Gene Symbol: ppiA
Description: peptidyl-prolyl cis-trans isomerase A (rotamase A)
Alias: ECK3351, JW3326, rot, rotA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     ppiA

Top Publications

  1. Nørregaard Madsen M, Mygind B, Pedersen R, Valentin Hansen P, Søgaard Andersen L. The gene encoding the periplasmic cyclophilin homologue, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor. Mol Microbiol. 1994;14:989-97 pubmed
    The rot gene in Escherichia coli encodes PPIase A, a periplasmic peptidyl-prolyl cis-trans isomerase with homology to the cyclophilin family of proteins...
  2. Kleerebezem M, Heutink M, Tommassen J. Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase. Mol Microbiol. 1995;18:313-20 pubmed
    The rotA gene of Escherichia coli encodes a peptidyl-prolyl cis/trans isomerase (PPIase), which is supposed to catalyse protein folding in the periplasm...
  3. Konno M, Sano Y, Okudaira K, Kawaguchi Y, Yamagishi Ohmori Y, Fushinobu S, et al. Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer. Eur J Biochem. 2004;271:3794-803 pubmed
  4. Pogliano J, Lynch A, Belin D, Lin E, Beckwith J. Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev. 1997;11:1169-82 pubmed
    ..shown that phosphorylated CpxR binds to elements upstream of the transcription start sites of dsbA, degP, and ppiA (rotA), the latter coding for a peptidyl-prolyl cis/trans isomerase...
  5. Liu J, Chen C, Walsh C. Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991;30:2306-10 pubmed
  6. Fejzo J, Etzkorn F, Clubb R, Shi Y, Walsh C, Wagner G. The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin. Biochemistry. 1994;33:5711-20 pubmed
    ..coli protein is substantially different at the site most distant to tryptophan 121 (human sequence). This site is constructed by a five-residue insertion in a loop of the E. coli protein, replacing another loop in the human protein. ..
  7. Justice S, Hunstad D, Harper J, Duguay A, Pinkner J, Bann J, et al. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J Bacteriol. 2005;187:7680-6 pubmed
    In Escherichia coli, FkpA, PpiA, PpiD, and SurA are the four known periplasmic cis-trans prolyl isomerases...
  8. Schönbrunner E, Schmid F. Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc Natl Acad Sci U S A. 1992;89:4510-3 pubmed
    ..The interdependence of the two enzymatic activities detected during in vitro folding experiments could be of importance for the de novo folding and disulfide bond formation of nascent proteins in the endoplasmic reticulum. ..
  9. Hayano T, Takahashi N, Kato S, Maki N, Suzuki M. Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells. Biochemistry. 1991;30:3041-8 pubmed
    ..Thus, we propose that the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase and, in turn, that some proteins which have isomerized may not be translocated efficiently. ..

More Information


  1. Konno M, Ito M, Hayano T, Takahashi N. The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer. J Mol Biol. 1996;256:897-908 pubmed
    ..Thus, the extra amino acid residue of E. coli CyPA, polar Gln89, lies along the pathway to the hydrophobic pocket of CyPA and seems to prevent the access hydrophobic part of CsA to the cleft of CyPA. ..
  2. Tran P, Bannor T, Doktor S, Nichols B. Chromosomal organization and expression of Escherichia coli pabA. J Bacteriol. 1990;172:397-410 pubmed
    ..The significance of these results and possible posttranscriptional control mechanisms which affect PabA expression from the P2-initiated polycistronic unit are discussed. ..
  3. Kawamukai M, Matsuda H, Fujii W, Utsumi R, Komano T. Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli. J Bacteriol. 1989;171:4525-9 pubmed
    ..coli. In addition, ORF190 has sequence similarity with the cyclosporin A-binding protein cyclophilin. ..
  4. Clubb R, Ferguson S, Walsh C, Wagner G. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry. 1994;33:2761-72 pubmed
    ..A residue essential for isomerase activity in human T cell cyclophilin (His126) is replaced by Tyr122 in E. coli cyclophilin without affecting enzymatic activity. ..
  5. Compton L, Davis J, MacDonald J, Bachinger H. Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases. Eur J Biochem. 1992;206:927-34 pubmed
    ..Circular dichroism spectroscopy indicates that the secondary structure of the cationic protein consists of 17% alpha-helix, 34% beta-sheet, 17% turns, 33% random coil and is very similar to human cytosolic PPIase. ..
  6. Liu J, Walsh C. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc Natl Acad Sci U S A. 1990;87:4028-32 pubmed
    ..The E. coli rotamase, a product of the gene we suggest be called "rot," has been purified to homogeneity after cloning of the gene by the polymerase chain reaction and its ..