Serine/threonine-protein kinase pknB - Mycobacterium tuberculosis

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P0A5S4 (PKNB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase pknB
EC=2.7.11.1

Gene names

Name:	pknB
Ordered Locus Names:	Rv0014c, MT0017
ORF Names:	MTCY10H4.14c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE negative regulation of catalytic activity Inferred from direct assay. Source: MTBBASE negative regulation of protein binding Inferred from direct assay. Source: MTBBASE positive regulation of DNA binding Inferred from direct assay. Source: MTBBASE positive regulation of catalytic activity Inferred from direct assay. Source: MTBBASE protein autophosphorylation Inferred from direct assay. Source: MTBBASE regulation of cell shape Inferred from mutant phenotype. Source: MTBBASE regulation of transferase activity Inferred from direct assay. Source: MTBBASE response to host immune response Inferred from direct assay. Source: MTBBASE
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from direct assay. Source: MTBBASE penicillin binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: MTBBASE protein serine/threonine kinase activity Inferred from direct assay. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

Serine/threonine-protein kinase pknB

PRO_0000171208

Regions

Domain

11 – 274

264

Protein kinase

Domain

356 – 422

PASTA 1

Domain

423 – 490

PASTA 2

Domain

491 – 557

PASTA 3

Domain

558 – 626

PASTA 4

Nucleotide binding

17 – 25

ATP

Sites

Active site

138

Proton acceptor

Metal binding

143

Magnesium

Metal binding

156

Magnesium

Binding site

ATP

Amino acid modifications

Modified residue

166

Phosphoserine; by autocatalysis Ref.4 Ref.6

Modified residue

169

Phosphoserine; by autocatalysis Ref.6

Modified residue

171

Phosphothreonine; by autocatalysis Ref.3 Ref.4 Ref.6

Modified residue

173

Phosphothreonine; by autocatalysis Ref.3 Ref.4 Ref.6

Modified residue

294

Phosphothreonine; by autocatalysis Ref.4 Ref.6

Modified residue

295

Phosphoserine; by autocatalysis Ref.6

Modified residue

309

Phosphothreonine; by autocatalysis Ref.4

Experimental info

Mutagenesis

171

T → A: Reduced activity and autophosphorylation. Ref.3

Mutagenesis

173

T → A: Reduced activity and autophosphorylation. Ref.3

Secondary structure

626

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A5S4 [UniParc].

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

FASTA

626

66,510

        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' referencesShow '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. 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. 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.

PIR

D70699.

RefSeq

NP_214528.1. NC_000962.2.
NP_334425.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MRU	X-ray	3.00	A/B	1-308	[»]
1O6Y	X-ray	2.20	A	1-279	[»]
2FUM	X-ray	2.89	A/B/C/D	1-279	[»]
2KUD	NMR	-	A	355-491	[»]
2KUE	NMR	-	A	423-557	[»]
2KUF	NMR	-	A	491-626	[»]
2KUI	NMR	-	A	355-626	[»]
3F61	X-ray	1.80	A	1-308	[»]
3F69	X-ray	2.80	A/B	1-308	[»]

ProteinModelPortal

P0A5S4.

SMR

P0A5S4. Positions 1-286.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-13376N.

IntAct

P0A5S4. 2 interactions.

PTM databases

PhosSite

P0A5S4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000002226; EBMYCP00000002226; EBMYCG00000002224.
EBMYCT00000069134; EBMYCP00000067193; EBMYCG00000069129.

GeneID

887072.
922465.

GenomeReviews

Gene locus MT0017 in contig AE000516_GR.
Gene locus Rv0014c in contig AL123456_GR.

KEGG

mtc:MT0017.
mtu:Rv0014c.

PATRIC

18121764. VBIMycTub22151_0018.

TIGR

MT0017.

Organism-specific databases

TubercuList

Rv0014c.

Phylogenomic databases

GeneTree

EBGT00050000014804.

HOGENOM

HBG755340.

OMA

TDTGKDP.

PhylomeDB

P0A5S4.

ProtClustDB

CLSK790192.

Family and domain databases

InterPro

IPR011009. 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]

K08884.

Pfam

PF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PKNB_MYCTU

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents