Hitesh Thakare¹*, Rakesh Thakare², Yajuved N Selokar¹ and Dayanand Gogle¹

¹Department of Molecular Biology and Genetic Engineering, Rashtrasant Tukadoji Maharaj Nagpur University, Nagpur, Maharashtra, India
²Department of Microbiology, Yashwantrao Chavhan College Lakhandur, Bhandara, Maharashtra, India

*Corresponding Author: Hitesh Thakare, Department of Molecular Biology and Genetic Engineering, Rashtrasant Tukadoji Maharaj Nagpur University, Nagpur, Maharashtra, India.

Received: November 25, 2025; Published: December 27, 2025

Abstract

Globally, nosocomial infections are primarily caused by the gram-negative bacillus bacteria Elizabethkingia meningoseptica. The elucidation of Elizabethkingia meningoseptica’s genome sequence has improved our understanding of the pathogenicity and lifestyle of this clinically significant organism. The study sought to provide an overview of a hypothetical protein that may be crucial to Elizabethkingia meningoseptica pathogenicity and virulence, including information on its expected structure, likely biological roles, and significance in this particular environment. Elizabethkingia meningoseptica’s putative protein, which contains 179 amino acid residues, was selected for study and modelling using a variety of bioinformatics tools and databases in this work. Investigations of the primary and secondary structures illustrate that AQX04507.1 is a stable hydrophilic protein containing a sizable number of α-helices. According to subcellular localization predictions made by PSORTb, SOSUI server, and CELLO, the protein is cytoplasmic. Functional genomics studies using NCBI-CDD, Pfam, and InterProScan suggested that the putative protein might contain the putative TPR-repeat lipoprotein domain of the PEP-CTERM system. Using the template structure of Parabacteroides merdae ATCC 43184, which is the crystal structure of a tetratricopeptide repeat (PARMER_03812) (PDB ID: 4R7S), an X-ray diffraction model with 99.81% sequence identity with the hypothetical protein, the HHpred server was used to create its 3D structure in the homology modeling method. Following energy minimization, the created protein model was found to be dependable and of acceptable quality based on a number of quality assessments and validation variables. The hypothetical protein AQX04507.1 of Elizabethkingia meningoseptica has been thoroughly characterized and functionally annotated in the current study. Additional experimental validation is necessary to ascertain the true function of AQX04507.1 and to validate its potential as a therapeutic target.

Keywords: Elizabethkingia meningoseptica; Hypothetical Protein; Homology Modelling; Tetratricopeptide Repeat (TPR) Lipoprotein; UCSF Chimera

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Citation

Citation: Hitesh Thakare., et al. “Unravelling the Functional Potential of a Hypothetical Protein from Elizabethkingia meningoseptica: An In silico Analysis".Acta Scientific Microbiology 9.1 (2026): 02-24.

Copyright

Copyright: © 2026 Hitesh Thakare., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.