whiB1
- Type
- protein_coding
- Name
- whiB1
- Locus Name
-
Rv3219
- Product
-
Transcriptional regulatory protein WhiB-like WhiB1. Contains [4FE-4S]2+ cluster.
- Functional Category
-
Regulatory proteins
- Location
- 3595713..3595967 (+ strand)
- Gene Length
- 254 bp
- Nucleotides
-
TGGATTGGCGCCACAAGGCGGTCTGTCGTGACGAGGATCCGGAACTGTTCTTCCCGGTAGGAAACAGTGGTCCGGCACTTGCGCAGATCGCTGACGCGAAACTGGTCTGTAATCGGTGCCCGGTCACCACAGAGTGCCTCAGCTGGGCACTGAATACCGGCCAGGACTCGGGCGTCTGGGGAGGCATGAGCGAAGACGAGCGGCGCGCGCTGAAGCGTCGCAACGCCCGCACGAAAGCCCGTACCGGGGTCTGA
- Drug Resistance
- Mutations
- Function
- Acts as a transcriptional repressor, inhibiting expression in vitro. Probably redox-responsive. The apo- but not holo-form binds to its own promoter as well as that of groEL2. Oxidized apo-form and nitrosylated holo-form also bind DNA. The apo-form has been shown to act as a protein disulfide reductase (PubMed:17157031) (PubMed:19016840), but also not to act as a protein disulfide reductase (PubMed:20929442). {ECO:0000269|PubMed:17157031, ECO:0000269|PubMed:19016840, ECO:0000269|PubMed:20929442, ECO:0000269|PubMed:22464736}.
- Family
-
WhiB family
- GO
-
- cell redox homeostasis GO:0045454 biological_process
- dinitrosyl-iron complex binding GO:0035731 molecular_function
- 4 iron, 4 sulfur cluster binding GO:0051539 molecular_function
- protein-disulfide reductase activity GO:0047134 molecular_function
- cytoplasm GO:0005737 cellular_component
- negative regulation of transcription, DNA-templated GO:0045892 biological_process
- DNA binding GO:0003677 molecular_function
- protein disulfide oxidoreductase activity GO:0015035 molecular_function
- response to nitric oxide GO:0071731 biological_process
- metal ion binding GO:0046872 molecular_function
- InterPro
5OAY
- Name
- Transcriptional regulator WhiB1
- Family
- WhiB family
- Protein Sequence
-
MDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV
- Mass
- 9,319 Da
- Length
- 84 Aa
Summary
Rv3219 doesn't seem to be a targeted by any drug.
Rv3219 doesn't seem to be involved in any pathway.
- Mycobacterium tuberculosis WhiB1 represses transcription of the essential chaperonin GroEL2.
- Tuberculosis (Edinb). 2012 Jul;92(4):328-32. doi: 10.1016/j.tube.2012.03.001. Epub 2012 Mar 29.
- Structure-function relationships of the Mycobacterium tuberculosis transcription factor WhiB1.
- PLoS One. 2012;7(7):e40407. doi: 10.1371/journal.pone.0040407. Epub 2012 Jul 5.
- Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins.
- J Am Chem Soc. 2011 Feb 2;133(4):1112-21. doi: 10.1021/ja109581t. Epub 2010 Dec 23.
- Mycobacterium tuberculosis cAMP receptor protein (Rv3676) differs from the Escherichia coli paradigm in its cAMP binding and DNA binding properties and transcription activation properties.
- J Biol Chem. 2010 Mar 5;285(10):7016-27. doi: 10.1074/jbc.M109.047720. Epub 2009 Dec 22.
- Mycobacterium tuberculosis WhiB1 is an essential DNA-binding protein with a nitric oxide-sensitive iron-sulfur cluster.
- Biochem J. 2010 Dec 15;432(3):417-27. doi: 10.1042/BJ20101440.
- Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv.
- FEBS J. 2009 Jan;276(1):76-93. doi: 10.1111/j.1742-4658.2008.06755.x.
- Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide.
- BMC Biochem. 2009 Jan 5;10:1. doi: 10.1186/1471-2091-10-1.
- Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase.
- Protein Expr Purif. 2007 Apr;52(2):422-32. doi: 10.1016/j.pep.2006.10.015. Epub 2006 Nov 10.
- A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor.
- Mol Microbiol. 2005 Jun;56(5):1274-86. doi: 10.1111/j.1365-2958.2005.04609.x.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.