Gene - combatTB X

pknE

Type: protein_coding
Name: pknE
Locus Name: Rv1743
Product: Probable transmembrane serine/threonine-protein kinase E PknE (protein kinase E) (STPK E)
Functional Category: Regulatory proteins
Location: 1969004..1970704 (+ strand)
Gene Length: 1700 bp
Nucleotides: TGGATGGCACCGCGGAATCGCGGGAGGGTACGCAGTTCGGGCCGTATCGGTTGCGGCGGTTGGTGGGTCGCGGCGGCATGGGCGACGTCTATGAGGCCGAAGACACGGTGCGCGAGCGGATCGTGGCACTAAAGCTGATGTCGGAGACGCTCTCCAGCGATCCGGTCTTCCGCACGCGTATGCAGCGCGAGGCCCGCACCGCGGGGCGCCTGCAGGAACCGCACGTCGTGCCGATTCACGACTTCGGTGAGATCGACGGGCAGCTCTACGTGGACATGCGCCTGATCAACGGCGTGGATCTGGCCGCGATGCTGAGACGCCAGGGGCCGCTGGCCCCACCGCGAGCGGTCGCGATCGTGCGCCAGATCGGCTCGGCGCTCGACGCCGCGCACGCTGCCGGGGCAACGCATCGCGACGTCAAACCGGAGAACATTCTGGTTAGCGCGGATGACTTCGCCTATCTTGTCGATTTCGGGATCGCCAGCGCCACCACCGACGAAAAGCTGACCCAGCTCGGCAACACGGTGGGCACCCTCTACTACATGGCGCCAGAGCGGTTCAGCGAGTCGCACGCAACTTACCGCGCCGACATTTATGCGTTGACCTGCGTGTTGTATGAGTGCTTGACCGGATCACCGCCGTATCAGGGAGACCAGCTCAGCGTGATGGGCGCGCACATCAACCAGGCGATCCCGCGGCCCAGCACGGTACGGCCGGGTATTCCGGTCGCCTTCGATGCGGTGATCGCCCGTGGCATGGCCAAAAATCCGGAGGACCGCTATGTCACCTGCGGTGATCTGTCAGCGGCGGCGCACGCAGCCCTGGCCACCGCGGATCAGGATCGTGCCACCGACATCTTGCGGCGCAGCCAGGTGGCCAAGCTGCCGGTGCCATCGACTCACCCGGTGTCACCGGGTACCCGGTGGCCGCAGCCGACGCCATGGGCTGGCGGGGCGCCGCCATGGGGGCCACCGTCGTCTCCGCTGCCCCGGTCAGCCCGCCAGCCCTGGTTGTGGGTTGGTGTTGCCGTCGCCGTCGTGGTGGCGCTGGCGGGCGGCCTGGGTATCGCGCTTGCCCATCCGTGGCGGTCATCTGGACCCCGCACGTCGGCACCGCCGCCACCGCCGCCCGCAGATGCGGTCGAGCTCCGCGTTCTCAACGACGGTGTCTTTGTGGGTAGCTCGGTGGCGCCGACAACGATCGACATTTTCAACGAACCCATCTGTCCACCCTGCGGCAGTTTCATCAGGTCGTATGCGAGCGATATCGATACCGCGGTGGCCGACAAGCAGCTGGCGGTGCGCTACCACCTGCTCAACTTCCTCGACGACCAGTCGCACAGCAAGAACTATTCGACGCGAGCGGTGGCCGCCTCGTACTGTGTAGCGGGGCAAAACGACCCGAAACTCTACGCCAGCTTCTACTCCGCCCTATTCGGCAGCGACTTTCAGCCGCAAGAGAACGCCGCATCGGATCGCACCGATGCCGAACTGGCACATCTTGCTCAAACAGTCGGCGCCGAGCCCACGGCGATCAGCTGTATCAAGTCAGGAGCTGATCTGGGCACCGCCCAAACGAAGGCCACAAACGCCAGCGAGACGCTGGCCGGCTTCAATGCCAGCGGTACGCCGTTCGTGTGGGACGGCAGCATGGTCGTGAACTATCAGGATCCGAGCTGGCTCGCGAGGCTGATCGGGTAG
Drug Resistance: Check for drug resistance association at TBDREAMDB
Mutations: Check for mutants available at TARGET

Function

Important for survival of the bacterium in the host during infection. Promotes the survival of infected macrophages by activating multiple signaling responses and suppressing apoptosis of macrophages during nitrate stress. May contribute to the adaptation of M.tuberculosis during stress conditions by maintaining the cellular integrity. Can phosphorylate the FHA domain of Rv1747. {ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:17892498, ECO:0000269|PubMed:21945589, ECO:0000269|PubMed:23108860}.

Family

Protein kinase superfamily, Ser/Thr protein kinase family

GO

integral component of membrane GO:0016021 cellular_component
protein kinase activity GO:0004672 molecular_function
protein serine/threonine kinase activity GO:0004674 molecular_function
protein phosphorylation GO:0006468 biological_process
response to nitrosative stress GO:0051409 biological_process
plasma membrane GO:0005886 cellular_component
ATP binding GO:0005524 molecular_function
extracellular region GO:0005576 cellular_component
negative regulation of fatty acid biosynthetic process GO:0045717 biological_process
negative regulation of catalytic activity GO:0043086 biological_process
positive regulation of catalytic activity GO:0043085 biological_process
pathogenesis GO:0009405 biological_process
protein autophosphorylation GO:0046777 biological_process

InterPro

UniProt: P9WI77
GenBank: Rv1743
EnsemblBacteria: Rv1743
Mycobrowser: Rv1743

Summary

Name: Serine/threonine-protein kinase PknE (EC 2.7.11.1)
Family: Protein kinase superfamily, Ser/Thr protein kinase family
Protein Sequence: MDGTAESREGTQFGPYRLRRLVGRGGMGDVYEAEDTVRERIVALKLMSETLSSDPVFRTRMQREARTAGRLQEPHVVPIHDFGEIDGQLYVDMRLINGVDLAAMLRRQGPLAPPRAVAIVRQIGSALDAAHAAGATHRDVKPENILVSADDFAYLVDFGIASATTDEKLTQLGNTVGTLYYMAPERFSESHATYRADIYALTCVLYECLTGSPPYQGDQLSVMGAHINQAIPRPSTVRPGIPVAFDAVIARGMAKNPEDRYVTCGDLSAAAHAALATADQDRATDILRRSQVAKLPVPSTHPVSPGTRWPQPTPWAGGAPPWGPPSSPLPRSARQPWLWVGVAVAVVVALAGGLGIALAHPWRSSGPRTSAPPPPPPADAVELRVLNDGVFVGSSVAPTTIDIFNEPICPPCGSFIRSYASDIDTAVADKQLAVRYHLLNFLDDQSHSKNYSTRAVAASYCVAGQNDPKLYASFYSALFGSDFQPQENAASDRTDAELAHLAQTVGAEPTAISCIKSGADLGTAQTKATNASETLAGFNASGTPFVWDGSMVVNYQDPSWLARLIG
Mass: 60,512 Da
Length: 566 Aa

Rv1743 doesn't seem to be a targeted by any drug.

Rv1743 doesn't seem to be involved in any pathway.

A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis.: J Mol Biol. 2006 Jul 7;360(2):409-20. doi: 10.1016/j.jmb.2006.05.015. Epub 2006 May 19.
pknE, a serine/threonine kinase of Mycobacterium tuberculosis modulates multiple apoptotic paradigms.: Infect Genet Evol. 2012 Jun;12(4):737-47. doi: 10.1016/j.meegid.2011.09.008. Epub 2011 Sep 16.
PknE, a serine/threonine protein kinase from Mycobacterium tuberculosis has a role in adaptive responses.: Arch Microbiol. 2013 Jan;195(1):75-80. doi: 10.1007/s00203-012-0848-4. Epub 2012 Oct 30.
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.
Protein kinase E of Mycobacterium tuberculosis has a role in the nitric oxide stress response and apoptosis in a human macrophage model of infection.: Cell Microbiol. 2008 Feb;10(2):365-74. doi: 10.1111/j.1462-5822.2007.01049.x. Epub 2007 Sep 24.
Characterization of the phosphorylation sites of Mycobacterium tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH by mass spectrometry.: Proteomics. 2006 Jul;6(13):3754-66. doi: 10.1002/pmic.200500900.
Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains.: Protein Sci. 2005 Jul;14(7):1918-21. doi: 10.1110/ps.051413405.
Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases.: Biochem Biophys Res Commun. 2005 Aug 5;333(3):858-67. doi: 10.1016/j.bbrc.2005.05.173.
Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis.: Biochem Biophys Res Commun. 2003 Sep 5;308(4):820-5. doi: 10.1016/s0006-291x(03)01476-1.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.: Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.