Rv3716c
- Type
- protein_coding
- Name
- Rv3716c
- Locus Name
-
Rv3716c
- Product
-
Conserved protein
- Functional Category
-
Conserved hypotheticals
- Location
- 4160512..4160913 (- strand)
- Gene Length
- 401 bp
- Nucleotides
-
ATGCAACCCGGAGGCGACATGTCGGCGCTGCTCGCTCAGGCGCAGCAGATGCAGCAAAAGCTCCTGGAGGCCCAGCAACAGCTGGCGAACTCTGAGGTGCACGGTCAAGCCGGTGGGGGCCTGGTCAAGGTCGTCGTCAAAGGCAGCGGGGAGGTGATCGGCGTGACGATCGACCCCAAGGTCGTCGATCCCGACGACATCGAGACCTTGCAGGACCTGATCGTCGGTGCGATGCGCGACGCGTCCCAGCAGGTGACGAAGATGGCGCAGGAACGGCTGGGTGCATTGGCCGGCGCGATGCGCCCGCCGGCACCACCGGCTGCGCCGCCGGGAGCGCCAGGTATGCCGGGTATGCCGGGTATGCCGGGTGCGCCGGGCGCACCACCTGTACCAGGGATCTG
- Drug Resistance
- Mutations
- Function
- Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}.
- Family
-
YbaB/EbfC family
- GO
-
- cytosol GO:0005829 cellular_component
- DNA binding GO:0003677 molecular_function
- plasma membrane GO:0005886 cellular_component
- bacterial nucleoid GO:0043590 cellular_component
- InterPro
5YRX
- Name
- Nucleoid-associated protein Rv3716c
- Family
- YbaB/EbfC family
- Protein Sequence
-
MQPGGDMSALLAQAQQMQQKLLEAQQQLANSEVHGQAGGGLVKVVVKGSGEVIGVTIDPKVVDPDDIETLQDLIVGAMRDASQQVTKMAQERLGALAGAMRPPAPPAAPPGAPGMPGMPGMPGAPGAPPVPGI
- Mass
- 13,357 Da
- Length
- 133 Aa
Summary
Rv3716c doesn't seem to be a targeted by any drug.
Rv3716c doesn't seem to be involved in any pathway.
- 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.
- Identification of acidic, low molecular mass proteins of Mycobacterium tuberculosis strain H37Rv by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry.
- Proteomics. 2001 Apr;1(4):494-507. doi: 10.1002/1615-9861(200104)1:4<494::AID-PROT494>3.0.CO;2-4.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.