Gene - combatTB X

Type: protein_coding
Name: Rv2175c
Locus Name: Rv2175c
Product: Conserved regulatory protein
Functional Category: Regulatory proteins
Location: 2437446..2437886 (- strand)
Gene Length: 440 bp
Nucleotides: ATGCCTGGCCGCGCACCAGGCTCTACACTTGCGCGGGTGGGCAGCATTCCCGCTGGCGATGACGTTTTGGACCCTGACGAACCGACGTACGACCTGCCCCGGGTCGCCGAGCTGCTCGGCGTTCCGGTCAGCAAGGTGGCCCAGCAGCTGCGGGAAGGTCATCTGGTGGCCGTGCGGCGCGCTGGTGGCGTGGTGATCCCTCAGGTCTTCTTCACCAACTCCGGTCAGGTGGTCAAGAGCCTGCCGGGGCTGTTGACCATCCTGCACGACGGGGGCTATCGCGACACCGAGATTATGCGCTGGCTGTTTACCCCCGATCCGTCGCTGACCATCACCCGCGACGGCTCGCGTGACGCCGTCAGCAACGCCCGTCCCGTCGATGCATTGCATGCCCACCAGGCTCGCGAGGTGGTGCGCCGGGCCCAGGCTATGGCGTATTG
Drug Resistance: Check for drug resistance association at TBDREAMDB
Mutations: Check for mutants available at TARGET

Function

Binds DNA at low salt concentrations. {ECO:0000269|PubMed:19457863}.

Family

Unknown

GO

InterPro

Summary

Name: DNA-binding protein Rv2175c
Family: Unknown
Protein Sequence: MPGRAPGSTLARVGSIPAGDDVLDPDEPTYDLPRVAELLGVPVSKVAQQLREGHLVAVRRAGGVVIPQVFFTNSGQVVKSLPGLLTILHDGGYRDTEIMRWLFTPDPSLTITRDGSRDAVSNARPVDALHAHQAREVVRRAQAMAY
Mass: 15,743 Da
Length: 146 Aa

Rv2175c doesn't seem to be a targeted by any drug.

Rv2175c doesn't seem to be involved in any pathway.

The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation.: J Biol Chem. 2009 Jul 17;284(29):19290-300. doi: 10.1074/jbc.M109.019653. Epub 2009 May 20.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.: Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c.: Proteomics. 2008 Feb;8(3):521-33. doi: 10.1002/pmic.200700442.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.: Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.