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
- 分子量
- 20431.205
- Theoretical pI
- 9.39
- GO Classification
-
Functionspeptidyl-prolyl cis-trans isomerase activityProcessesprotein folding/protein peptidyl-prolyl isomerizationComponentsouter 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
-
- Pro_isomerase (PF00160)
- 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
-
Resource Link UniProtKB ID P0AFL3 UniProtKB Entry Name PPIA_ECOLI GenBank Protein ID 145287 GenBank Gene ID M55429 - General References
-
- 加藤Hayano T,高桥N, S, Maki N,铃木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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]