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Search term: pknG

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namepknG
Rv numberRv0410c
TypeCDS
FunctionInvolved in signal transduction (via phosphorylation). Thought to regulate amino-acid uptake and stationary-phase metabolism. Phosphorylates the peptide substrate myelin basic protein (MBP) at serine residues [catalytic activity: ATP + a protein = ADP + a phosphoprotein].
ProductSerine/threonine-protein kinase PknG (protein kinase G) (STPK G)
CommentsRv0410c, (MTCY22G10.06c), len: 750 aa. PknG, serine/threonine-protein kinase (see citations below), equivalent to PKNG_MYCLE|P57993|13092623|CAC29812.1|AL583918 probable serine/threonine-protein kinase from Mycobacterium leprae (767 aa). Also similar to others e.g. AB76890.1|AL159139 putative serine/threonine protein kinase from Streptomyces coelicolor (774 aa); etc. Contains PS00108 Serine/Threonine protein kinases active-site signature. Contains Hank's kinase subdomain. Belongs to the Ser/Thr family of protein kinases. Structure of PknG with inhibitor AX20017 reveals that the inhibitor-binding pocket is shaped by a unique set of amino acid side chains not found in any human kinase (See Scherr et al., 2007).
Molecular mass (Da)81577.4
Isoelectric point5.5467
Gene length (bp)2253
Protein length750
Location (kb)495.062


Functional categoryregulatory proteins


ProteomicsIdentified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). M. bovis BCG pknG|Rv0410c mutant is transferred to lysosomes during macrophage infection while wild-type is not (See Walburger et al., 2004). M. tuberculosis H37Rv pknG|Rv0410c mutant grows slower than wild-type, in vitro; accumulates glutamate and glutamine; is not attenuated in CD-1 mice (See Cowley et al., 2004). M. tuberculosis H37Rv pknG|Rv0410c mutant shows increased sensitivity to erythromycin and sulfachloropyridazine (See Wolff et al., 2009).
see TB knockouts/mutants availability


Coordinates
TypeStartEndOrientation
CDS495062497314-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv0410c|pknG
MAKASETERSGPGTQPADAQTATSATVRPLSTQAVFRPDFGDEDNFPHPTLGPDTEPQDR
MATTSRVRPPVRRLGGGLVEIPRAPDIDPLEALMTNPVVPESKRFCWNCGRPVGRSDSET
KGASEGWCPYCGSPYSFLPQLNPGDIVAGQYEVKGCIAHGGLGWIYLALDRNVNGRPVVL
KGLVHSGDAEAQAMAMAERQFLAEVVHPSIVQIFNFVEHTDRHGDPVGYIVMEYVGGQSL
KRSKGQKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQLKLIDLGAVSRI
NSFGYLYGTPGFQAPEIVRTGPTVATDIYTVGRTLAALTLDLPTRNGRYVDGLPEDDPVL
KTYDSYGRLLRRAIDPDPRQRFTTAEEMSAQLTGVLREVVAQDTGVPRPGLSTIFSPSRS
TFGVDLLVAHTDVYLDGQVHAEKLTANEIVTALSVPLVDPTDVAASVLQATVLSQPVQTL
DSLRAARHGALDADGVDFSESVELPLMEVRALLDLGDVAKATRKLDDLAERVGWRWRLVW
YRAVAELLTGDYDSATKHFTEVLDTFPGELAPKLALAATAELAGNTDEHKFYQTVWSTND
GVISAAFGLARARSAEGDRVGAVRTLDEVPPTSRHFTTARLTSAVTLLSGRSTSEVTEEQ
IRDAARRVEALPPTEPRVLQIRALVLGGALDWLKDNKASTNHILGFPFTSHGLRLGVEAS
LRSLARVAPTQRHRYTLVDMANKVRPTSTF
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP65728
Protein Data Bank2PZI


Orthologs/Cross-references
CDC1551MT0423
Enzyme Classification2.7.11.1
Gene Ontologyprotein serine/threonine kinase activity
ATP binding
protein amino acid phosphorylation
M. bovisMb0418c
M. lepraeML0304
M. marinumMMAR_0713
M. smegmatisMSMEG_0786
UniProtP65728
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv0410c


Expression Data
TBDBRv0410c


Bibliography
Av-Gay Y, Everett M,
The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
Trends Microbiol (2000) 8(5):238-44
Cited for: Review
Koul A, Choidas A, Tyagi AK, Drlica K, Singh Y, Ullrich A,
Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization
Microbiology (2001) 147(Pt 8):2307-14
Cited for: Product/Biochemistry
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Walburger A, Koul A, Ferrari G, Nguyen L, Prescianotto-Baschong C, Huygen K, Klebl B, Thompson C, Bacher G, Pieters J,
Protein kinase G from pathogenic mycobacteria promotes survival within macrophages.
Science (2004) 304(5678):1800-4
Cited for: Mutant
Cowley S, Ko M, Pick N, Chow R, Downing KJ, Gordhan BG, Betts JC, Mizrahi V, Smith DA, Stokes RW, Av-Gay Y,
The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo.
Mol Microbiol (2004) 52(6):1691-702
Cited for: Mutant
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Scherr N, Honnappa S, Kunz G, Mueller P, Jayachandran R, Winkler F, Pieters J, Steinmetz MO,
Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2007) 104(29):12151-6
Cited for: Structure
Szekely R, Waczek F, Szabadkai I, Nemeth G, Hegymegi-Barakonyi B, Eros D, Szokol B, Pato J, Hafenbradl D, Satchell J, Saint-Joanis B, Saint -Joanis B, Cole ST, Orfi L, Klebl BM, Keri G,
A novel drug discovery concept for tuberculosis: inhibition of bacterial and host cell signalling.
Immunol Lett (2008) 116(2):225-31
Cited for: Biochemistry
O'Hare HM, Duran R, Cervenansky C, Bellinzoni M, Wehenkel AM, Pritsch O, Obal G, Baumgartner J, Vialaret J, Johnsson K, Alzari PM,
Regulation of glutamate metabolism by protein kinases in mycobacteria.
Mol Microbiol (2008) 70(6):1408-23
Cited for: Biochemistry
Wolff KA, Nguyen HT, Cartabuke RH, Singh A, Ogwang S, Nguyen L,
Protein kinase G is required for intrinsic antibiotic resistance in mycobacteria.
Antimicrob Agents Chemother (2009) 53(8):3515-9
Cited for: Mutant
Tiwari D, Singh RK, Goswami K, Verma SK, Prakash B, Nandicoori VK,
Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host.
J Biol Chem (2009) 284(40):27467-79
Cited for: Biochemistry/Mutant
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
Kruh NA, Troudt J, Izzo A, Prenni J, Dobos KM,
Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo.
PLoS One (2010) 5(11):e13938
Cited for: Proteomics
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant