FKBP-type peptidyl-prolyl cis-trans isomerase slyD (P0A9K9)

Identification
Name:FKBP-type peptidyl-prolyl cis-trans isomerase slyD
Synonyms:
  • PPIase
  • Histidine-rich protein
  • Metallochaperone slyD
  • Rotamase
  • Sensitivity to lysis protein D
  • WHP
Gene Name:slyD
Enzyme Class:
Biological Properties
General Function:Posttranslational modification, protein turnover, chaperones
Specific Function:Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity
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:
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:
>591 bp
ATGAAAGTAGCAAAAGACCTGGTGGTCAGCCTGGCCTATCAGGTACGTACAGAAGACGGT
GTGTTGGTTGATGAGTCTCCGGTGAGTGCGCCGCTGGACTACCTGCATGGTCACGGTTCC
CTGATCTCTGGCCTGGAAACGGCGCTGGAAGGTCATGAAGTTGGCGACAAATTTGATGTC
GCTGTTGGCGCGAACGACGCTTACGGTCAGTACGACGAAAACCTGGTGCAACGTGTTCCT
AAAGACGTATTTATGGGCGTTGATGAACTGCAGGTAGGTATGCGTTTCCTGGCTGAAACC
GACCAGGGTCCGGTACCGGTTGAAATCACTGCGGTTGAAGACGATCACGTCGTGGTTGAT
GGTAACCACATGCTGGCCGGTCAGAACCTGAAATTCAACGTTGAAGTTGTGGCGATTCGC
GAAGCGACTGAAGAAGAACTGGCTCATGGTCACGTTCACGGCGCGCACGATCACCACCAC
GATCACGACCACGACGGTTGCTGCGGCGGTCATGGCCACGATCACGGTCATGAACACGGT
GGCGAAGGCTGCTGTGGCGGTAAAGGCAACGGCGGTTGCGGTTGCCACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:196
Protein Molecular Weight:20853
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>FKBP-type peptidyl-prolyl cis-trans isomerase slyD
MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDV
AVGANDAYGQYDENLVQRVPKDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVD
GNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHHDHDHDGCCGGHGHDHGHEHG
GEGCCGGKGNGGCGCH
References
External Links:
ResourceLink
Uniprot ID:P0A9K9
Uniprot Name:SLYD_ECOLI
GenBank Gene ID:L28082
Genebank Protein ID:862299
CCDB:SLYD_ECOLI
General Reference:
  • Bernhardt, T. G., Roof, W. D., Young, R. (2002). "The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174." Mol Microbiol 45:99-108. Pubmed: 12100551
  • 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
  • Graubner, W., Schierhorn, A., Bruser, T. (2007). "DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone." J Biol Chem 282:7116-7124. Pubmed: 17215254
  • 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
  • Horne, S. M., Young, K. D. (1995). "Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins." Arch Microbiol 163:357-365. Pubmed: 7540828
  • Hottenrott, S., Schumann, T., Pluckthun, A., Fischer, G., Rahfeld, J. U. (1997). "The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase." J Biol Chem 272:15697-15701. Pubmed: 9188461
  • Kaluarachchi, H., Sutherland, D. E., Young, A., Pickering, I. J., Stillman, M. J., Zamble, D. B. (2009). "The Ni(II)-binding properties of the metallochaperone SlyD." J Am Chem Soc 131:18489-18500. Pubmed: 19947632
  • Martino, L., He, Y., Hands-Taylor, K. L., Valentine, E. R., Kelly, G., Giancola, C., Conte, M. R. (2009). "The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity." FEBS J 276:4529-4544. Pubmed: 19645725
  • Roof, W. D., Horne, S. M., Young, K. D., Young, R. (1994). "slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases." J Biol Chem 269:2902-2910. Pubmed: 8300625
  • Scholz, C., Eckert, B., Hagn, F., Schaarschmidt, P., Balbach, J., Schmid, F. X. (2006). "SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities." Biochemistry 45:20-33. Pubmed: 16388577
  • Weininger, U., Haupt, C., Schweimer, K., Graubner, W., Kovermann, M., Bruser, T., Scholz, C., Schaarschmidt, P., Zoldak, G., Schmid, F. X., Balbach, J. (2009). "NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function." J Mol Biol 387:295-305. Pubmed: 19356587
  • Wulfing, C., Lombardero, J., Pluckthun, A. (1994). "An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif." J Biol Chem 269:2895-2901. Pubmed: 8300624
  • Zhang, J. W., Butland, G., Greenblatt, J. F., Emili, A., Zamble, D. B. (2005). "A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway." J Biol Chem 280:4360-4366. Pubmed: 15569666
  • Zhang, J. W., Leach, M. R., Zamble, D. B. (2007). "The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase." J Bacteriol 189:7942-7944. Pubmed: 17720786