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Volume 271, Number 36, Issue of September 6, 1996 pp. 22130-22138
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Isolation and Amino Acid Sequence of a New 22-kDa FKBP-like Peptidyl-prolyl cis/trans-Isomerase of Escherichia coli
SIMILARITY TO Mip-LIKE PROTEINS OF PATHOGENIC BACTERIA

(Received for publication, March 14, 1996, and in revised form, June 15, 1996)

Jens-U. Rahfeld , K. Peter Rücknagel , Gerlind Stoller , Shelley M. Horne , Angelika Schierhorn ^¶ , Kevin D. Young and Gunter Fischer

From the  Max-Planck-Gesellschaft, Arbeitsgruppe ``Enzymologie der Peptidbindung,'' Kurt-Mothes-Strae 3, D-06120 Halle/Saale, Germany, the ^¶ Martin-Luther-Universität Halle Wittenberg, Lehrstuhl für Molekulare Biochemie, Kurt-Mothes-Strae 3, D-06120 Halle/Saale, Germany, and the  Department of Microbiology & Immunology, School of Medicine, University of North Dakota, Grand Forks, North Dakota 58202-9037

We identified a periplasmic peptidyl-prolyl cis/trans-isomerase (PPIase) of the (FK506-binding protein (FKBP) type in Escherichia coli (FK506 represents a natural peptidomacrolide containing an acylated pipecolic acid residue). After purification to homogeneity, its complete amino acid sequence was determined by a combination of Edman degradation and electrospray mass spectrometry of the authentic protein and peptides generated by proteolysis. The molecular mass calculated from the amino acid sequence of the protein was 22,085.53 Da, which corresponded perfectly with the value of 22,084 ± 1.47 Da as determined by mass spectrometry. The corresponding gene was cloned and analyzed, and Southern blot experiments revealed the existence of similar genes in various Gram-negative bacteria. The amino acid sequence of the novel FKBP22 shows similarity to Mip (macrophage infectivity potentiator)-like proteins produced by a number of pathogenic bacteria. However, FKBP22 is inhibited more strongly by FK506 than are other Mip-homologues, as indicated by the K_i value of 25 nM. The subsite specificity regarding the P₁ position of the substrate resembles that for Mip-FKBP25 from Legionella pneumophila. The mature FKBP22 enzyme of 205 amino acids exists as a dimer in solution.

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