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P0A5S4 (PKNB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

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

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Post-translational modification

Dephosphorylated by pstP. Ref.3 Ref.4 Ref.6

Sequence similarities

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

Contains 4 PASTA domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Serine/threonine-protein kinase pknB
PRO_0000171208

Regions

Domain11 – 274264Protein kinase
Domain356 – 42267PASTA 1
Domain423 – 49068PASTA 2
Domain491 – 55767PASTA 3
Domain558 – 62669PASTA 4
Nucleotide binding17 – 259ATP

Sites

Active site1381Proton acceptor
Metal binding1431Magnesium
Metal binding1561Magnesium
Binding site401ATP

Amino acid modifications

Modified residue1661Phosphoserine; by autocatalysis Ref.4 Ref.6
Modified residue1691Phosphoserine; by autocatalysis Ref.6
Modified residue1711Phosphothreonine; by autocatalysis Ref.3 Ref.4 Ref.6
Modified residue1731Phosphothreonine; by autocatalysis Ref.3 Ref.4 Ref.6
Modified residue2941Phosphothreonine; by autocatalysis Ref.4 Ref.6
Modified residue2951Phosphoserine; by autocatalysis Ref.6
Modified residue3091Phosphothreonine; by autocatalysis Ref.4

Experimental info

Mutagenesis1711T → A: Reduced activity and autophosphorylation. Ref.3
Mutagenesis1731T → A: Reduced activity and autophosphorylation. Ref.3

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: 9634230] [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: 12218036] [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: 12950916] [Abstract]
Cited for: PROTEIN SEQUENCE OF 162-189, KINASE ACTIVITY, PHOSPHORYLATION AT THR-171 AND THR-173, MUTAGENESIS OF THR-171 AND THR-173, MASS SPECTROMETRY.
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: 15967413] [Abstract]
Cited for: PHOSPHORYLATION AT SER-166; THR-171; THR-173; THR-294 AND THR-309, MASS SPECTROMETRY.
[5]"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: 16436437] [Abstract]
Cited for: FUNCTION AS A KINASE WITH PBPA AS SUBSTRATE.
Strain: ATCC 25618 / H37Rv.
[6]"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: 12548283] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-308, KINASE 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842572 Genomic DNA. Translation: CAB02434.1.
AE000516 Genomic DNA. Translation: AAK44239.1.
PIRD70699.
RefSeqNP_214528.1. NC_000962.2.
NP_334425.1. NC_002755.2.

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 1-286.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-13376N.
IntActP0A5S4. 2 interactions.

PTM databases

PhosSiteP0A5S4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000002226; EBMYCP00000002226; EBMYCG00000002224.
EBMYCT00000069134; EBMYCP00000067193; EBMYCG00000069129.
GeneID887072.
922465.
GenomeReviewsGene locus MT0017 in contig AE000516_GR.
Gene locus Rv0014c in contig AL123456_GR.
KEGGmtc:MT0017.
mtu:Rv0014c.
PATRIC18121764. VBIMycTub22151_0018.
TIGRMT0017.

Organism-specific databases

TubercuListRv0014c.

Phylogenomic databases

GeneTreeEBGT00050000014804.
HOGENOMHBG755340.
OMATDTGKDP.
PhylomeDBP0A5S4.
ProtClustDBCLSK790192.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
KOK08884.
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...

Entry information

Entry namePKNB_MYCTU
AccessionPrimary (citable) accession number: P0A5S4
Secondary accession number(s): P71584
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families