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P72003 (PKNF_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 PknF
EC=2.7.11.1
Gene names
Name:pknF
Ordered Locus Names:Rv1746, MT1788
ORF Names:MTCY28.09
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates the FHA domains of the ABC transporter Rv1747, the heat-shock protein GroEL 1, and Rv0020c. May play a role in the regulation of glucose transport, cell growth and septum formation. Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4 Ref.9 Ref.10

Subunit structure

Interacts with Rv1747. Ref.6

Subcellular location

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

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP. Ref.5

Disruption phenotype

Disruption does not attenuate growth in macrophages. Ref.10

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

groEL2P0A5203EBI-2945875,EBI-2945826
hspXP0A5B72EBI-2945875,EBI-2945921

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Serine/threonine-protein kinase PknF
PRO_0000171213

Regions

Transmembrane306 – 32621Helical; Potential
Domain12 – 279268Protein kinase
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1371Proton acceptor By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue81Phosphothreonine; by autocatalysis Ref.5
Modified residue131Phosphothreonine; by autocatalysis Ref.5
Modified residue1731Phosphothreonine; by autocatalysis Ref.5
Modified residue1751Phosphothreonine; by autocatalysis Ref.5
Modified residue2871Phosphothreonine; by autocatalysis Ref.5
Modified residue2901Phosphoserine; by autocatalysis Ref.5

Experimental info

Mutagenesis411K → M: Loss of kinase activity. Abolishes interaction with Rv1747. Ref.3 Ref.6 Ref.9
Mutagenesis1731T → A: Abolishes interaction with Rv1747. Impairs autokinase activity. Ref.6 Ref.9
Mutagenesis1751T → A: Decreases interaction with Rv1747. Decreases autokinase activity. Ref.6 Ref.9
Mutagenesis1781T → A: Decreases interaction with Rv1747. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P72003 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 8A9C755F912D4776

FASTA47650,668
        10         20         30         40         50         60 
MPLAEGSTFA GFTIVRQLGS GGMGEVYLAR HPRLPRQDAL KVLRADVSAD GEYRARFNRE 

        70         80         90        100        110        120 
ADAAASLWHP HIVAVHDRGE FDGQLWIDMD FVDGTDTVSL LRDRYPNGMP GPEVTEIITA 

       130        140        150        160        170        180 
VAEALDYAHE RRLLHRDVKP ANILIANPDS PDRRIMLADF GIAGWVDDPS GLTATNMTVG 

       190        200        210        220        230        240 
TVSYAAPEQL MGNELDGRAD QYALAATAFH LLTGSPPFQH ANPAVVISQH LSASPPAIGD 

       250        260        270        280        290        300 
RVPELTPLDP VFAKALAKQP KDRYQRCVDF ARALGHRLGG AGDPDDTRVS QPVAVAAPAK 

       310        320        330        340        350        360 
RSLLRTAVIV PAVLAMLLVM AVAVAVREFQ RADDERAAQP ARTRTTTSAG TTTSVAPAST 

       370        380        390        400        410        420 
TRPAPTTPTT TGAADTATAS PTAAVVAIGA LCFPLGSTGT TKTGATAYCS TLQGTNTTIW 

       430        440        450        460        470 
SLTEDTVASP TVTATADPTE APLPIEQESP IRVCMQQTGQ TRRECREEIR RSNGWP

« 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]"Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization."
Koul A., Choidas A., Tyagi A.K., Drlica K., Singh Y., Ullrich A.
Microbiology 147:2307-2314(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-41.
Strain: ATCC 25618 / H37Rv.
[4]"Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis."
Molle V., Soulat D., Jault J.M., Grangeasse C., Cozzone A.J., Prost J.F.
FEMS Microbiol. Lett. 234:215-223(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
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 THR-8; THR-13; THR-173; THR-175; THR-287 AND SER-290, MASS SPECTROMETRY.
[6]"An ABC transporter containing a forkhead-associated domain interacts with a serine-threonine protein kinase and is required for growth of Mycobacterium tuberculosis in mice."
Curry J.M., Whalan R., Hunt D.M., Gohil K., Strom M., Rickman L., Colston M.J., Smerdon S.J., Buxton R.S.
Infect. Immun. 73:4471-4477(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RV1747, MUTAGENESIS OF LYS-41; THR-173; THR-175 AND THR-178.
Strain: ATCC 25618 / H37Rv.
[7]"Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division."
Deol P., Vohra R., Saini A.K., Singh A., Chandra H., Chopra P., Das T.K., Tyagi A.K., Singh Y.
J. Bacteriol. 187:3415-3420(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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.
[9]"The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases."
Canova M.J., Kremer L., Molle V.
J. Bacteriol. 191:2876-2883(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-41; THR-173 AND THR-175.
[10]"Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is positively regulated by Ser/Thr phosphorylation in Mycobacterium tuberculosis."
Spivey V.L., Molle V., Whalan R.H., Rodgers A., Leiba J., Stach L., Walker K.B., Smerdon S.J., Buxton R.S.
J. Biol. Chem. 286:26198-26209(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842577 Genomic DNA. Translation: CAB09332.1.
AE000516 Genomic DNA. Translation: AAK46061.1.
AL123456 Genomic DNA. Translation: CCP44512.1.
PIRC70986.
RefSeqNP_216262.1. NC_000962.3.
NP_336247.1. NC_002755.2.
YP_006515144.1. NC_018143.1.

3D structure databases

ProteinModelPortalP72003.
SMRP72003. Positions 18-265.
ModBaseSearch...

Protein-protein interaction databases

IntActP72003. 2 interactions.
STRING83332.Rv1746.

PTM databases

PhosSiteP0603143.

Proteomic databases

PRIDEP72003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46061; AAK46061; MT1788.
GeneID13316535.
885275.
925724.
KEGGmtc:MT1788.
mtu:Rv1746.
mtv:RVBD_1746.
PATRIC18125688. VBIMycTub22151_1957.

Organism-specific databases

TubercuListRv1746.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000077804.
KOK08884.
OMAPATMVEV.
ProtClustDBCLSK791369.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKNF_MYCTU
AccessionPrimary (citable) accession number: P72003
Secondary accession number(s): L0T7T0, O08151
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 101 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

SIMILARITY comments

Index of protein domains and families

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