Peptidyl-prolyl cis-trans isomerase A (P0AFL3)

Identification
Name:Peptidyl-prolyl cis-trans isomerase A
Synonyms:
  • PPIase A
  • Cyclophilin A
  • Rotamase A
Gene Name:ppiA
Enzyme Class:
Biological Properties
General Function:Posttranslational modification, protein turnover, chaperones
Specific Function:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
  • Cationic antimicrobial peptide (CAMP) resistance eco01503
KEGG Reactions:
1.0Peptidylproline (omega=180) ↔ 1.0Peptidylproline (omega=0)
1.0Peptidylproline (omega=180) ↔ 1.0Peptidylproline (omega=0)
ReactionCard
Metabolites:
ECMDB IDNameView
GO Classification:
Function
catalytic activity
cis-trans isomerase activity
isomerase activity
peptidyl-prolyl cis-trans isomerase activity
Process
cellular protein metabolic process
macromolecule metabolic process
metabolic process
protein folding
protein metabolic process
Gene Properties
Blattner:Not Available
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>573 bp
ATGTTCAAATCGACCCTGGCGGCGATGGCTGCTGTTTTCGCTCTTTCTGCTCTTTCTCCC
GCTGCAATGGCAGCGAAAGGGGACCCGCACGTATTGTTGACAACCTCAGCTGGTAACATC
GAACTGGAGCTGGATAAACAAAAAGCGCCAGTGTCTGTGCAAAACTTTGTCGATTATGTG
AACAGCGGTTTTTATAACAACACTACCTTTCACCGCGTCATTCCTGGCTTTATGATTCAG
GGCGGCGGTTTCACCGAGCAGATGCAGCAGAAAAAACCAAACCCGCCAATCAAAAATGAA
GCCGATAACGGCCTGCGCAACACGCGTGGCACCATCGCGATGGCACGTACCGCTGACAAA
GACAGCGCCACCAGCCAGTTCTTTATCAACGTTGCCGATAACGCCTTCCTTGACCATGGT
CAGCGTGATTTCGGTTACGCGGTATTTGGTAAAGTGGTGAAAGGCATGGACGTTGCCGAT
AAGATTTCCCAGGTGCCGACTCATGACGTTGGTCCGTACCAGAATGTGCCGTCAAAACCG
GTAGTTATCCTTTCCGCTAAAGTCCTGCCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:190
Protein Molecular Weight:20431
Protein Theoretical pI:9
PDB File:1CLH
Signaling Regions:
  • 1-24
Transmembrane Regions:
  • None
Protein Sequence:
>Peptidyl-prolyl cis-trans isomerase A
MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYV
NSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADK
DSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKP
VVILSAKVLP
References
External Links:
ResourceLink
Uniprot ID:P0AFL3
Uniprot Name:PPIA_ECOLI
GenBank Gene ID:M28363
Genebank Protein ID:145954
PDB ID:1CLH
CCDB:PPIA_ECOLI
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Clubb, R. T., Ferguson, S. B., Walsh, C. T., Wagner, G. (1994). "Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin." Biochemistry 33:2761-2772. Pubmed: 8130188
  • Compton, L. A., Davis, J. M., Macdonald, J. R., Bachinger, H. P. (1992). "Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases." Eur J Biochem 206:927-934. Pubmed: 1606970
  • Fejzo, J., Etzkorn, F. A., Clubb, R. T., Shi, Y., Walsh, C. T., Wagner, G. (1994). "The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin." Biochemistry 33:5711-5720. Pubmed: 8180197
  • Hayano, T., Takahashi, N., Kato, S., Maki, N., Suzuki, M. (1991). "Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells." Biochemistry 30:3041-3048. Pubmed: 2007139
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kawamukai, M., Matsuda, H., Fujii, W., Utsumi, R., Komano, T. (1989). "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli." J Bacteriol 171:4525-4529. Pubmed: 2546924
  • Liu, J., Chen, C. M., Walsh, C. T. (1991). "Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue." Biochemistry 30:2306-2310. Pubmed: 2001362
  • Liu, J., Walsh, C. T. (1990). "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 87:4028-4032. Pubmed: 2190212
  • Tran, P. V., Bannor, T. A., Doktor, S. Z., Nichols, B. P. (1990). "Chromosomal organization and expression of Escherichia coli pabA." J Bacteriol 172:397-410. Pubmed: 2403545