Molecular characterization of a 17-kDa outer-membrane protein from Klebsiella pneumoniae.

A cosmid-based genomic library of Klebsiella pneumoniae 52145 (O1:K2) was introduced into Escherichia coli, and clones were screened for the bacteriocin 28b resistance phenotype. One clone was found which conferred partial resistance to bacteriocin 28b. By using Tn5tac1 insertions, it was shown that this phenotype was due to the expression, in E. coli, of an outer-membrane protein (OMP) with an apparent molecular mass of 17 kDa (OmpK17). The DNA region defined by insertion mutagenesis was sequenced and found to contain an ORF of 510 bp. The deduced amino acid sequence has 170 residues with a theoretical molecular mass of 18.4 kDa. The protein contains an N-terminal signal sequence of 24 amino acid residues. When compared with other enterobacterial OMPs, OmpK17 most closely resembles members of a family of small OMPs of Enterobacteriaceae the known functions of which appear to be related to virulence. Immunoblotting experiments showed that OmpK17 is also present in various K. pneumoniae strains belonging to different O and K serotypes.