Abstract

This study aims to describe the global detection and functional inference of hypothetical protein CA803_03125 from Staphylococcus aureus SO-1977. Computational methods were utilized to study this protein based on sequence similarity and presence of known protein domains. The BLASTp result revealed a significant similarity between the hypothetical protein (CA803_03125) and ADP-ribose hydrolase protein from four S. aureus strains (MW2, MRSA252, COL, and N315). Evolutionary tree diagram revealed a close relationship between the hypothetical protein and proteins of MW2 and COL strains. The physicochemical characterization revealed that all proteins were found to be stable, soluble, hydrophilic and acidic in their nature. The Macro domain was found to exist within all proteins. Moreover, the proteins were of pronounced similarity in terms of primary, secondary and tertiary organization. The protein CA803_03125 (SO-1977) is already known and well characterized as ADP-ribose hydrolase; therefore, we would recommend that its NCBI data has to be updated to be submitted under the name of ADP-ribose hydrolase.

Highlights

  • Methicillin-resistant Staphylococcus aureus (MRSA) is any strain of a bacterium, Staphylococcus aureus that has developed resistance to most of the available antibiotics

  • The protein-BLAST search revealed that the Hypothetical Protein (HP) CA803_03125 was similar to ADP-ribose hydrolase proteins belong to the other S. aureus spp (Table 1)

  • The phylogenetic tree showed that protein sequences with accession numbers: Q8NYB7.1 and Q5HIW9.1 were the closest strains (NCBI Taxonomy IDs: 196620 and 93062 respectively) to HP CA803_03125 (Figure 2)

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Summary

Introduction

Methicillin-resistant Staphylococcus aureus (MRSA) is any strain of a bacterium, Staphylococcus aureus that has developed resistance to most of the available antibiotics. Hundreds of bacterial genomes are available, while their annotation is of interest [3]. Many of these protein functions are still unknown. For this reason, there is an increasing demand for the annotation of the functions of uncharacterized proteins, called “hypothetical proteins” [4]. Several approaches have been developed by scientists with the aid of various computational tools to predict protein function. This has been achieved from information derived from sequence similarity, ISSN 0973-2063 (online) 0973-8894 (print)

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