Abstract
Background and Aims:
Helicobacter pylori (H. pylori) is a Gram-negative pathogenic bacterium that causes gastritis in humans. The exact molecular mechanism of most of the non-annotated hypothetical proteins involved in the virulence of H. pylori is yet to be identified. This paper aims to characterize the structure and function of the non-annotated hypothetical protein (HP) HPAG1_0137 from the H. pylori bacterium (strain HPAG1) in silico.
Methods:
We predicted several properties of HPAG1_0137, such as its physicochemical characteristics, secondary and tertiary structures, and functional annotation using different computational tools, followed by structural validation and quality assessment. We also performed virulence, protein crystallization, and active site predictions.
Results:
The study found that HPAG1_0137 has 242 amino acids and an acidic pI and is thermally stable, water-soluble, and distributed in the cytoplasm. Structurally, alpha-helices and random coils are this protein’s most prominent structural components. We found structural models to be highly native and of decent quality.
Conclusions:
This study will facilitate a better understanding of the HPAG1_0137 protein molecular mechanism of action. In addition, it will provide the basis for additional proteomic, genomic data, and structural and pharmacological research for functional and therapeutic potential identification.

Key words: Helicobacter pylori, hypothetical protein, HPAG1_0137 protein, homology modeling, in silico characterization