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OmpC-like porin was isolated from the outer membrane (OM) of
Yersinia enterocolitica
cultured at 37°C (the “warm” variant) and its physicochemical and functional properties were studied. The amino acid sequence of OmpC porin was established, and the primary structure and transmembrane topology of this protein were analyzed in comparison with the OmpF porin isolated from
Y. enterocolitica
cultured at 6°C (the “cold” variant). Both porins of
Y. enterocolitica
had a high homology degree (65%) between themselves and with OmpC and OmpF porins from OM of
Escherichia coli
(58 and 76% homology, respectively). The secondary structure of OmpC and OmpF porins from OM of
Y. enterocolitica
consists of 16 β-strands connected by short “periplasmic” and longer “extracellular” loops with disordered structure, according to the topological model developed for porins of
E. coli
. The molecular structures of OmpC and OmpF porins of
Y. enterocolitica
have significant differences in the structure of the “extracellular” loops and in the position of one of three tryptophan residues. Using the bilayer lipid membrane (BLM) technique, pores formed by OmpC porin of
Y. enterocolitica
were shown to differ in electrophysiological characteristics from channels of OmpF protein of this microorganism. The isolated OmpC porin reconstructed into BLM displayed functional plasticity similarly to OmpF protein and nonspecific porins of other enterobacteria. The conductivity level of the channels formed by this protein in the BLM was regulated by value of the applied potential.