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MetaCyc Enzyme: peptidyl-prolyl cis-trans isomerase C (rotamase C)

Gene: ppiC Accession Numbers: EG12352 (MetaCyc), b3775, ECK3767

Synonyms: parvA, Par10, parvulin

Species: Escherichia coli K-12 substr. MG1655

Summary:
ppiC encodes a peptidyl-prolyl cis-trans isomerase, parvulin, which defines a new family of PPIases [Rahfeld94, Rahfeld94a]. Unlike other peptidyl-prolyl cis-trans isomerases, the enzymatic activity of parvulin is not inhibited by FK506 or cyclosporin A [Rahfeld94]. The natural compound juglone specifically and irreversibly inactivates parvulin by covalent modification [Hennig98]. The stereospecificity of the enzyme has been studied [Schiene98], and a solution structure of PpiC has been determined [Kuhlewein04].

AhpC has been identified as a specific interaction partner of PpiC [Malesevic10].

A ppiC mutant is more sensitive to oxidative stress than wild type [Malesevic10].

Resequencing of multiple isolates of the MG1655 strain has identified several genetic variations compared to the reference sequence, including a single-nucleotide polymorphism in the yifO-ppiC intergenic region [Freddolino12]. This EcoliWiki page summarizes these sequence differences.

Reviews: [Rudd95, Koonin95]

Locations: cytosol

Map Position: [3,957,555 <- 3,957,836]

Molecular Weight of Polypeptide: 10.232 kD (from nucleotide sequence), 10.1 kD (experimental) [Rahfeld94 ]

Unification Links: ASAP:ABE-0012334 , CGSC:35829 , DIP:DIP-48081N , EchoBASE:EB2256 , EcoGene:EG12352 , EcoliWiki:b3775 , Mint:MINT-1225694 , OU-Microarray:b3775 , PortEco:ppiC , Pride:P0A9L5 , Protein Model Portal:P0A9L5 , RefSeq:NP_418223 , RegulonDB:EG12352 , SMR:P0A9L5 , String:511145.b3775 , UniProt:P0A9L5

Relationship Links: InterPro:IN-FAMILY:IPR000297 , InterPro:IN-FAMILY:IPR023058 , PDB:Structure:1JNS , PDB:Structure:1JNT , Pfam:IN-FAMILY:PF00639 , Prosite:IN-FAMILY:PS01096 , Prosite:IN-FAMILY:PS50198

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000413 - protein peptidyl-prolyl isomerization Inferred by computational analysis Inferred from experiment [Rahfeld94, UniProtGOA11a, GOA01]
GO:0006457 - protein folding Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003755 - peptidyl-prolyl cis-trans isomerase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Rahfeld94]
GO:0005515 - protein binding Inferred from experiment [Malesevic10]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: information transfer protein related chaperoning, repair (refolding)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: peptidyl-prolyl cis-trans isomerase

Synonyms: peptidylprolyl isomerase, PPIase, rotamase

EC Number: 5.2.1.8

peptidylproline (ω = 180) <=> peptidylproline (ω = 0)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
PpiC prefers amino acid residues with hydrophobic side chains such as leucine and phenylalanine in the P1 position of the peptide substrate [Rahfeld94] and shows only a slight preference for nonpolar residues following proline [Schmidpeter11].

Inhibitors (Irreversible): 5-hydroxy-1,4-naphthoquinone [Hennig98]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Rahfeld94, Rahfeld94a, UniProt11a]
UniProt: Removed.
Conserved-Region 2 -> 91
[UniProt09]
UniProt: PpiC;
Chain 2 -> 93
[UniProt09]
UniProt: Peptidyl-prolyl cis-trans isomerase C;

History:
10/20/97 Gene b3775 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12352; confirmed by SwissProt match.


References

Freddolino12: Freddolino PL, Amini S, Tavazoie S (2012). "Newly identified genetic variations in common Escherichia coli MG1655 stock cultures." J Bacteriol 194(2);303-6. PMID: 22081388

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Golbik05: Golbik R, Yu C, Weyher-Stingl E, Huber R, Moroder L, Budisa N, Schiene-Fischer C (2005). "Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates." Biochemistry 44(49);16026-34. PMID: 16331962

Hennig98: Hennig L, Christner C, Kipping M, Schelbert B, Rucknagel KP, Grabley S, Kullertz G, Fischer G (1998). "Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone." Biochemistry 37(17);5953-60. PMID: 9558330

Koonin95: Koonin EV, van der Vies SM (1995). "Conserved sequence motifs in bacterial and bacteriophage chaperonins." Trends Biochem Sci 20(1);14-5. PMID: 7878732

Kuhlewein04: Kuhlewein A, Voll G, Hernandez Alvarez B, Kessler H, Fischer G, Rahfeld JU, 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(9);2378-87. PMID: 15322281

Malesevic10: Malesevic M, Poehlmann A, Hernandez Alvarez B, Diessner A, Trager M, Rahfeld JU, Jahreis G, Liebscher S, Bordusa F, Fischer G, Lucke C (2010). "The protein-free IANUS peptide array uncovers interaction sites between Escherichia coli parvulin 10 and alkyl hydroperoxide reductase." Biochemistry 49(39);8626-35. PMID: 20806779

Rahfeld94: Rahfeld JU, Schierhorn A, Mann K, Fischer G (1994). "A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli." FEBS Lett 343(1);65-9. PMID: 8163020

Rahfeld94a: Rahfeld JU, Rucknagel KP, 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(2);180-4. PMID: 7925971

Rudd95: Rudd KE, Sofia HJ, Koonin EV, Plunkett G, Lazar S, Rouviere PE (1995). "A new family of peptidyl-prolyl isomerases." Trends Biochem Sci 20(1);12-4. PMID: 7878731

Schiene98: Schiene C, Reimer U, Schutkowski M, Fischer G (1998). "Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases." FEBS Lett 432(3);202-6. PMID: 9720925

Schmidpeter11: Schmidpeter PA, Jahreis G, Geitner AJ, Schmid FX (2011). "Prolyl isomerases show low sequence specificity toward the residue following the proline." Biochemistry 50(21);4796-803. PMID: 21510665

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc12.