Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase PknB

Gene

pknB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase that regulates many aspects of mycobacterial physiology, and is critical for growth in vitro and survival of the pathogen in the host (PubMed:24706757). Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA (Rv0020c), MviN, PstP, EmbR, Rv1422, Rv1747 and RseA (PubMed:15978616, PubMed:15985609, PubMed:15987910, PubMed:16436437, PubMed:16817899, PubMed:16980473, PubMed:19121323, PubMed:19826007, PubMed:20025669, PubMed:21423706, PubMed:22275220). Also catalyzes the phosphorylation of the core proteasome alpha-subunit (PrcA), and thereby regulates the proteolytic activity of the proteasome (PubMed:25224505). Is a major regulator of the oxygen-dependent replication switch since PknB activity is necessary for reactivation of cells from the hypoxic state (PubMed:24409094). Shows a strong preference for Thr versus Ser as the phosphoacceptor. Overexpression of PknB alters cell morphology and leads to cell death (PubMed:24706757) (PubMed:24409094).14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.7 Publications

Enzyme regulationi

Interaction of the PASTA domains with peptidoglycan leads to septal and polar localization of PknB, and dimerization of the intracellular kinase domain. Dimerization activates the kinase domain via an allosteric mechanism, triggering autophosphorylation and phosphorylation of target proteins. Inhibited by mitoxantrone. Inhibition prevents mycobacterial growth.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATPPROSITE-ProRule annotation2 Publications
Active sitei138 – 1381Proton acceptor
Metal bindingi143 – 1431Magnesium
Metal bindingi156 – 1561Magnesium
Binding sitei156 – 1561ATPPROSITE-ProRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATPPROSITE-ProRule annotation2 Publications
Nucleotide bindingi93 – 953ATPPROSITE-ProRule annotation2 Publications
Nucleotide bindingi140 – 1434ATPPROSITE-ProRule annotation2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • manganese ion binding Source: MTBBASE
  • protein kinase activity Source: MTBBASE
  • protein serine/threonine kinase activity Source: MTBBASE

GO - Biological processi

  • growth Source: MTBBASE
  • negative regulation of catalytic activity Source: MTBBASE
  • negative regulation of fatty acid biosynthetic process Source: MTBBASE
  • negative regulation of protein binding Source: MTBBASE
  • pathogenesis Source: UniProtKB-KW
  • positive regulation of catalytic activity Source: MTBBASE
  • positive regulation of DNA binding Source: MTBBASE
  • protein autophosphorylation Source: MTBBASE
  • regulation of cell shape Source: MTBBASE
  • regulation of transferase activity Source: MTBBASE
  • response to host immune response Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PknB (EC:2.7.11.1)
Gene namesi
Name:pknB
Ordered Locus Names:Rv0014c
ORF Names:MTCY10H4.14c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0014c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 332331CytoplasmicSequence analysisAdd
BLAST
Transmembranei333 – 35321HelicalSequence analysisAdd
BLAST
Topological domaini354 – 626273ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Essential for growth, it cannot be disrupted (PubMed:16980473). PknB depletion in M.tuberculosis results in cell death and aberrant cell morphology, and leads to complete clearance of the pathogen from the host tissues using the murine infection model (PubMed:24706757).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101R → A: Impairs kinase activity. 1 Publication
Mutagenesisi33 – 331L → D: Impairs kinase activity. 1 Publication
Mutagenesisi40 – 401K → M: Lack of autophosphorylation. Decreases affinity for FhaB. 2 Publications
Mutagenesisi76 – 761D → A: Impairs kinase activity. 1 Publication
Mutagenesisi138 – 1381D → N: Impairs kinase activity. 1 Publication
Mutagenesisi171 – 1711T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. 3 Publications
Mutagenesisi173 – 1731T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. 3 Publications
Mutagenesisi294 – 2941T → A: Does not affect activity. 1 Publication
Mutagenesisi309 – 3091T → A: Does not affect activity. 1 Publication

Chemistry

ChEMBLiCHEMBL1908385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 626625Serine/threonine-protein kinase PknBPRO_0000171208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei166 – 1661Phosphoserine; by autocatalysis2 Publications
Modified residuei169 – 1691Phosphoserine; by autocatalysis1 Publication
Modified residuei171 – 1711Phosphothreonine; by autocatalysis5 Publications
Modified residuei173 – 1731Phosphothreonine; by autocatalysis4 Publications
Modified residuei294 – 2941Phosphothreonine; by autocatalysis2 Publications
Modified residuei295 – 2951Phosphoserine; by autocatalysis1 Publication
Modified residuei309 – 3091Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylated. Dephosphorylated by PstP.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP9WI81.

PTM databases

iPTMnetiP9WI81.

Expressioni

Inductioni

Expressed predominantly in exponential phase (PubMed:15985609). PknB levels are regulated in response to hypoxia; its expression is down-regulated during hypoxia and recovers to aerated levels upon reaeration (at mRNA and protein level) (PubMed:24409094).2 Publications

Interactioni

Subunit structurei

Homodimer. Interacts with the FHA domain of GarA, FhaB and FhaA.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-2946037,EBI-2946037
garAP9WJA92EBI-2946037,EBI-6405522

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiP9WI81. 3 interactions.
STRINGi83332.Rv0014c.

Chemistry

BindingDBiP9WI81.

Structurei

Secondary structure

1
626
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Turni8 – 103Combined sources
Beta strandi11 – 199Combined sources
Beta strandi21 – 3010Combined sources
Turni31 – 344Combined sources
Beta strandi35 – 428Combined sources
Helixi44 – 463Combined sources
Helixi50 – 6011Combined sources
Beta strandi74 – 829Combined sources
Beta strandi85 – 939Combined sources
Beta strandi97 – 993Combined sources
Helixi100 – 1078Combined sources
Helixi112 – 13120Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi167 – 1693Combined sources
Helixi185 – 1895Combined sources
Helixi195 – 21117Combined sources
Helixi221 – 23010Combined sources
Helixi236 – 2394Combined sources
Beta strandi240 – 2423Combined sources
Helixi245 – 25410Combined sources
Helixi259 – 2613Combined sources
Helixi266 – 27712Combined sources
Beta strandi358 – 3614Combined sources
Helixi370 – 38011Combined sources
Beta strandi383 – 39311Combined sources
Helixi404 – 4074Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi415 – 42410Combined sources
Beta strandi426 – 4283Combined sources
Helixi433 – 4353Combined sources
Helixi437 – 44610Combined sources
Beta strandi452 – 4576Combined sources
Helixi461 – 4633Combined sources
Beta strandi466 – 4727Combined sources
Beta strandi476 – 4794Combined sources
Beta strandi484 – 4896Combined sources
Beta strandi494 – 4963Combined sources
Beta strandi502 – 5043Combined sources
Helixi505 – 51511Combined sources
Beta strandi520 – 5256Combined sources
Beta strandi532 – 5398Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi551 – 5566Combined sources
Beta strandi559 – 5624Combined sources
Helixi571 – 58111Combined sources
Beta strandi587 – 5948Combined sources
Helixi597 – 5993Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi603 – 6086Combined sources
Beta strandi612 – 6154Combined sources
Beta strandi620 – 6256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRUX-ray3.00A/B1-308[»]
1O6YX-ray2.20A1-279[»]
2FUMX-ray2.89A/B/C/D1-279[»]
2KUDNMR-A355-491[»]
2KUENMR-A423-557[»]
2KUFNMR-A491-626[»]
2KUINMR-A355-626[»]
3F61X-ray1.80A1-308[»]
3F69X-ray2.80A/B1-308[»]
ProteinModelPortaliP9WI81.
SMRiP9WI81. Positions 2-299, 355-626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 274264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini356 – 42267PASTA 1PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 49068PASTA 2PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 55767PASTA 3PROSITE-ProRule annotationAdd
BLAST
Domaini558 – 62669PASTA 4PROSITE-ProRule annotationAdd
BLAST

Domaini

The intracellular kinase domain and all four extracytoplasmic PASTA domains are essential for PknB function and cell survival (PubMed:24706757). The PASTA domains interact with peptidoglycans and are required for PknB localization (PubMed:21829358).2 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 4 PASTA domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
KOiK12132.
OMAiAIDYFGG.
PhylomeDBiP9WI81.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WI81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP
60 70 80 90 100
SFYLRFRREA QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL
110 120 130 140 150
RDIVHTEGPM TPKRAIEVIA DACQALNFSH QNGIIHRDVK PANIMISATN
160 170 180 190 200
AVKVMDFGIA RAIADSGNSV TQTAAVIGTA QYLSPEQARG DSVDARSDVY
210 220 230 240 250
SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH EGLSADLDAV
260 270 280 290 300
VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA
310 320 330 340 350
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI
360 370 380 390 400
NTFGGITRDV QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI
410 420 430 440 450
GTDPAANTSV SAGDEITVNV STGPEQREIP DVSTLTYAEA VKKLTAAGFG
460 470 480 490 500
RFKQANSPST PELVGKVIGT NPPANQTSAI TNVVIIIVGS GPATKDIPDV
510 520 530 540 550
AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP AGTTVPVDSV
560 570 580 590 600
IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH
610 620
NRVVYQNPPA GTGVNRDGII TLRFGQ
Length:626
Mass (Da):66,510
Last modified:April 16, 2014 - v1
Checksum:i6C27EEBE9D5A453B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42736.1.
PIRiD70699.
RefSeqiNP_214528.1. NC_000962.3.
WP_003400356.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP42736; CCP42736; Rv0014c.
GeneIDi887072.
KEGGimtu:Rv0014c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42736.1.
PIRiD70699.
RefSeqiNP_214528.1. NC_000962.3.
WP_003400356.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRUX-ray3.00A/B1-308[»]
1O6YX-ray2.20A1-279[»]
2FUMX-ray2.89A/B/C/D1-279[»]
2KUDNMR-A355-491[»]
2KUENMR-A423-557[»]
2KUFNMR-A491-626[»]
2KUINMR-A355-626[»]
3F61X-ray1.80A1-308[»]
3F69X-ray2.80A/B1-308[»]
ProteinModelPortaliP9WI81.
SMRiP9WI81. Positions 2-299, 355-626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WI81. 3 interactions.
STRINGi83332.Rv0014c.

Chemistry

BindingDBiP9WI81.
ChEMBLiCHEMBL1908385.

PTM databases

iPTMnetiP9WI81.

Proteomic databases

PaxDbiP9WI81.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP42736; CCP42736; Rv0014c.
GeneIDi887072.
KEGGimtu:Rv0014c.

Organism-specific databases

TubercuListiRv0014c.

Phylogenomic databases

eggNOGiENOG4105D9P. Bacteria.
COG0515. LUCA.
COG2815. LUCA.
KOiK12132.
OMAiAIDYFGG.
PhylomeDBiP9WI81.

Miscellaneous databases

PROiP9WI81.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR005543. PASTA_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis."
    Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T., Cervenansky C., Alzari P.M.
    Mol. Microbiol. 49:1493-1508(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 162-189, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-171 AND THR-173, MUTAGENESIS OF THR-171 AND THR-173, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.
  3. "Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB."
    Av-Gay Y., Jamil S., Drews S.J.
    Infect. Immun. 67:5676-5682(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
    Strain: ATCC 25618 / H37Rv.
  4. "Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases."
    Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P., Boitel B., Cole S.T., Alzari P.M., Cervenansky C.
    Biochem. Biophys. Res. Commun. 333:858-867(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-166; THR-171; THR-173; THR-294 AND THR-309, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape."
    Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C., Husson R.N.
    Genes Dev. 19:1692-1704(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, PHOSPHORYLATION AT THR-171 AND THR-173, OVEREXPRESSION, MUTAGENESIS OF LYS-40.
    Strain: ATCC 25618 / H37Rv.
  6. "Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions."
    Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C., Alzari P.M.
    J. Mol. Biol. 350:953-963(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GARA, MUTAGENESIS OF THR-171 AND THR-173.
    Strain: ATCC 25618 / H37Rv.
  7. "Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains."
    Grundner C., Gay L.M., Alber T.
    Protein Sci. 14:1918-1921(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis."
    Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.
    FEBS J. 273:2711-2721(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, DEPHOSPHORYLATION BY PSTP.
  9. "The Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growth."
    Fernandez P., Saint-Joanis B., Barilone N., Jackson M., Gicquel B., Cole S.T., Alzari P.M.
    J. Bacteriol. 188:7778-7784(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: ATCC 25618 / H37Rv.
  10. "The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division."
    Dasgupta A., Datta P., Kundu M., Basu J.
    Microbiology 152:493-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH PBPA AS SUBSTRATE.
    Strain: ATCC 25618 / H37Rv.
  11. "Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis."
    Gupta M., Sajid A., Arora G., Tandon V., Singh Y.
    J. Biol. Chem. 284:34723-34734(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FHAB, MUTAGENESIS OF LYS-40; THR-171; THR-173; THR-294 AND THR-309.
  12. "PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity."
    Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K.
    J. Mol. Biol. 386:451-464(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH GLMU AS SUBSTRATE.
  13. "RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis."
    Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.
    Mol. Microbiol. 75:592-606(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH RSEA AS A SUBSTRATE.
    Strain: ATCC 25618 / H37Rv.
  14. "Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB."
    Lombana T.N., Echols N., Good M.C., Thomsen N.D., Ng H.L., Greenstein A.E., Falick A.M., King D.S., Alber T.
    Structure 18:1667-1677(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ARG-10; LEU-33; ASP-76 AND ASP-138.
    Strain: ATCC 25618 / H37Rv.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  16. "Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB."
    Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y.
    PLoS ONE 6:E17871-E17871(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH PSTP AS SUBSTRATE.
    Strain: ATCC 25618 / H37Rv.
  17. "The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization."
    Mir M., Asong J., Li X., Cardot J., Boons G.J., Husson R.N.
    PLoS Pathog. 7:E1002182-E1002182(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN.
  18. "Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase."
    Roumestand C., Leiba J., Galophe N., Margeat E., Padilla A., Bessin Y., Barthe P., Molle V., Cohen-Gonsaud M.
    Structure 19:1525-1534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHAA.
    Strain: ATCC 25618 / H37Rv.
  19. Cited for: FUNCTION.
  20. "Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host."
    Chawla Y., Upadhyay S., Khan S., Nagarajan S.N., Forti F., Nandicoori V.K.
    J. Biol. Chem. 289:13858-13875(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DOMAIN.
    Strain: H37Rv.
  21. Cited for: FUNCTION, IDENTIFICATION OF PRCA AS SUBSTRATE.
    Strain: H37Rv.
  22. "Mycobacterium tuberculosis Ser/Thr protein kinase B mediates an oxygen-dependent replication switch."
    Ortega C., Liao R., Anderson L.N., Rustad T., Ollodart A.R., Wright A.T., Sherman D.R., Grundner C.
    PLoS Biol. 12:E1001746-E1001746(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: ATCC 27294 / TMC 102 / H37Rv.
  23. "Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis."
    Ortiz-Lombardia M., Pompeo F., Boitel B., Alzari P.M.
    J. Biol. Chem. 278:13094-13100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-279 IN COMPLEX WITH ATP.
  24. "Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases."
    Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., Alber T.
    Nat. Struct. Biol. 10:168-174(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-308 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY, METAL BINDING AT ASN-143 AND ASP-156, ATP BINDING AT LYS-40, PHOSPHORYLATION AT SER-166; SER-169; THR-171; THR-173; THR-294 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY.
  25. "The structure of PknB in complex with mitoxantrone, an ATP-competitive inhibitor, suggests a mode of protein kinase regulation in mycobacteria."
    Wehenkel A., Fernandez P., Bellinzoni M., Catherinot V., Barilone N., Labesse G., Jackson M., Alzari P.M.
    FEBS Lett. 580:3018-3022(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 1-279 IN COMPLEX WITH MITOXANTRONE, ENZYME REGULATION, SUBUNIT.
  26. "Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase."
    Mieczkowski C., Iavarone A.T., Alber T.
    EMBO J. 27:3186-3197(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-308 IN COMPLEX WITH ADP, PHOSPHORYLATION AT THR-171.
  27. "The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation."
    Barthe P., Mukamolova G.V., Roumestand C., Cohen-Gonsaud M.
    Structure 18:606-615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 355-491, ENZYME REGULATION.

Entry informationi

Entry nameiPKNB_MYCTU
AccessioniPrimary (citable) accession number: P9WI81
Secondary accession number(s): L0T5F6, P0A5S4, P71584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Overexpression causes major growth and morphological changes that indicate defects in cell wall synthesis and possibly in cell division.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.