Outer membrane protein A

Details

Name
Outer membrane protein A
Kind
protein
Synonyms
  • con
  • Outer membrane protein II*
  • tolG
  • tut
Gene Name
ompA
UniProtKB Entry
P0A910Swiss-Prot
Organism
Escherichia coli (strain K12)
NCBI Taxonomy ID
83333
Amino acid sequence
>lcl|BSEQ0011477|Outer membrane protein A
MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGA
FGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGG
MVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDN
GMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQ
LYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGM
GESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA
Number of residues
346
Molecular Weight
37200.545
Theoretical pI
6.37
GO Classification
Functions
porin activity / structural molecule activity
Processes
cellular response to DNA damage stimulus / conjugation / detection of virus / ion transmembrane transport / ion transport / transport / viral entry into host cell
Components
cell outer membrane / integral component of membrane / membrane / outer membrane / pore complex
General Function
With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape (PubMed:11906175, PubMed:361695). Non-covalently binds peptidoglycan (Probable) (PubMed:25135663). Acts as a porin with low permeability that allows slow penetration of small solutes (PubMed:1370823, PubMed:20004640, PubMed:21069910). A very abundant protein, there can be up to 210,000 OmpA molecules per cell (PubMed:24766808). Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at a rate comparable to that of OmpF porin; the pores interconvert very rarely (PubMed:7517935). Native and reconstituted protein forms ion channels with 2 conductance states of (50-80 pS) and (260-320 pS); the states are interconvertible in this study. Interconversion requires refolding of the periplasmic domain (PubMed:10636850). Small pores are converted into large pores by increasing temperature; in this model the C-terminal periplasmic domain forms 8 more beta sheets to form a larger pore (PubMed:15850404). The center of the isolated beta-barrel is polar and has a central gate (involving Glu-73, Lys-103, Glu-149 and Arg-159, sandwiched between Tyr-29, Phe-40 and Tyr-94), with no obvious passage for water or ions (Probable) (PubMed:9808047). Gating involves the Glu-73-Arg-159 salt bridge; gate opening probably involves formation of alternate salt bridges Glu-149-Arg-159 and Glu-73-Lys-103 (PubMed:17041590). Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable).
Specific Function
identical protein binding
Pfam Domain Function
Signal Regions
1-21
Transmembrane Regions
27-37 55-66 70-78 96-107 112-124 138-151 156-163 182-190
Cellular Location
Cell outer membrane
Gene sequence
>lcl|BSEQ0011478|Outer membrane protein A (ompA)
ATGAAAAAGACAGCTATCGCGATTGCAGTGGCACTGGCTGGTTTCGCTACCGTAGCGCAG
GCCGCTCCGAAAGATAACACCTGGTACACTGGTGCTAAACTGGGCTGGTCCCAGTACCAT
GACACTGGTTTCATCAACAACAATGGCCCGACCCATGAAAACCAACTGGGCGCTGGTGCT
TTTGGTGGTTACCAGGTTAACCCGTATGTTGGCTTTGAAATGGGTTACGACTGGTTAGGT
CGTATGCCGTACAAAGGCAGCGTTGAAAACGGTGCATACAAAGCTCAGGGCGTTCAACTG
ACCGCTAAACTGGGTTACCCAATCACTGACGACCTGGACATCTACACTCGTCTGGGTGGC
ATGGTATGGCGTGCAGACACTAAATCCAACGTTTATGGTAAAAACCACGACACCGGCGTT
TCTCCGGTCTTCGCTGGCGGTGTTGAGTACGCGATCACTCCTGAAATCGCTACCCGTCTG
GAATACCAGTGGACCAACAACATCGGTGACGCACACACCATCGGCACTCGTCCGGACAAC
GGCATGCTGAGCCTGGGTGTTTCCTACCGTTTCGGTCAGGGCGAAGCAGCTCCAGTAGTT
GCTCCGGCTCCAGCTCCGGCACCGGAAGTACAGACCAAGCACTTCACTCTGAAGTCTGAC
GTTCTGTTCAACTTCAACAAAGCAACCCTGAAACCGGAAGGTCAGGCTGCTCTGGATCAG
CTGTACAGCCAGCTGAGCAACCTGGATCCGAAAGACGGTTCCGTAGTTGTTCTGGGTTAC
ACCGACCGCATCGGTTCTGACGCTTACAACCAGGGTCTGTCCGAGCGCCGTGCTCAGTCT
GTTGTTGATTACCTGATCTCCAAAGGTATCCCGGCAGACAAGATCTCCGCACGTGGTATG
GGCGAATCCAACCCGGTTACTGGCAACACCTGTGACAACGTGAAACAGCGTGCTGCACTG
ATCGACTGCCTGGCTCCGGATCGTCGCGTAGAGATCGAAGTTAAAGGTATCAAAGACGTT
GTAACTCAGCCGCAGGCTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A910
UniProtKB Entry NameOMPA_ECOLI
GenBank Protein ID42160
GenBank Gene IDV00307
PDB ID(s)1BXW, 1G90, 1QJP, 2GE4, 2JMM, 3NB3
KEGG IDecj:JW0940
NCBI Gene ID945571
General References
  1. Beck E, Bremer E: Nucleotide sequence of the gene ompA coding the outer membrane protein II of Escherichia coli K-12. Nucleic Acids Res. 1980 Jul 11;8(13):3011-27. [Article]
  2. Movva NR, Nakamura K, Inouye M: Gene structure of the OmpA protein, a major surface protein of Escherichia coli required for cell-cell interaction. J Mol Biol. 1980 Nov 5;143(3):317-28. [Article]
  3. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Chen R, Schmidmayr W, Kramer C, Chen-Schmeisser U, Henning U: Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4592-6. [Article]
  7. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  8. Molloy MP, Herbert BR, Walsh BJ, Tyler MI, Traini M, Sanchez JC, Hochstrasser DF, Williams KL, Gooley AA: Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Electrophoresis. 1998 May;19(5):837-44. [Article]
  9. Morona R, Klose M, Henning U: Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins. J Bacteriol. 1984 Aug;159(2):570-8. [Article]
  10. Morona R, Kramer C, Henning U: Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12. J Bacteriol. 1985 Nov;164(2):539-43. [Article]
  11. Sugawara E, Nikaido H: Pore-forming activity of OmpA protein of Escherichia coli. J Biol Chem. 1992 Feb 5;267(4):2507-11. [Article]
  12. Kuhn A, Kiefer D, Kohne C, Zhu HY, Tschantz WR, Dalbey RE: Evidence for a loop-like insertion mechanism of pro-Omp A into the inner membrane of Escherichia coli. Eur J Biochem. 1994 Dec 15;226(3):891-7. [Article]
  13. Gromiha MM, Ponnuswamy PK: Prediction of transmembrane beta-strands from hydrophobic characteristics of proteins. Int J Pept Protein Res. 1993 Nov;42(5):420-31. [Article]
  14. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  15. Koebnik R: Structural and functional roles of the surface-exposed loops of the beta-barrel membrane protein OmpA from Escherichia coli. J Bacteriol. 1999 Jun;181(12):3688-94. [Article]
  16. Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3. [Article]
  17. Fontaine F, Fuchs RT, Storz G: Membrane localization of small proteins in Escherichia coli. J Biol Chem. 2011 Sep 16;286(37):32464-74. doi: 10.1074/jbc.M111.245696. Epub 2011 Jul 21. [Article]
  18. Pautsch A, Schulz GE: Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol. 1998 Nov;5(11):1013-7. [Article]
  19. Pautsch A, Schulz GE: High-resolution structure of the OmpA membrane domain. J Mol Biol. 2000 Apr 28;298(2):273-82. [Article]
  20. Arora A, Abildgaard F, Bushweller JH, Tamm LK: Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat Struct Biol. 2001 Apr;8(4):334-8. [Article]
  21. le Coutre J, Whitelegge JP, Gross A, Turk E, Wright EM, Kaback HR, Faull KF: Proteomics on full-length membrane proteins using mass spectrometry. Biochemistry. 2000 Apr 18;39(15):4237-42. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
(Hydroxyethyloxy)Tri(Ethyloxy)OctaneexperimentalunknowntargetDetails