Peptidyl-prolyl cis-trans isomerase C (P0A9L5)

Identification
Name:Peptidyl-prolyl cis-trans isomerase C
Synonyms:
  • PPIase C
  • Par10
  • Parvulin
  • Rotamase C
Gene Name:ppiC
Enzyme Class:
Biological Properties
General Function:Posttranslational modification, protein turnover, chaperones
Specific Function:PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
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
isomerase activity
Gene Properties
Blattner:Not Available
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>282 bp
ATGGCAAAAACAGCAGCAGCACTGCATATCCTTGTAAAAGAAGAGAAACTGGCTCTGGAT
CTTCTCGAGCAGATTAAGAACGGGGCCGATTTCGGCAAGCTGGCGAAGAAACACTCCATT
TGCCCATCAGGCAAACGCGGCGGTGATTTAGGTGAATTCCGCCAGGGTCAGATGGTTCCG
GCGTTCGATAAAGTGGTTTTCTCTTGTCCGGTACTGGAGCCGACCGGCCCGCTGCACACC
CAGTTCGGATATCACATCATTAAGGTGCTGTACCGCAACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:93
Protein Molecular Weight:10232
Protein Theoretical pI:10
PDB File:1JNT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Peptidyl-prolyl cis-trans isomerase C
MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVP
AFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN
References
External Links:
ResourceLink
Uniprot ID:P0A9L5
Uniprot Name:PPIC_ECOLI
GenBank Gene ID:M87049
Genebank Protein ID:836657
PDB ID:1JNT
CCDB:PPIC_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
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • 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
  • Koonin, E. V., van der Vies, S. M. (1995). "Conserved sequence motifs in bacterial and bacteriophage chaperonins." Trends Biochem Sci 20:14-15. Pubmed: 7878732
  • Kuhlewein, A., Voll, G., Hernandez Alvarez, B., Kessler, H., Fischer, G., Rahfeld, J. U., Gemmecker, G. (2004). "Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases." Protein Sci 13:2378-2387. Pubmed: 15322281
  • Rahfeld, J. U., Rucknagel, K. P., Schelbert, B., Ludwig, B., Hacker, J., Mann, K., Fischer, G. (1994). "Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin." FEBS Lett 352:180-184. Pubmed: 7925971
  • Rahfeld, J. U., Schierhorn, A., Mann, K., Fischer, G. (1994). "A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli." FEBS Lett 343:65-69. Pubmed: 8163020