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Escherichia coli K-12 substr. MG1655 Polypeptide: outer membrane protein A

Gene: ompA Accession Numbers: EG10669 (EcoCyc), b0957, ECK0948

Synonyms: con, tolG, tut, outer membrane protein II*, polypeptide II*, protein II*, outer membrane protein D, outer membrane protein 3a, outer membrane protein 0-11, outer membrane protein B

Regulation Summary Diagram: ?

Regulation summary diagram for ompA

OmpA is a member of the OmpA-OmpF Porin (OOP) family. OmpA is believed to be a nonspecific diffusion channel, allowing various small solutes to cross the outer membrane [Sugawara92]. OmpA is also thought to function as a phage receptor [Datta77] and as a mediator of F-factor dependent conjugation [Van77] and has been implicated in the maintenance of normal cell morphology [Sonntag78].

OmpA is 325 amino acids long and is one of the most abundant proteins in the outer membrane of E. coli [Sugawara94]. The structure of the full length protein remains unsettled (see review by [Reusch12].The structure of the transmembrane domain of OmpA has been determined by X-ray crystallography to a resolution of 2.5 and 1.65 Å [Pautsch98, Pautsch00], and by NMR spectroscopy [Arora01, Cierpicki06]. The mature form of OmpA is a large pore with no periplasmic domain; however, at low temperatures, OmpA forms a stable, 8-stranded all-next-neighbor antiparallel beta-barrel domain in the outer membrane with a small pore, tight periplasmic turns, large surface loops, and a large periplasmic C-terminal domain [Pautsch00, Arora01, Zakharian05]. This latter, two domain structure may represent a partially folded intermediate that is stable at low temperature [Zakharian05, Negoda10]. The C-terminal domain of OmpA may interact with the peptidoglycan layer in the periplasm [De94].

The gate of OmpA is a salt bridge within the channel that opens when alternate ion pairs form with the two residues [Hong06]. There is some debate as to whether OmpA is truly a channel having both open and closed conformation [Sugawara94], or whether the observed porin activity is artifactual. The surface exposed loops of OmpA are phage receptor sites and mutations in these regions reduce phage sensitivity [Morona85, Koebnik99, Power06].

OmpA was found as a dimer in the outer membrane [Stenberg05]. In vivo homomultimeric OmpA interaction was detected using cross-linking experiments. All the cross-link sites detected were in the C-terminal domain of OmpA [Zheng11]. OmpA forms both monomers and dimers in detergent micelles. The amino acid region from residue 188-276 is required for dimerisation [Marcoux14].

Targeting of OmpA to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06]. The periplasmic chaperone Skp, and lipopolysaccharide (LPS) are both required for efficient insertion and folding of OmpA into phospholipid bilayers in vitro. Binding to Skp maintains OmpA in an unfolded state in solution [Bulieris03]. OmpA is inserted into the outer membrane by the Bam outer membrane protein assembly complex [Doerrler05, Charlson06].

OmpA has been unfolded and refolded in vitro [Dornmair90, Surrey95, Surrey96]. Purified OmpA spontaneously refolds and inserts into lipid vesicles in vitro [Surrey92].

micA and rseX are small RNAs that bind as antisense RNAs to the translation initiation region of ompA mRNA, blocking ribosome binding and downregulating OmpA expression [Udekwu05, Douchin06]. micA binding also results in ompA mRNA destabilization by RNase E [Udekwu05, Andrade06]. This destabilization occurs when quickly growing cells enter stationary phase, and requires the RNA-binding protein Hfq [Udekwu05, Rasmussen05]. micA transcription is controlled by σE [Rhodius05, Johansen06]. In response to the σE envelope stress response, ompA transcription decreases [Rhodius05]. RNase R, PAPI, and PNPase are also involved in destabilization of the ompA mRNA transcript [Andrade06]. ompA expression increases as part of the Ntr response to help alleviate nitrogen limitation [Baev06].

OmpA is overexpressed during biofilmformation [Orme06] OmpA influences biofilm formation in a surface dependent manner by repressing cellulose production through the CpxRA stress response system [Barrios06, Ma09a]. ompA deletion mutants show increased cellulose production resulting in sticky colonies [Ma09a]. ompA cpxR double deletion mutants show no effect on cellulose production or biofilm formation [Ma09a].

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

Reviews: [Kleinschmidt03, Reusch12]

Citations: [Garten75, Endermann78, Danoff11, Muela08, Burgess08, Ried94, Qu09, Patel09, Qu07, Klose88, Schweizer78]

Gene Citations: [Chen80, Movva80, Beck80]

Locations: outer membrane

Map Position: [1,018,236 <- 1,019,276] (21.95 centisomes, 79°)
Length: 1041 bp / 346 aa

Molecular Weight of Polypeptide: 37.201 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003240 , CGSC:437 , DIP:DIP-31879N , EchoBASE:EB0663 , EcoGene:EG10669 , EcoliWiki:b0957 , Mint:MINT-1308131 , ModBase:P0A910 , OU-Microarray:b0957 , PortEco:ompA , PR:PRO_000023450 , Pride:P0A910 , Protein Model Portal:P0A910 , RefSeq:NP_415477 , RegulonDB:EG10669 , SMR:P0A910 , String:511145.b0957 , Swiss-Model:P0A910 , UniProt:P0A910

Relationship Links: InterPro:IN-FAMILY:IPR000498 , InterPro:IN-FAMILY:IPR002368 , InterPro:IN-FAMILY:IPR006664 , InterPro:IN-FAMILY:IPR006665 , InterPro:IN-FAMILY:IPR006690 , InterPro:IN-FAMILY:IPR011250 , PDB:Structure:1BXW , PDB:Structure:1G90 , PDB:Structure:1QJP , PDB:Structure:2GE4 , PDB:Structure:2JMM , PDB:Structure:3NB3 , Pfam:IN-FAMILY:PF00691 , Pfam:IN-FAMILY:PF01389 , Prints:IN-FAMILY:PR01021 , Prints:IN-FAMILY:PR01022 , Prosite:IN-FAMILY:PS01068 , Prosite:IN-FAMILY:PS51123

In Paralogous Gene Group: 231 (2 members)

Genetic Regulation Schematic: ?

Genetic regulation schematic for ompA

GO Terms:

Biological Process: GO:0000746 - conjugation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Ried87]
GO:0006810 - transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Arora00]
GO:0006811 - ion transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Arora00]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0009597 - detection of virus Inferred from experiment [Henning78]
GO:0034220 - ion transmembrane transport Inferred from experiment [Arora00]
GO:0046718 - viral entry into host cell Inferred from experiment [Henning78]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Zheng11, Ge13, Arifuzzaman06, MartinezHackert09]
GO:0015288 - porin activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Sugawara92, Arora00]
GO:0042802 - identical protein binding Inferred from experiment [Zheng11]
GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a, Arutyunov10, Klose88a, Bulieris03]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Bulieris03]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Klose88, Bulieris03]
GO:0019867 - outer membrane Inferred from experiment [Klose88a, Bulieris03]
GO:0046930 - pore complex Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Pautsch00, Sugawara92]

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

Essentiality data for ompA 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]

Curated 09-Apr-2007 by Johnson A , TIGR
Last-Curated ? 04-Jun-2014 by Mackie A , Macquarie University

Sequence Features

Protein sequence of outer membrane protein A with features indicated

Feature Class Location Common Name Citations Comment
Signal-Sequence 1 -> 21 OmpA signal sequence
[Pasquali94, Chen80, Molloy98, Link97, Pautsch98]
Chain 22 -> 346  
UniProt: Outer membrane protein A;
Transmembrane-Region 27 -> 37 β1 strand
Transmembrane-Region 55 -> 66 β2 strand
Transmembrane-Region 70 -> 78 β3 strand
Transmembrane-Region 96 -> 107 β4 strand
Transmembrane-Region 112 -> 124 β5 strand
Transmembrane-Region 138 -> 151 β6 strand
Transmembrane-Region 156 -> 163 β7 strand
Transmembrane-Region 182 -> 190 β8 strand
Protein-Binding-Region 188 -> 276  
Implicated in dimer interface
Protein-Segment 197 -> 208  
[UniProt10, Marcoux14]
UniProt: Hinge-like; Sequence Annotation Type: region of interest;
Protein-Segment 201 -> 208  
UniProt: 4 X 2 AA tandem repeats of A-P; Sequence Annotation Type: region of interest;
Repeat 201 -> 202  
UniProt: 1;
Repeat 203 -> 204  
UniProt: 2;
Repeat 205 -> 206  
UniProt: 3;
Repeat 207 -> 208  
UniProt: 4;
Conserved-Region 210 -> 338  
[UniProt09, Marcoux14]
UniProt: OmpA-like; may interact with peptidoglycan
Disulfide-Bond-Site 311, 323  

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b0957 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10669; confirmed by SwissProt match.


Andrade06: Andrade JM, Cairrao F, Arraiano CM (2006). "RNase R affects gene expression in stationary phase: regulation of ompA." Mol Microbiol 60(1);219-28. PMID: 16556233

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Arora00: Arora A, Rinehart D, Szabo G, Tamm LK (2000). "Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers." J Biol Chem 275(3);1594-600. PMID: 10636850

Arora01: Arora A, Abildgaard F, Bushweller JH, Tamm LK (2001). "Structure of outer membrane protein A transmembrane domain by NMR spectroscopy." Nat Struct Biol 8(4);334-8. PMID: 11276254

Arutyunov10: Arutyunov D, Arenson B, Manchak J, Frost LS (2010). "F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation." J Bacteriol 192(6);1730-4. PMID: 20081027

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

Baev06: Baev MV, Baev D, Radek AJ, Campbell JW (2006). "Growth of Escherichia coli MG1655 on LB medium: monitoring utilization of amino acids, peptides, and nucleotides with transcriptional microarrays." Appl Microbiol Biotechnol 71(3);317-22. PMID: 16575570

Barrios06: Barrios AF, Zuo R, Ren D, Wood TK (2006). "Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility." Biotechnol Bioeng 93(1);188-200. PMID: 16317765

Beck80: Beck E, Bremer E (1980). "Nucleotide sequence of the gene ompA coding the outer membrane protein II of Escherichia coli K-12." Nucleic Acids Res 8(13);3011-27. PMID: 6253901

Bulieris03: Bulieris PV, Behrens S, Holst O, Kleinschmidt JH (2003). "Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide." J Biol Chem 278(11);9092-9. PMID: 12509434

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

Charlson06: Charlson ES, Werner JN, Misra R (2006). "Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide." J Bacteriol 188(20);7186-94. PMID: 17015657

Chen80: Chen R, Schmidmayr W, Kramer C, Chen-Schmeisser U, Henning U (1980). "Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12." Proc Natl Acad Sci U S A 77(8);4592-6. PMID: 7001461

Cierpicki06: Cierpicki T, Liang B, Tamm LK, Bushweller JH (2006). "Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A." J Am Chem Soc 128(21);6947-51. PMID: 16719475

Danoff11: Danoff EJ, Fleming KG (2011). "The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel." Biophys Chem 159(1);194-204. PMID: 21782315

Datta77: Datta DB, Arden B, Henning U (1977). "Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors." J Bacteriol 1977;131(3);821-9. PMID: 330500

De94: De Mot R, Vanderleyden J (1994). "The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan." Mol Microbiol 12(2);333-4. PMID: 8057857

Doerrler05: Doerrler WT, Raetz CR (2005). "Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant." J Biol Chem 280(30);27679-87. PMID: 15951436

Dornmair90: Dornmair K, Kiefer H, Jahnig F (1990). "Refolding of an integral membrane protein. OmpA of Escherichia coli." J Biol Chem 265(31);18907-11. PMID: 2229053

Douchin06: Douchin V, Bohn C, Bouloc P (2006). "Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli." J Biol Chem 281(18);12253-9. PMID: 16513633

Endermann78: Endermann R, Kramer C, Henning U (1978). "Major outer membrane proteins of Escherichia coli K-12: evidence for protein II being a transmembrane protein." FEBS Lett 86(1);21-4. PMID: 340280

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

Garten75: Garten W, Hindennach I, Henning U (1975). "The major proteins of the Escherichia coli outer cell envelope membrane. Characterization of proteins II* and III, comparison of all proteins." Eur J Biochem 59(1);215-21. PMID: 1107024

Ge13: Ge X, Wang R, Ma J, Liu Y, Ezemaduka AN, Chen PR, Fu X, Chang Z (2013). "DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli." FEBS J. PMID: 24373465

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."

Henning78: Henning U, Sonntag I, Hindennach I (1978). "Mutants (ompA) affecting a major outer membrane protein of Escherichia coli K12." Eur J Biochem 92(2);491-8. PMID: 367782

Hong06: Hong H, Szabo G, Tamm LK (2006). "Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening." Nat Chem Biol 2(11);627-35. PMID: 17041590

Johansen06: Johansen J, Rasmussen AA, Overgaard M, Valentin-Hansen P (2006). "Conserved small non-coding RNAs that belong to the sigmaE regulon: role in down-regulation of outer membrane proteins." J Mol Biol 364(1);1-8. PMID: 17007876

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

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Kleinschmidt03: Kleinschmidt JH (2003). "Membrane protein folding on the example of outer membrane protein A of Escherichia coli." Cell Mol Life Sci 60(8);1547-58. PMID: 14513830

Klose88: Klose M, MacIntyre S, Schwarz H, Henning U (1988). "The influence of amino substitutions within the mature part of an Escherichia coli outer membrane protein (OmpA) on assembly of the polypeptide into its membrane." J Biol Chem 263(26);13297-302. PMID: 3047121

Klose88a: Klose M, Schwarz H, MacIntyre S, Freudl R, Eschbach ML, Henning U (1988). "Internal deletions in the gene for an Escherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide." J Biol Chem 263(26);13291-6. PMID: 3047120

Koebnik99: Koebnik R (1999). "Structural and functional roles of the surface-exposed loops of the beta-barrel membrane protein OmpA from Escherichia coli." J Bacteriol 181(12);3688-94. PMID: 10368142

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

Ma09a: Ma Q, Wood TK (2009). "OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system." Environ Microbiol. PMID: 19601955

Marcoux14: Marcoux J, Politis A, Rinehart D, Marshall DP, Wallace MI, Tamm LK, Robinson CV (2014). "Mass Spectrometry Defines the C-Terminal Dimerization Domain and Enables Modeling of the Structure of Full-Length OmpA." Structure 22(5);781-90. PMID: 24746938

MartinezHackert09: Martinez-Hackert E, Hendrickson WA (2009). "Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone." Cell 138(5);923-34. PMID: 19737520

Molloy98: Molloy MP, Herbert BR, Walsh BJ, Tyler MI, Traini M, Sanchez JC, Hochstrasser DF, Williams KL, Gooley AA (1998). "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis." Electrophoresis 19(5);837-44. PMID: 9629924

Morona85: Morona R, Kramer C, Henning U (1985). "Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12." J Bacteriol 164(2);539-43. PMID: 3902787

Movva80: Movva NR, Nakamura K, Inouye M (1980). "Regulatory region of the gene for the ompA protein, a major outer membrane protein of Escherichia coli." Proc Natl Acad Sci U S A 77(7);3845-9. PMID: 7001445

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

Negoda10: Negoda A, Negoda E, Reusch RN (2010). "Resolving the native conformation of Escherichia coli OmpA." FEBS J 277(21);4427-37. PMID: 21069910

Orme06: Orme R, Douglas CW, Rimmer S, Webb M (2006). "Proteomic analysis of Escherichia coli biofilms reveals the overexpression of the outer membrane protein OmpA." Proteomics 6(15);4269-77. PMID: 16888722

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

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.

Patel09: Patel GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH (2009). "The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential." Biochemistry 48(43);10235-45. PMID: 19780589

Pautsch00: Pautsch A, Schulz GE (2000). "High-resolution structure of the OmpA membrane domain." J Mol Biol 298(2);273-82. PMID: 10764596

Pautsch98: Pautsch A, Schulz GE (1998). "Structure of the outer membrane protein A transmembrane domain." Nat Struct Biol 5(11);1013-7. PMID: 9808047

Power06: Power ML, Ferrari BC, Littlefield-Wyer J, Gordon DM, Slade MB, Veal DA (2006). "A naturally occurring novel allele of Escherichia coli outer membrane protein A reduces sensitivity to bacteriophage." Appl Environ Microbiol 72(12);7930-2. PMID: 16980421

Qu07: Qu J, Mayer C, Behrens S, Holst O, Kleinschmidt JH (2007). "The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions." J Mol Biol 374(1);91-105. PMID: 17928002

Qu09: Qu J, Behrens-Kneip S, Holst O, Kleinschmidt JH (2009). "Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study." Biochemistry 48(22);4926-36. PMID: 19382746

Rasmussen05: Rasmussen AA, Eriksen M, Gilany K, Udesen C, Franch T, Petersen C, Valentin-Hansen P (2005). "Regulation of ompA mRNA stability: the role of a small regulatory RNA in growth phase-dependent control." Mol Microbiol 58(5);1421-9. PMID: 16313626

Reusch12: Reusch RN (2012). "Insights into the structure and assembly of Escherichia coli outer membrane protein A." FEBS J. PMID: 22251410

Rhodius05: Rhodius VA, Suh WC, Nonaka G, West J, Gross CA (2005). "Conserved and variable functions of the sigmaE stress response in related genomes." PLoS Biol 4(1);e2. PMID: 16336047

Ried87: Ried G, Henning U (1987). "A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K-12." FEBS Lett 223(2);387-90. PMID: 3311813

Ried94: Ried G, Koebnik R, Hindennach I, Mutschler B, Henning U (1994). "Membrane topology and assembly of the outer membrane protein OmpA of Escherichia coli K12." Mol Gen Genet 243(2);127-35. PMID: 8177210

Schweizer78: Schweizer M, Hindennach I, Garten W, Henning U (1978). "Major proteins of the Escherichia coli outer cell envelope membrane. Interaction of protein II with lipopolysaccharide." Eur J Biochem 82(1);211-7. PMID: 340230

Sonntag78: Sonntag I, Schwarz H, Hirota Y, Henning U (1978). "Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins." J Bacteriol 136(1);280-5. PMID: 361695

Stenberg05: Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280(41);34409-19. PMID: 16079137

Sugawara92: Sugawara E, Nikaido H (1992). "Pore-forming activity of OmpA protein of Escherichia coli." J Biol Chem 1992;267(4);2507-11. PMID: 1370823

Sugawara94: Sugawara E, Nikaido H (1994). "OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms." J Biol Chem 1994;269(27);17981-7. PMID: 7517935

Surrey92: Surrey T, Jahnig F (1992). "Refolding and oriented insertion of a membrane protein into a lipid bilayer." Proc Natl Acad Sci U S A 89(16);7457-61. PMID: 1502158

Surrey95: Surrey T, Jahnig F (1995). "Kinetics of folding and membrane insertion of a beta-barrel membrane protein." J Biol Chem 270(47);28199-203. PMID: 7499313

Surrey96: Surrey T, Schmid A, Jahnig F (1996). "Folding and membrane insertion of the trimeric beta-barrel protein OmpF." Biochemistry 35(7);2283-8. PMID: 8652568

Udekwu05: Udekwu KI, Darfeuille F, Vogel J, Reimegard J, Holmqvist E, Wagner EG (2005). "Hfq-dependent regulation of OmpA synthesis is mediated by an antisense RNA." Genes Dev 19(19);2355-66. PMID: 16204185

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 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."

Van77: Van Alphen L, Havekes L, Lugtenberg B (1977). "Major outer membrane protein d of Escherichia coli K12. Purification and in vitro activity of bacteriophages k3 and f-pilus mediated conjugation." FEBS Lett 1977;75(1);285-90. PMID: 323051

Zakharian05: Zakharian E, Reusch RN (2005). "Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer." Biochemistry 44(17);6701-7. PMID: 15850404

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Other References Related to Gene Regulation

Cole82b: Cole ST, Bremer E, Hindennach I, Henning U (1982). "Characterisation of the promoters for the ompA gene which encodes a major outer membrane protein of Escherichia coli." Mol Gen Genet 1982;188(3);472-9. PMID: 6298577

Gibert90: Gibert I, Barbe J (1990). "Cyclic AMP stimulates transcription of the structural gene of the outer-membrane protein OmpA of Escherichia coli." FEMS Microbiol Lett 56(3);307-11. PMID: 2160397

Lin11: Lin HH, Hsu CC, Yang CD, Ju YW, Chen YP, Tseng CP (2011). "Negative Effect of Glucose on ompA mRNA Stability: a Potential Role of Cyclic AMP in the Repression of hfq in Escherichia coli." J Bacteriol 193(20);5833-40. PMID: 21840983

Movva81: Movva RN, Green P, Nakamura K, Inouye M (1981). "Interaction of cAMP receptor protein with the ompA gene, a gene for a major outer membrane protein of Escherichia coli." FEBS Lett 1981;128(2);186-90. PMID: 7021177

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Viveiros07: Viveiros M, Dupont M, Rodrigues L, Couto I, Davin-Regli A, Martins M, Pages JM, Amaral L (2007). "Antibiotic stress, genetic response and altered permeability of E. coli." PLoS ONE 2;e365. PMID: 17426813

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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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