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Q81JX0 (KITH_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine kinase

EC=2.7.1.21
Gene names
Name:tdk
Ordered Locus Names:BA_5573, GBAA_5573, BAS5179
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. HAMAP-Rule MF_00124

Subunit structure

Homotetramer. Ref.4

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00124.

Sequence similarities

Belongs to the thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thymidine kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174953

Regions

Nucleotide binding15 – 228ATP By similarity
Nucleotide binding88 – 914ATP By similarity
Region170 – 1745Substrate binding HAMAP-Rule MF_00124

Sites

Active site891Proton acceptor Potential
Metal binding1451Zinc
Metal binding1481Zinc
Metal binding1831Zinc
Metal binding1861Zinc
Binding site1201Substrate; via amide nitrogen
Binding site1791Substrate By similarity

Secondary structure

................................. 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81JX0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D2A9B182355D9D13

FASTA19421,642
        10         20         30         40         50         60 
MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG 

        70         80         90        100        110        120 
LKVKAVPVSA SKDIFKHITE EMDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF 

       130        140        150        160        170        180 
RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS PASRTQRLID GEPAAFDDPI ILVGASESYE 

       190 
PRCRHCHAVP TKQR 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[4]"Structural studies of thymidine kinases from Bacillus anthracis and Bacillus cereus provide insights into quaternary structure and conformational changes upon substrate binding."
Kosinska U., Carnrot C., Sandrini M.P., Clausen A.R., Wang L., Piskur J., Eriksson S., Eklund H.
FEBS J. 274:727-737(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND DEOXYTHYMIDINE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP29216.1.
AE017334 Genomic DNA. Translation: AAT34716.1.
AE017225 Genomic DNA. Translation: AAT57468.1.
RefSeqNP_847730.1. NC_003997.3.
YP_022241.1. NC_007530.2.
YP_031418.1. NC_005945.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J9RX-ray2.70A1-194[»]
ProteinModelPortalQ81JX0.
SMRQ81JX0. Positions 1-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ81JX0. 5 interactions.
STRING198094.BA_5573.

Protocols and materials databases

DNASU1085264.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP29216; AAP29216; BA_5573.
AAT34716; AAT34716; GBAA_5573.
AAT57468; AAT57468; BAS5179.
GeneID1085264.
2819897.
2851937.
KEGGban:BA_5573.
bar:GBAA_5573.
bat:BAS5179.

Phylogenomic databases

eggNOGCOG1435.
HOGENOMHOG000076390.
KOK00857.
OMAQAICLSC.
OrthoDBEOG69D3J2.

Enzyme and pathway databases

BioCycANTHRA:TDK-MONOMER.
BANT260799:GJAJ-5254-MONOMER.
BANT261594:GJ7F-5433-MONOMER.
MetaCyc:MONOMER-17898.

Family and domain databases

HAMAPMF_00124. Thymidine_kinase.
InterProIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[Graphical view]
PANTHERPTHR11441. PTHR11441. 1 hit.
PfamPF00265. TK. 1 hit.
[Graphical view]
PIRSFPIRSF035805. TK_cell. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ81JX0.

Entry information

Entry nameKITH_BACAN
AccessionPrimary (citable) accession number: Q81JX0
Secondary accession number(s): Q6HQH0, Q6KJU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 83 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references