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Identification of salt-inducible peptide with putative kinase activity in halophilic bacterium Virgibacillus
Mahmoud-Reza Rafiee1, Ashrafaddin Sokhansanj, Mitra Yoosefi
1Department of Cellular and Molecular Biology, School of Biology, University-college of Sciences, University of Tehran, Tehran 14155-6455, Iran.
Abstract:
Strain XII, a moderately halophilic bacterium, expressed a peptide in response to saline media. This peptide was designated as salt-inducible factor (Sif-A). The purpose of this study is to describe Sif-A, which might be involved in the osmoresistance mechanism of strain XII. The complete sequence of sif-A was determined using PCR. sif-A codes for a polypeptide of 20.518 kDa. The polypeptide has a putative signal peptide of 27 amino acids (2.667 kDa) preceding the mature protein (17.869 kDa). Motif analysis of the deduced amino acid sequence indicated that there is a p-loop NTPase domain on the C-terminal of the peptide, which might correlate with its function. The sequence of the 16S rRNA gene was analyzed phylogenetically to classify strain XII. This organism was found to have the closest association with Virgibacillus halodenitrificans, which was proven by its phenotypic characteristics.
