are fed a lactose diet. An ahpCF mutant shows increased doubling time under conditions of high osmolality [Rothe12].

Reviews: [Poole05a, Imlay08, Mishra12, Rothe13, Lu14a]

Citations: [Ferrante95, Gundlach14]

GO Terms:
Biological Process:
Inferred from experimentGO:0033194 - response to hydroperoxide [Seaver01a]
Inferred from experimentGO:0045454 - cell redox homeostasis [Seaver01]
Molecular Function:
Inferred from experimentGO:0008785 - alkyl hydroperoxide reductase activity [Dip14, Dip14a]

Last-Curated 18-Nov-2014 by Keseler I, SRI International

Enzymatic reaction of: alkyl hydroperoxide reductase

Inferred from experiment

EC Number: 1.8.1.-

an organic hydroperoxide + NADH + H+ → an alcohol + NAD+ + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for an organic hydroperoxide: hydrogen peroxide [Dip14a, Seaver01a]

Cofactors or Prosthetic Groups: FAD [Bieger01]

Sequence Features

Protein sequence of alkyl hydroperoxide reductase, AhpC component with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
Inferred from experiment[Wilkins98, Link97, Quadroni96, Cha95, Ueshima92, Pasquali94, Quadroni96, Cha95, Wilkins98, Link97, Ueshima92, Cha95]
Conserved-Region 2 -> 157
Inferred by computational analysis[UniProt15]
UniProt: Thioredoxin.
Chain 2 -> 187
Author statement[UniProt15]
UniProt: Alkyl hydroperoxide reductase subunit C.
N6-acetyllysine-Modification 17
Inferred from experiment[Zhang09a]
UniProt: N6-acetyllysine.
Disulfide-Bond-Site 47
Inferred by computational analysis[UniProt15]
UniProt: Interchain (with C-166); in linked form.
Active-Site 47
Inferred by computational analysis[UniProt15]
UniProt: Cysteine sulfenic acid (-SOH) intermediate.
N6-acetyllysine-Modification 93
Inferred from experiment[Zhang09a]
UniProt: N6-acetyllysine.
N6-acetyllysine-Modification 153
Inferred from experiment[Zhang09a]
UniProt: N6-acetyllysine.
Disulfide-Bond-Site 166
Inferred by computational analysis[UniProt15]
UniProt: Interchain (with C-47); in linked form.
N6-acetyllysine-Modification 169
Inferred from experiment[Zhang09a]
UniProt: N6-acetyllysine.
N6-acetyllysine-Modification 171
Inferred from experiment[Zhang09a]
UniProt: N6-acetyllysine.

Sequence Pfam Features

Protein sequence of alkyl hydroperoxide reductase, AhpC component with features indicated

Feature Class Location Citations Comment
Pfam PF00578 10 -> 133
Inferred by computational analysis[Finn14]
AhpC-TSA : AhpC/TSA family
Pfam PF10417 154 -> 182
Inferred by computational analysis[Finn14]
1-cysPrx_C : C-terminal domain of 1-Cys peroxiredoxin

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Units

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b0605 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11384; confirmed by SwissProt match.


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

Bieger01: Bieger B, Essen LO (2001). "Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli." J Mol Biol 307(1);1-8. PMID: 11243797

Blankenhorn99: Blankenhorn D, Phillips J, Slonczewski JL (1999). "Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis." J Bacteriol 181(7);2209-16. PMID: 10094700

Campos07: Campos E, Montella C, Garces F, Baldoma L, Aguilar J, Badia J (2007). "Aerobic L-ascorbate metabolism and associated oxidative stress in Escherichia coli." Microbiology 153(Pt 10);3399-408. PMID: 17906139

Cha95: Cha MK, Kim HK, Kim IH (1995). "Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli." J Biol Chem 1995;270(48);28635-41. PMID: 7499381

Chang12: Chang Y, Schlebach JP, VerHeul RA, Park C (2012). "Simplified proteomics approach to discover protein-ligand interactions." Protein Sci 21(9);1280-7. PMID: 22733688

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

Dip14: Dip PV, Kamariah N, Nartey W, Beushausen C, Kostyuchenko VA, Ng TS, Lok SM, Saw WG, Eisenhaber F, Eisenhaber B, Gruber G (2014). "Key roles of the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress." Biochim Biophys Acta 1837(12);1932-1943. PMID: 25193562

Dip14a: Dip PV, Kamariah N, Subramanian Manimekalai MS, Nartey W, Balakrishna AM, Eisenhaber F, Eisenhaber B, Gruber G (2014). "Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli." Acta Crystallogr D Biol Crystallogr 70(Pt 11);2848-62. PMID: 25372677

Faulkner08: Faulkner MJ, Veeravalli K, Gon S, Georgiou G, Beckwith J (2008). "Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways." Proc Natl Acad Sci U S A 105(18);6735-40. PMID: 18456836

Ferrante95: Ferrante AA, Augliera J, Lewis K, Klibanov AM (1995). "Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase." Proc Natl Acad Sci U S A 92(17);7617-21. PMID: 7644465

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Garbe00: Garbe TR, Kobayashi M, Yukawa H (2000). "Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity." Arch Microbiol 173(1);78-82. PMID: 10648109

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

Glebes15: Glebes TY, Sandoval NR, Gillis JH, Gill RT (2015). "Comparison of genome-wide selection strategies to identify furfural tolerance genes in Escherichia coli." Biotechnol Bioeng 112(1);129-40. PMID: 24981318

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Greenberg88: Greenberg JT, Demple B (1988). "Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants." EMBO J 7(8);2611-7. PMID: 2847922

Gundlach14: Gundlach J, Winter J (2014). "Evolution of Escherichia coli for maximum HOCl resistance through constitutive expression of the OxyR regulon." Microbiology 160(Pt 8);1690-704. PMID: 24899627

Imlay08: Imlay JA (2008). "Cellular defenses against superoxide and hydrogen peroxide." Annu Rev Biochem 77;755-76. PMID: 18173371

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Jung03: Jung IL, Kim IG (2003). "Transcription of ahpC, katG, and katE genes in Escherichia coli is regulated by polyamines: polyamine-deficient mutant sensitive to H2O2-induced oxidative damage." Biochem Biophys Res Commun 301(4);915-22. PMID: 12589799

Kumar04: Kumar JK, Tabor S, Richardson CC (2004). "Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli." Proc Natl Acad Sci U S A 101(11);3759-64. PMID: 15004283

Kwon08a: Kwon S, Jung Y, Lim D (2008). "Proteomic analysis of heat-stable proteins in Escherichia coli." BMB Rep 41(2);108-11. PMID: 18315945

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

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

Lu05: Lu C, Albano CR, Bentley WE, Rao G (2005). "Quantitative and kinetic study of oxidative stress regulons using green fluorescent protein." Biotechnol Bioeng 89(5);574-87. PMID: 15672380

Lu14a: Lu J, Holmgren A (2014). "The thioredoxin antioxidant system." Free Radic Biol Med 66;75-87. PMID: 23899494

Ma12a: Ma L, Payne SM (2012). "AhpC Is Required for Optimal Production of Enterobactin by Escherichia coli." J Bacteriol 194(24);6748-57. PMID: 23042987

Malesevic10: Malesevic M, Poehlmann A, Hernandez Alvarez B, Diessner A, Trager M, Rahfeld JU, Jahreis G, Liebscher S, Bordusa F, Fischer G, Lucke C (2010). "The protein-free IANUS peptide array uncovers interaction sites between Escherichia coli parvulin 10 and alkyl hydroperoxide reductase." Biochemistry 49(39);8626-35. PMID: 20806779

Mishra12: Mishra S, Imlay J (2012). "Why do bacteria use so many enzymes to scavenge hydrogen peroxide?." Arch Biochem Biophys 525(2);145-60. PMID: 22609271

Moreau01: Moreau PL, Gerard F, Lutz NW, Cozzone P (2001). "Non-growing Escherichia coli cells starved for glucose or phosphate use different mechanisms to survive oxidative stress." Mol Microbiol 39(4);1048-60. PMID: 11251823

Pasquali94: Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. (1994). Data submission to UniProtKB on 1994-09.

Poole05a: Poole LB (2005). "Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases." Arch Biochem Biophys 433(1);240-54. PMID: 15581580

Quadroni96: Quadroni M, Staudenmann W, Kertesz M, James P (1996). "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Eur J Biochem 239(3);773-81. PMID: 8774726

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

Ravindra13: Ravindra Kumar S, Imlay JA (2013). "How Escherichia coli tolerates profuse hydrogen peroxide formation by a catabolic pathway." J Bacteriol 195(20);4569-79. PMID: 23913322

Ritz01: Ritz D, Lim J, Reynolds CM, Poole LB, Beckwith J (2001). "Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion." Science 294(5540);158-60. PMID: 11588261

Rothe12: Rothe M, Alpert C, Engst W, Musiol S, Loh G, Blaut M (2012). "Impact of nutritional factors on the proteome of intestinal Escherichia coli: induction of OxyR-dependent proteins AhpF and Dps by a lactose-rich diet." Appl Environ Microbiol 78(10);3580-91. PMID: 22427493

Rothe13: Rothe M, Blaut M (2013). "Evolution of the gut microbiota and the influence of diet." Benef Microbes 4(1);31-7. PMID: 23257016

SchurigBriccio09: Schurig-Briccio LA, Farias RN, Rodriguez-Montelongo L, Rintoul MR, Rapisarda VA (2009). "Protection against oxidative stress in Escherichia coli stationary phase by a phosphate concentration-dependent genes expression." Arch Biochem Biophys 483(1);106-10. PMID: 19138658

Seaver01: Seaver LC, Imlay JA (2001). "Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli." J Bacteriol 183(24);7182-9. PMID: 11717277

Seaver01a: Seaver LC, Imlay JA (2001). "Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli." J Bacteriol 183(24);7173-81. PMID: 11717276

Serina04: Serina S, Nozza F, Nicastro G, Faggioni F, Mottl H, Deho G, Polissi A (2004). "Scanning the Escherichia coli chromosome by random transposon mutagenesis and multiple phenotypic screening." Res Microbiol 155(8);692-701. PMID: 15380559

Smillie92: Smillie DA, Hayward RS, Suzuki T, Fujita N, Ishihama A (1992). "Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome." J Bacteriol 174(11);3826-7. PMID: 1592833

Storz89: Storz G, Jacobson FS, Tartaglia LA, Morgan RW, Silveira LA, Ames BN (1989). "An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp." J Bacteriol 171(4);2049-55. PMID: 2649484

Tsuji95: Tsuji K, Copeland NG, Jenkins NA, Obinata M (1995). "Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli." Biochem J 307 ( Pt 2);377-81. PMID: 7733872

Ueshima92: Ueshima R, Fujita N, Ishihama A (1992). "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit." Biochem Biophys Res Commun 184(2);634-9. PMID: 1575737

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

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

Villa12: Villa F, Remelli W, Forlani F, Vitali A, Cappitelli F (2012). "Altered expression level of Escherichia coli proteins in response to treatment with the antifouling agent zosteric acid sodium salt." Environ Microbiol 14(7);1753-61. PMID: 22176949

Wang09: Wang X, Zhao X (2009). "Contribution of oxidative damage to antimicrobial lethality." Antimicrob Agents Chemother 53(4);1395-402. PMID: 19223646

Wilkins98: Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278(3);599-608. PMID: 9600841

Yamamoto08a: Yamamoto Y, Ritz D, Planson AG, Jonsson TJ, Faulkner MJ, Boyd D, Beckwith J, Poole LB (2008). "Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity." Mol Cell 29(1);36-45. PMID: 18206967

Zhang09a: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Other References Related to Gene Regulation

Baez13: Baez A, Shiloach J (2013). "Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase." Microb Cell Fact 12;23. PMID: 23497217

Liu01: Liu R, Blackwell TW, States DJ (2001). "Conformational model for binding site recognition by the E.coli MetJ transcription factor." Bioinformatics 17(7);622-33. PMID: 11448880

Ozyamak13: Ozyamak E, de Almeida C, de Moura AP, Miller S, Booth IR (2013). "Integrated stress response of Escherichia coli to methylglyoxal: transcriptional readthrough from the nemRA operon enhances protection through increased expression of glyoxalase I." Mol Microbiol 88(5);936-50. PMID: 23646895

Storz90: Storz G, Tartaglia LA, Ames BN (1990). "Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation." Science 1990;248(4952);189-94. PMID: 2183352

Tartaglia89: Tartaglia LA, Storz G, Ames BN (1989). "Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress." J Mol Biol 1989;210(4);709-19. PMID: 2693740

Tartaglia92: Tartaglia LA, Gimeno CJ, Storz G, Ames BN (1992). "Multidegenerate DNA recognition by the OxyR transcriptional regulator." J Biol Chem 267(3);2038-45. PMID: 1730735

Toledano94: Toledano MB, Kullik I, Trinh F, Baird PT, Schneider TD, Storz G (1994). "Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection." Cell 78(5);897-909. PMID: 8087856

Zheng01a: Zheng M, Wang X, Doan B, Lewis KA, Schneider TD, Storz G (2001). "Computation-directed identification of OxyR DNA binding sites in Escherichia coli." J Bacteriol 183(15);4571-9. PMID: 11443092

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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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