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P72001 (PKNE_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. 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
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 PknE
EC=2.7.11.1
Gene names
Name:pknE
Ordered Locus Names:Rv1743, MT1785
ORF Names:MTCY28.05
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important for survival of the bacterium in the host during infection. Promotes the survival of infected macrophages by activating multiple signaling responses and suppressing apoptosis of macrophages during nitrate stress. May contribute to the adaptation of M.tuberculosis during stress conditions by maintaining the cellular integrity. Can phosphorylate the FHA domain of Rv1747. Ref.5 Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3

Subunit structure

Homodimer. Ref.10

Subcellular location

Cell membrane; Single-pass membrane protein Ref.3.

Induction

Induced by nitric oxide stress. Repressed under oxidative stress. Ref.7

Post-translational modification

Autophosphorylated on serine and threonine residues. Dephosphorylated by PstP. Ref.3 Ref.4 Ref.6

Disruption phenotype

Mutants show increased resistance to nitric oxide donors, increased sensitivity to reducing agents, and growth reduction at pH 7.0 and in the presence of lysozyme. They increase macrophage apoptosis, and exhibit lower rates of survival and multiplication in an in vitro macrophage model of infection. Ref.7 Ref.8 Ref.9

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Serine/threonine-protein kinase PknE
PRO_0000171211

Regions

Topological domain1 – 337337Cytoplasmic Potential
Transmembrane338 – 35821Helical; Potential
Topological domain359 – 566208Extracellular Potential
Domain16 – 275260Protein kinase
Nucleotide binding22 – 309ATP By similarity

Sites

Active site1391Proton acceptor By similarity
Binding site451ATP By similarity

Amino acid modifications

Modified residue71Phosphoserine; by autocatalysis Ref.4
Modified residue111Phosphothreonine; by autocatalysis Ref.4
Modified residue501Phosphothreonine; by autocatalysis Ref.4
Modified residue591Phosphothreonine; by autocatalysis Ref.4
Modified residue1701Phosphothreonine; by autocatalysis Ref.4
Modified residue1751Phosphothreonine; by autocatalysis Ref.4
Modified residue1781Phosphothreonine; by autocatalysis Ref.4

Experimental info

Mutagenesis451K → M: Lack of kinase activity. Ref.3

Secondary structure

1 ........................................ 566
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P72001 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C31534068DE60FE4

FASTA56660,512
        10         20         30         40         50         60 
MDGTAESREG TQFGPYRLRR LVGRGGMGDV YEAEDTVRER IVALKLMSET LSSDPVFRTR 

        70         80         90        100        110        120 
MQREARTAGR LQEPHVVPIH DFGEIDGQLY VDMRLINGVD LAAMLRRQGP LAPPRAVAIV 

       130        140        150        160        170        180 
RQIGSALDAA HAAGATHRDV KPENILVSAD DFAYLVDFGI ASATTDEKLT QLGNTVGTLY 

       190        200        210        220        230        240 
YMAPERFSES HATYRADIYA LTCVLYECLT GSPPYQGDQL SVMGAHINQA IPRPSTVRPG 

       250        260        270        280        290        300 
IPVAFDAVIA RGMAKNPEDR YVTCGDLSAA AHAALATADQ DRATDILRRS QVAKLPVPST 

       310        320        330        340        350        360 
HPVSPGTRWP QPTPWAGGAP PWGPPSSPLP RSARQPWLWV GVAVAVVVAL AGGLGIALAH 

       370        380        390        400        410        420 
PWRSSGPRTS APPPPPPADA VELRVLNDGV FVGSSVAPTT IDIFNEPICP PCGSFIRSYA 

       430        440        450        460        470        480 
SDIDTAVADK QLAVRYHLLN FLDDQSHSKN YSTRAVAASY CVAGQNDPKL YASFYSALFG 

       490        500        510        520        530        540 
SDFQPQENAA SDRTDAELAH LAQTVGAEPT AISCIKSGAD LGTAQTKATN ASETLAGFNA 

       550        560 
SGTPFVWDGS MVVNYQDPSW LARLIG

« 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]"Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis."
Molle V., Girard-Blanc C., Kremer L., Doublet P., Cozzone A.J., Prost J.F.
Biochem. Biophys. Res. Commun. 308:820-825(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-45.
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-7; THR-11; THR-50; THR-59; THR-170; THR-175 AND THR-178, MASS SPECTROMETRY.
[5]"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.
[6]"Characterization of the phosphorylation sites of Mycobacterium tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH by mass spectrometry."
Molle V., Zanella-Cleon I., Robin J.P., Mallejac S., Cozzone A.J., Becchi M.
Proteomics 6:3754-3766(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[7]"Protein kinase E of Mycobacterium tuberculosis has a role in the nitric oxide stress response and apoptosis in a human macrophage model of infection."
Jayakumar D., Jacobs W.R. Jr., Narayanan S.
Cell. Microbiol. 10:365-374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VIRULENCE, INDUCTION, DISRUPTION PHENOTYPE.
Strain: ATCC 25618 / H37Rv.
[8]"PknE, a serine/threonine protein kinase from Mycobacterium tuberculosis has a role in adaptive responses."
Kumar D., Palaniyandi K., Challu V.K., Kumar P., Narayanan S.
Arch. Microbiol. 195:75-80(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VIRULENCE, DISRUPTION PHENOTYPE.
Strain: ATCC 25618 / H37Rv.
[9]"pknE, a serine/threonine kinase of Mycobacterium tuberculosis modulates multiple apoptotic paradigms."
Kumar D., Narayanan S.
Infect. Genet. Evol. 12:737-747(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VIRULENCE, DISRUPTION PHENOTYPE.
[10]"A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis."
Gay L.M., Ng H.L., Alber T.
J. Mol. Biol. 360:409-420(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-289, SUBUNIT.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842577 Genomic DNA. Translation: CAB09329.1.
AE000516 Genomic DNA. Translation: AAK46058.1.
AL123456 Genomic DNA. Translation: CCP44509.1.
PIRH70985.
RefSeqNP_216259.1. NC_000962.3.
NP_336244.1. NC_002755.2.
YP_006515141.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H34X-ray2.80A/B1-289[»]
ProteinModelPortalP72001.
SMRP72001. Positions 14-268.
ModBaseSearch...

Protein-protein interaction databases

IntActP72001. 2 interactions.
STRING83332.Rv1743.

PTM databases

PhosSiteP0603140.

Proteomic databases

PRIDEP72001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46058; AAK46058; MT1785.
GeneID13316532.
885284.
923921.
KEGGmtc:MT1785.
mtu:Rv1743.
mtv:RVBD_1743.
PATRIC18125678. VBIMycTub22151_1952.

Organism-specific databases

TubercuListRv1743.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000050013.
KOK08884.
OMATTTIDIF.
ProtClustDBCLSK791367.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP72001.

Entry information

Entry namePKNE_MYCTU
AccessionPrimary (citable) accession number: P72001
Secondary accession number(s): L0TA94, O08149
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 117 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents