Peptidyl-prolyl cis-trans isomerase A

Details

Name
Peptidyl-prolyl cis-trans isomerase A
Synonyms
  • 5.2.1.8
  • Cyclophilin A
  • PPIase A
  • rot
  • rotA
  • Rotamase A
Gene Name
ppiA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020745|Peptidyl-prolyl cis-trans isomerase A
MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYV
NSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADK
DSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKP
VVILSAKVLP
Number of residues
190
Molecular Weight
20431.205
Theoretical pI
9.39
GO Classification
Functions
peptidyl-prolyl cis-trans isomerase activity
Processes
protein folding / protein peptidyl-prolyl isomerization
Components
outer membrane-bounded periplasmic space
General Function
Peptidyl-prolyl cis-trans isomerase activity
Specific Function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0020746|Peptidyl-prolyl cis-trans isomerase A (ppiA)
ATGTTCAAATCGACCCTGGCGGCGATGGCTGCTGTTTTCGCTCTTTCTGCTCTTTCTCCC
GCAGCAATGGCAGCGAAAGGGGACCCGCACGTATTGTTGACAACCTCAGCTGGTAACATC
GAACTGGAGCTGGATAAACAAAAAGCGCCAGTGTCTGTGCAAAACTTTGTCGATTATGTG
AACAGCGGTTTTTATAACAACACTACCTTTCACCGCGTCATTCCTGGCTTTATGATTCAG
GGCGGCGGTTTCACCGAGCAGATGCAGCAGAAAAAACCAAACCCGCCAATCAAAAATGAA
GCCGATAACGGCCTGCGCAACACGCGTGGCACCATCGCGATGGCACGTACCGCTGACAAA
GACAGCGCCACCAGCCAGTTCTTTATCAACGTTGCCGATAACGCCTTCCTTGACCATGGT
CAGCGTGATTTCGGTTACGCGGTATTTGGTAAAGTGGTGAAAGGCATGGACGTTGCCGAT
AAGATTTCCCAGGTGCCGACTCATGACGTTGGTCCGTACCAGAATGTGCCGTCAAAACCG
GTAGTTATCCTTTCCGCTAAAGTCCTGCCGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AFL3
UniProtKB Entry NamePPIA_ECOLI
GenBank Protein ID145287
GenBank Gene IDM55429
General References
  1. 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 Mar 26;30(12):3041-8. [Article]
  2. 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 Aug;171(8):4525-9. [Article]
  3. 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]
  4. 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]
  5. Tran PV, Bannor TA, Doktor SZ, Nichols BP: Chromosomal organization and expression of Escherichia coli pabA. J Bacteriol. 1990 Jan;172(1):397-410. [Article]
  6. Liu J, Walsh CT: 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 Jun;87(11):4028-32. [Article]
  7. Compton LA, Davis JM, Macdonald JR, Bachinger HP: Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases. Eur J Biochem. 1992 Jun 15;206(3):927-34. [Article]
  8. Liu J, Chen CM, Walsh CT: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991 Mar 5;30(9):2306-10. [Article]
  9. Clubb RT, Ferguson SB, Walsh CT, Wagner G: Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry. 1994 Mar 15;33(10):2761-72. [Article]
  10. Fejzo J, Etzkorn FA, Clubb RT, Shi Y, Walsh CT, Wagner G: The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin. Biochemistry. 1994 May 17;33(19):5711-20. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08168Coumarin 120experimentalunknownDetails