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Q814U0 (KITH_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thymidine kinase
EC=2.7.1.21
Gene names
Name:tdk
Ordered Locus Names:BC_5330
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length195 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.2

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: HAMAP

thymidine kinase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174955

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

Sequences

Sequence LengthMass (Da)Tools
Q814U0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 937F6D890890302E

FASTA19521,696
        10         20         30         40         50         60 
MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG 

        70         80         90        100        110        120 
LKVKAVPVSA SKDIFEHITE ELDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF 

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

       190 
PRCRHCHAVP ANKDK

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.
[2]"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 (2.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TTP, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016877 Genomic DNA. Translation: AAP12193.1.
RefSeqNP_834992.1. NC_004722.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA1X-ray2.80A1-195[»]
ProteinModelPortalQ814U0.
SMRQ814U0. Positions 1-191.
ModBaseSearch...

Protein-protein interaction databases

STRING226900.BC5330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP12193; AAP12193; BC_5330.
GeneID1207670.
KEGGbce:BC5330.
PATRIC32606864. VBIBacCer54481_5503.

Phylogenomic databases

eggNOGCOG1435.
KOK00857.
OMAKVHAICV.
ProtClustDBPRK04296.

Enzyme and pathway databases

BioCycBCER226900:GJEU-5322-MONOMER.

Family and domain databases

HAMAPMF_00124. Thymidine_kinase.
InterProIPR001267. 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.
PROSITEPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ814U0.

Entry information

Entry nameKITH_BACCR
AccessionPrimary (citable) accession number: Q814U0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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