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P0A5S4 (PKNB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PknB

EC=2.7.11.1
Gene names
Name:pknB
Ordered Locus Names:Rv0014c, MT0017
ORF Names:MTCY10H4.14c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA (Rv0020c), MviN, PstP, EmbR, Rv1422 and Rv1747. Shows a strong preference for Thr versus Ser as the phosphoacceptor. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.12 Ref.20

Enzyme regulation

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. Ref.14 Ref.16 Ref.21 Ref.23

Subunit structure

Homodimer. Interacts with the FHA domain of GarA, FhaB and FhaA. Ref.7 Ref.12 Ref.14 Ref.17 Ref.21

Subcellular location

Cell membrane; Single-pass membrane protein. Note: Localizes to septum and cell poles. Ref.16

Induction

Expressed predominantly in exponential phase. Ref.6 Ref.14 Ref.16 Ref.21 Ref.23

Domain

The PASTA domains interact with peptidoglycans and are required for PknB localization. Ref.16

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.20 Ref.22

Disruption phenotype

Essential for growth, it cannot be disrupted. Ref.10

Miscellaneous

Overexpression causes major growth and morphological changes that indicate defects in cell wall synthesis and possibly in cell division (Ref.6).

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 4 PASTA domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processgrowth

Inferred from mutant phenotype PubMed 12657046Ref.6Ref.10. Source: MTBBASE

negative regulation of catalytic activity

Inferred from direct assay PubMed 16873379. Source: MTBBASE

negative regulation of fatty acid biosynthetic process

Inferred from direct assay PubMed 20178986. Source: MTBBASE

negative regulation of protein binding

Inferred from direct assay PubMed 18685700. Source: MTBBASE

positive regulation of DNA binding

Inferred from direct assay Ref.9. Source: MTBBASE

positive regulation of catalytic activity

Inferred from direct assay PubMed 16873379. Source: MTBBASE

protein autophosphorylation

Inferred from direct assay Ref.4Ref.6. Source: MTBBASE

regulation of cell shape

Inferred from mutant phenotype Ref.6. Source: MTBBASE

regulation of transferase activity

Inferred from direct assay Ref.13. Source: MTBBASE

response to host immune response

Inferred from direct assay Ref.4. Source: MTBBASE

   Cellular_componentcell wall

Inferred from direct assay PubMed 20825248. Source: MTBBASE

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from direct assay Ref.4. Source: MTBBASE

penicillin binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine kinase activity

Inferred from direct assay Ref.4Ref.6PubMed 18685700Ref.13Ref.12. Source: MTBBASE

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Serine/threonine-protein kinase PknB
PRO_0000171208

Regions

Topological domain1 – 332332Cytoplasmic Potential
Transmembrane333 – 35321Helical; Potential
Topological domain354 – 626273Extracellular Potential
Domain11 – 274264Protein kinase
Domain356 – 42267PASTA 1
Domain423 – 49068PASTA 2
Domain491 – 55767PASTA 3
Domain558 – 62669PASTA 4
Nucleotide binding17 – 259ATP
Nucleotide binding93 – 953ATP
Nucleotide binding140 – 1434ATP

Sites

Active site1381Proton acceptor
Metal binding1431Magnesium
Metal binding1561Magnesium
Binding site401ATP
Binding site1561ATP

Amino acid modifications

Modified residue1661Phosphoserine; by autocatalysis Ref.5 Ref.20
Modified residue1691Phosphoserine; by autocatalysis Ref.20
Modified residue1711Phosphothreonine; by autocatalysis Ref.3 Ref.5 Ref.6 Ref.20 Ref.22
Modified residue1731Phosphothreonine; by autocatalysis Ref.3 Ref.5 Ref.6 Ref.20
Modified residue2941Phosphothreonine; by autocatalysis Ref.5 Ref.20
Modified residue2951Phosphoserine; by autocatalysis Ref.20
Modified residue3091Phosphothreonine; by autocatalysis Ref.5

Experimental info

Mutagenesis101R → A: Impairs kinase activity. Ref.14
Mutagenesis331L → D: Impairs kinase activity. Ref.14
Mutagenesis401K → M: Lack of autophosphorylation. Decreases affinity for FhaB. Ref.6 Ref.12
Mutagenesis761D → A: Impairs kinase activity. Ref.14
Mutagenesis1381D → N: Impairs kinase activity. Ref.14
Mutagenesis1711T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. Ref.3 Ref.7 Ref.12
Mutagenesis1731T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. Ref.3 Ref.7 Ref.12
Mutagenesis2941T → A: Does not affect activity. Ref.12
Mutagenesis3091T → A: Does not affect activity. Ref.12

Secondary structure

................................................................................................ 626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A5S4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 6C27EEBE9D5A453B

FASTA62666,510
        10         20         30         40         50         60 
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA 

        70         80         90        100        110        120 
QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL RDIVHTEGPM TPKRAIEVIA 

       130        140        150        160        170        180 
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSGNSV TQTAAVIGTA 

       190        200        210        220        230        240 
QYLSPEQARG DSVDARSDVY SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH 

       250        260        270        280        290        300 
EGLSADLDAV VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA 

       310        320        330        340        350        360 
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI NTFGGITRDV 

       370        380        390        400        410        420 
QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI GTDPAANTSV SAGDEITVNV 

       430        440        450        460        470        480 
STGPEQREIP DVSTLTYAEA VKKLTAAGFG RFKQANSPST PELVGKVIGT NPPANQTSAI 

       490        500        510        520        530        540 
TNVVIIIVGS GPATKDIPDV AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP 

       550        560        570        580        590        600 
AGTTVPVDSV IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH 

       610        620 
NRVVYQNPPA GTGVNRDGII TLRFGQ 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"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, MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[4]"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.
[5]"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, MASS SPECTROMETRY.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[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]"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.
[16]"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.
[17]"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.
[18]"A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria."
Gee C.L., Papavinasasundaram K.G., Blair S.R., Baer C.E., Falick A.M., King D.S., Griffin J.E., Venghatakrishnan H., Zukauskas A., Wei J.R., Dhiman R.K., Crick D.C., Rubin E.J., Sassetti C.M., Alber T.
Sci. Signal. 5:RA7-RA7(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"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.
[20]"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, MASS SPECTROMETRY.
[21]"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.
[22]"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.
[23]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK44239.1.
AL123456 Genomic DNA. Translation: CCP42736.1.
PIRD70699.
RefSeqNP_214528.1. NC_000962.3.
NP_334425.1. NC_002755.2.
YP_006513328.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A5S4.
SMRP0A5S4. Positions 2-287, 355-626.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-13376N.
IntActP0A5S4. 3 interactions.
MINTMINT-7293801.
STRING83332.Rv0014c.

PTM databases

PhosSiteP0603150.

Proteomic databases

PRIDEP0A5S4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK44239; AAK44239; MT0017.
GeneID13315991.
887072.
922465.
KEGGmtc:MT0017.
mtu:Rv0014c.
PATRIC18121764. VBIMycTub22151_0018.

Organism-specific databases

TubercuListRv0014c.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037185.
KOK08884.
OMATGKDPGT.
ProtClustDBCLSK790192.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP0A5S4.
ChEMBLCHEMBL1908385.
EvolutionaryTraceP0A5S4.

Entry information

Entry namePKNB_MYCTU
AccessionPrimary (citable) accession number: P0A5S4
Secondary accession number(s): L0T5F6, P71584
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families