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O53510 (PKNL_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PknL
EC=2.7.11.1
Gene names
Name:pknL
Ordered Locus Names:Rv2176, MT2232
ORF Names:MTV021.09
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates the DNA-binding protein Rv2175c. May be involved in the regulation of cell division and cell envelope biosynthesis. Ref.4 Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4 Ref.5

Subcellular location

Cell membrane; Single-pass membrane protein Probable Ref.4.

Post-translational modification

Autophosphorylated. Thr-173 is required for autophosphorylation and transphosphorylation activities. Thr-175 is not necessary for autophosphorylation activity, but is required for full kinase activity. Ref.3 Ref.4

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 – 399399Serine/threonine-protein kinase PknL
PRO_0000171226

Regions

Topological domain1 – 368368Cytoplasmic Potential
Transmembrane369 – 38921Helical; Potential
Topological domain390 – 39910Extracellular Potential
Domain19 – 278260Protein kinase
Nucleotide binding25 – 339ATP By similarity

Sites

Active site1421Proton acceptor By similarity
Binding site481ATP By similarity

Amino acid modifications

Modified residue321Phosphothreonine; by autocatalysis Ref.4
Modified residue621Phosphothreonine; by autocatalysis Ref.4
Modified residue1731Phosphothreonine; by autocatalysis Ref.4
Modified residue1751Phosphothreonine; by autocatalysis Ref.4
Modified residue3231Phosphothreonine; by autocatalysis Ref.4

Experimental info

Mutagenesis481K → M: Lack of kinase activity. Ref.3 Ref.4
Mutagenesis1711S → A: Does not affect autophosphorylation and transphosphorylation activities. Ref.4
Mutagenesis1731T → A: Strong decrease in autophosphorylation activity. Lack of transphosphorylation activity. Ref.4
Mutagenesis1741S → A: Does not affect autophosphorylation and transphosphorylation activities. Ref.4
Mutagenesis1751T → A: Decrease in autophosphorylation activity. Does not affect transphosphorylation activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O53510 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1E63000018942C89

FASTA39942,834
        10         20         30         40         50         60 
MVEAGTRDPL ESALLDSRYL VQAKIASGGT STVYRGLDVR LDRPVALKVM DSRYAGDEQF 

        70         80         90        100        110        120 
LTRFRLEARA VARLNNRALV AVYDQGKDGR HPFLVMELIE GGTLRELLIE RGPMPPHAVV 

       130        140        150        160        170        180 
AVLRPVLGGL AAAHRAGLVH RDVKPENILI SDDGDVKLAD FGLVRAVAAA SITSTGVILG 

       190        200        210        220        230        240 
TAAYLSPEQV RDGNADPRSD VYSVGVLVYE LLTGHTPFTG DSALSIAYQR LDADVPRASA 

       250        260        270        280        290        300 
VIDGVPPQFD ELVACATARN PADRYADAIA MGADLEAIAE ELALPEFRVP APRNSAQHRS 

       310        320        330        340        350        360 
AALYRSRITQ QGQLGAKPVH HPTRQLTRQP GDCSEPASGS EPEHEPITGQ FAGIAIEEFI 

       370        380        390 
WARQHARRMV LVWVSVVLAI TGLVASAAWT IGSNLSGLL

« 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]"Molecular cloning and biochemical characterization of a serine threonine protein kinase, PknL, from Mycobacterium tuberculosis."
Lakshminarayan H., Narayanan S., Bach H., Sundaram K.G., Av-Gay Y.
Protein Expr. Purif. 58:309-317(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-48.
Strain: ATCC 25618 / H37Rv.
[4]"The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c."
Canova M.J., Veyron-Churlet R., Zanella-Cleon I., Cohen-Gonsaud M., Cozzone A.J., Becchi M., Kremer L., Molle V.
Proteomics 8:521-533(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, PHOSPHORYLATION AT THR-32; THR-62; THR-173; THR-175 AND THR-323, MUTAGENESIS OF LYS-48; SER-171; THR-173; SER-174 AND THR-175.
Strain: ATCC 25618 / H37Rv.
[5]"The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation."
Cohen-Gonsaud M., Barthe P., Canova M.J., Stagier-Simon C., Kremer L., Roumestand C., Molle V.
J. Biol. Chem. 284:19290-19300(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842579 Genomic DNA. Translation: CAA17480.1.
AE000516 Genomic DNA. Translation: AAK46517.1.
AL123456 Genomic DNA. Translation: CCP44953.1.
PIRB70936.
RefSeqNP_216692.1. NC_000962.3.
NP_336703.1. NC_002755.2.
YP_006515595.1. NC_018143.1.

3D structure databases

ProteinModelPortalO53510.
SMRO53510. Positions 15-363.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2176.

PTM databases

PhosSiteP0904619.

Proteomic databases

PRIDEO53510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46517; AAK46517; MT2232.
GeneID13318864.
888340.
924227.
KEGGmtc:MT2232.
mtu:Rv2176.
mtv:RVBD_2176.
PATRIC18126664. VBIMycTub22151_2444.

Organism-specific databases

TubercuListRv2176.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037187.
KOK08884.
OMARTIVENI.
ProtClustDBCLSK791676.

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 namePKNL_MYCTU
AccessionPrimary (citable) accession number: O53510
Secondary accession number(s): L0TAE8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 102 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

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