Bioinformatic analysis of metal transportomes from Mycobacteria Sp.

<p>Mycobacterium is immovable induce aerobic, acid-fast gram-positive bacilli with high genomic content (59-66%). In the operon structure frequently establish for the genes of three molecular components: the ABC-binding protein, the membrane protein, and the substrate-binding protein, the rate...

Full description

Saved in:
Bibliographic Details
Main Authors: Shanti Kumari Lunavat (Author), Jai Satya Gowri Gogada (Author), Surya Satyanarayana Singh (Author), Raghu Gogada (Author)
Format: Book
Published: Open Journal of Bioinformatics and Biostatistics - Peertechz Publications, 2021-09-07.
Subjects:
Online Access:Connect to this object online.
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:<p>Mycobacterium is immovable induce aerobic, acid-fast gram-positive bacilli with high genomic content (59-66%). In the operon structure frequently establish for the genes of three molecular components: the ABC-binding protein, the membrane protein, and the substrate-binding protein, the rates of multidrug resistant and metal ions. The main objective of this study was to analyze the metal ions from five Mycobacterium species and to identify the metal transporters with "Genomic Island" associated features, in-silico analysis allowed identification of metal and drug transporters, phylogenetic analysis, genomic island path analysis, prediction of interacting metal ions, 3D structure, domain analysis and for the NiCoT metal transporter from Mycobacterium tuberculosis. These data are the first results of a big frame project that aims to accelerate the prioritizing of gene candidates that control element accumulation by taking advantage of high-throughput. The present in-silico study reveals the complete suite of NiCoT Metal Transporter in Mycobacterium tuberculosis H37Rv, which is involved in urease enzyme activity and biological function. The STRING analysis defines that the functional partners involved in transport of metal ions. While high expression yields of membrane proteins remain significant bottleneck for many proteins.</p>
DOI:10.17352/ojbb.000011