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Pathway Description
Operon: Carnitine Operon
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Signaling
Created: 2015-09-08
Last Updated: 2019-08-16
The caiTABCDE operon in E. coli contains six genes that produce proteins involved in the anaerobic metabolism of carnitine. This operon can be activated by the aerobic respiration control protein ArcA, which binds to several places upstream of the promoter. This binding activates transcription in the proper conditions, such as the need for fermentative metabolism. The operon can also be repressed by the DNA-binding protein H-NS. This protein binds to and alters the structure of DNA, suppressing the genes until it is removed. Finally, the caiA gene mRNA can specifically be prevented from being translated by small regulatory RNA that binds to the transcript, while the other genes are translated normally.
The first gene in the operon, caiT, encodes for the L-carnitine/gamma butyrobetaine antiporter protein, which is responsible for transporting methyl-L-carninte into the cell, while transporting gamma butyrobetaine out of it.
The second gene, caiA, encodes crotonobetainyl-CoA reductase, a protein that catalyzes the conversion of crotonobetainyl-CoA into gamma-butyrobetainyl-CoA. This protein is thought to interact with L-carnitine CoA-transferase, the protein encoded by caiB, which transfers the CoA from gamma-butyrobetainyl-CoA to L-carnitine, forming L-carnityl-CoA and gamma-butyrobetaine. It can also transfer between crotonobetainyl-CoA and L-carnitine.
The fourth gene in the operon, caiC, encodes a crotonobetaine/carnitine CoA ligase, which like caiB catalyzes the reversible transfer of CoA between carnitine, gamma-butyrobetaine and crotobetaine.
The fifth gene, caiD, encodes carnitinyl-CoA dehydratase, which reversibly removes a water molecule from crotonobetainyl-CoA, forming carnitinyl-CoA.
The final gene, caiE, encodes a putative transferase whose function is currently unknown. However, when the protein is overexpressed, it functions similarly to caiB and caiD, as a CoA ligase and dehydratase.
References
Operon: Carnitine Operon References
Kleber HP: Bacterial carnitine metabolism. FEMS Microbiol Lett. 1997 Feb 1;147(1):1-9.
Pubmed: 9037756
Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA: Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol Microbiol. 1994 Sep;13(5):775-86.
Pubmed: 7815937
Buchet A, Eichler K, Mandrand-Berthelot MA: Regulation of the carnitine pathway in Escherichia coli: investigation of the cai-fix divergent promoter region. J Bacteriol. 1998 May;180(10):2599-608.
Pubmed: 9573142
Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA: Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol Microbiol. 1994 Sep;13(5):775-86. doi: 10.1111/j.1365-2958.1994.tb00470.x.
Pubmed: 7815937
Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. doi: 10.1093/nar/20.13.3305.
Pubmed: 1630901
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. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Eichler K, Schunck WH, Kleber HP, Mandrand-Berthelot MA: Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase. J Bacteriol. 1994 May;176(10):2970-5. doi: 10.1128/jb.176.10.2970-2975.1994.
Pubmed: 8188598
Pon CL, Calogero RA, Gualerzi CO: Identification, cloning, nucleotide sequence and chromosomal map location of hns, the structural gene for Escherichia coli DNA-binding protein H-NS. Mol Gen Genet. 1988 May;212(2):199-202. doi: 10.1007/bf00334684.
Pubmed: 2841565
La Teana A, Falconi M, Scarlato V, Lammi M, Pon CL: Characterization of the structural genes for the DNA-binding protein H-NS in Enterobacteriaceae. FEBS Lett. 1989 Feb 13;244(1):34-8. doi: 10.1016/0014-5793(89)81156-1.
Pubmed: 2494066
Falconi M, Gualtieri MT, La Teana A, Losso MA, Pon CL: Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS. Mol Microbiol. 1988 May;2(3):323-9. doi: 10.1111/j.1365-2958.1988.tb00035.x.
Pubmed: 3135462
Drury LS, Buxton RS: DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins. J Biol Chem. 1985 Apr 10;260(7):4236-42.
Pubmed: 2984198
Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. doi: 10.1093/nar/23.12.2105.
Pubmed: 7610040
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