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P95078 (PKNK_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 109. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PknK

EC=2.7.11.1
Alternative name(s):
Protein kinase K
Gene names
Name:pknK
Ordered Locus Names:Rv3080c, MT3165
ORF Names:MTCY22D7.01, MTV013.01c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length1110 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key microbial factor involved in regulation of early and late events in tuberculosis infection, and in host-pathogen interactions. Modulates host immunity during early infection. Slows mycobacterial growth during chronic infection in host and during a variety of stress conditions in vitro. Regulates the expression of a large subset of tRNA genes as a means to facilitate adaptation to changing growth environments. In vitro, directs the inhibition of transcription and translation processes in a phosphorylation-dependent manner. Phosphorylates the transcriptional regulator VirS, thereby increasing the affinity of VirS for the mycobacterial monooxygenase (mymA) promoter. In vitro, can also phosphorylate the mycobacterial monooxygenase operon products Rv3083 (MymA), Rv3084 (LipR), Rv3085 and Rv3088. Ref.3 Ref.4 Ref.5 Ref.6

Catalytic activity

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

Subunit structure

Forms oligomeric complexes in solution. Ref.5

Subcellular location

Cytoplasm. Cell membrane. Secretedcell wall. Note: Probably attached to the cell membrane through interactions mediated by its C-terminal region. May be secreted during infection. Ref.3 Ref.4

Induction

Induced during early infection in human macrophages. Ref.4 Ref.6

Domain

The C-terminal region exerts intrasteric control that autoregulates kinase activity. Ref.5

Post-translational modification

Can autophosphorylate the carboxyl terminal region in addition to Thr-179 and Thr-181.

Disruption phenotype

Deletion affects cell size and cell wall composition, increases survival during persistent infection in mice, and increases resistance to acidic pH, hypoxia, oxidative and stationary-phase stresses in vitro. Ref.4

Sequence similarities

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

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-6418825,EBI-6418825

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11101110Serine/threonine-protein kinase PknK
PRO_0000171224

Regions

Domain26 – 283258Protein kinase
Nucleotide binding32 – 409ATP By similarity

Sites

Active site1491Proton acceptor By similarity
Metal binding1541Magnesium By similarity
Metal binding1671Magnesium By similarity
Binding site551ATP By similarity

Amino acid modifications

Modified residue1791Phosphothreonine; by autocatalysis Ref.3
Modified residue1811Phosphothreonine; by autocatalysis Ref.3

Experimental info

Mutagenesis551K → M: Loss of activity. Ref.3
Mutagenesis1791T → A: Loss of activity; when associated with A-181. Ref.3
Mutagenesis1811T → A: Loss of activity; when associated with A-179. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P95078 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: 2F81BF18BCD3E472

FASTA1,110119,418
        10         20         30         40         50         60 
MTDVDPHATR RDLVPNIPAE LLEAGFDNVE EIGRGGFGVV YRCVQPSLDR AVAVKVLSTD 

        70         80         90        100        110        120 
LDRDNLERFL REQRAMGRLS GHPHIVTVLQ VGVLAGGRPF IVMPYHAKNS LETLIRRHGP 

       130        140        150        160        170        180 
LDWRETLSIG VKLAGALEAA HRVGTLHRDV KPGNILLTDY GEPQLTDFGI ARIAGGFETA 

       190        200        210        220        230        240 
TGVIAGSPAF TAPEVLEGAS PTPASDVYSL GATLFCALTG HAAYERRSGE RVIAQFLRIT 

       250        260        270        280        290        300 
SQPIPDLRKQ GLPADVAAAI ERAMARHPAD RPATAADVGE ELRDVQRRNG VSVDEMPLPV 

       310        320        330        340        350        360 
ELGVERRRSP EAHAAHRHTG GGTPTVPTPP TPATKYRPSV PTGSLVTRSR LTDILRAGGR 

       370        380        390        400        410        420 
RRLILIHAPS GFGKSTLAAQ WREELSRDGA AVAWLTIDND DNNEVWFLSH LLESIRRVRP 

       430        440        450        460        470        480 
TLAESLGHVL EEHGDDAGRY VLTSLIDEIH ENDDRIAVVI DDWHRVSDSR TQAALGFLLD 

       490        500        510        520        530        540 
NGCHHLQLIV TSWSRAGLPV GRLRIGDELA EIDSAALRFD TDEAAALLND AGGLRLPRAD 

       550        560        570        580        590        600 
VQALTTSTDG WAAALRLAAL SLRGGGDATQ LLRGLSGASD VIHEFLSENV LDTLEPELRE 

       610        620        630        640        650        660 
FLLVASVTER TCGGLASALA GITNGRAMLE EAEHRGLFLQ RTEDDPNWFR FHQMFADFLH 

       670        680        690        700        710        720 
RRLERGGSHR VAELHRRASA WFAENGYLHE AVDHALAAGD PARAVDLVEQ DETNLPEQSK 

       730        740        750        760        770        780 
MTTLLAIVQK LPTSMVVSRA RLQLAIAWAN ILLQRPAPAT GALNRFETAL GRAELPEATQ 

       790        800        810        820        830        840 
ADLRAEADVL RAVAEVFADR VERVDDLLAE AMSRPDTLPP RVPGTAGNTA ALAAICRFEF 

       850        860        870        880        890        900 
AEVYPLLDWA APYQEMMGPF GTVYAQCLRG MAARNRLDIV AALQNFRTAF EVGTAVGAHS 

       910        920        930        940        950        960 
HAARLAGSLL AELLYETGDL AGAGRLMDES YLLGSEGGAV DYLAARYVIG ARVKAAQGDH 

       970        980        990       1000       1010       1020 
EGAADRLSTG GDTAVQLGLP RLAARINNER IRLGIALPAA VAADLLAPRT IPRDNGIATM 

      1030       1040       1050       1060       1070       1080 
TAELDEDSAV RLLSAGDSAD RDQACQRAGA LAAAIDGTRR PLAALQAQIL HIETLAATGR 

      1090       1100       1110 
ESDARNELAP VATKCAELGL SRLLVDAGLA 

« 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]"The Mycobacterium tuberculosis protein kinase K modulates activation of transcription from the promoter of mycobacterial monooxygenase operon through phosphorylation of the transcriptional regulator VirS."
Kumar P., Kumar D., Parikh A., Rananaware D., Gupta M., Singh Y., Nandicoori V.K.
J. Biol. Chem. 284:11090-11099(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-179 AND THR-181, MUTAGENESIS OF LYS-55; THR-179 AND THR-181.
Strain: ATCC 25618 / H37Rv.
[4]"Mycobacterium tuberculosis protein kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications for immune modulation."
Malhotra V., Arteaga-Cortes L.T., Clay G., Clark-Curtiss J.E.
Microbiology 156:2829-2841(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE.
Strain: ATCC 25618 / H37Rv.
[5]"Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control."
Malhotra V., Okon B.P., Clark-Curtiss J.E.
J. Bacteriol. 194:4184-4196(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, DOMAIN.
Strain: ATCC 25618 / H37Rv.
[6]"Functional characterization delineates that a Mycobacterium tuberculosis specific protein kinase (Rv3080c) is responsible for the growth, phagocytosis and intracellular survival of avirulent mycobacteria."
Kumari R., Singh S.K., Singh D.K., Singh P.K., Chaurasiya S.K., Srivastava K.K.
Mol. Cell. Biochem. 369:67-74(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK47501.1.
AL123456 Genomic DNA. Translation: CCP45889.1.
PIRA70652.
RefSeqNP_217596.1. NC_000962.3.
NP_337687.1. NC_002755.2.
YP_006516541.1. NC_018143.2.

3D structure databases

ProteinModelPortalP95078.
SMRP95078. Positions 30-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING83332.Rv3080c.

Proteomic databases

PRIDEP95078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47501; AAK47501; MT3165.
CCP45889; CCP45889; Rv3080c.
GeneID13317885.
888659.
926679.
KEGGmtc:MT3165.
mtu:Rv3080c.
mtv:RVBD_3080c.
PATRIC18128722. VBIMycTub22151_3458.

Organism-specific databases

TubercuListRv3080c.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000074403.
KOK13419.
OMARIDLQIN.
OrthoDBEOG69GZGV.
ProtClustDBCLSK792267.

Enzyme and pathway databases

BioCycMTBCDC:MT3165-MONOMER.
MTBRV:RV3080C-MONOMER.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016236. Ser/Thr_kinase_PknK_prd.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000574. Ser/Thr_PK_PknK_prd. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKNK_MYCTU
AccessionPrimary (citable) accession number: P95078
Secondary accession number(s): L0TEA2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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

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