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Q03221 (KITH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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:BSU37060
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00124

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 termComplete 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 – 195195Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174963

Regions

Nucleotide binding15 – 228ATP By similarity
Nucleotide binding88 – 914ATP By similarity

Sites

Active site891Proton acceptor Potential
Metal binding1451Zinc By similarity
Metal binding1481Zinc By similarity
Metal binding1831Zinc By similarity
Metal binding1861Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03221 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 1F4EFE266714249F

FASTA19521,450
        10         20         30         40         50         60 
MYIMKQSGWL ELICGSMFSG KSEELIRRVK RATYAKQEVR VFKPVIDNRY SEAAVVSHNG 

        70         80         90        100        110        120 
TSMTSYAISS AADIWDHISE STDVVAVDEV QFFDQEIVEV LSSLADKGYR VIAAGLDMDF 

       130        140        150        160        170        180 
RGEPFGVVPN IMAIAESVTK LQAVCSVCGS PASRTQRLID GKPASYDDPV ILVGAAESYE 

       190 
ARCRHHHEVP GKSKK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a putative Bacillus subtilis rho gene."
Quirk P.G., Dunkley E.A. Jr., Lee P., Krulwich T.A.
J. Bacteriol. 175:647-654(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BD99 / MS119.
[2]Quirk P.G.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97678 Unassigned DNA. Translation: AAA02902.1.
Z49782 Genomic DNA. Translation: CAA89879.1.
AL009126 Genomic DNA. Translation: CAB15723.1.
PIRS55432.
RefSeqNP_391587.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ03221.
SMRQ03221. Positions 1-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU37060.

Proteomic databases

PaxDbQ03221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15723; CAB15723; BSU37060.
GeneID937033.
KEGGbsu:BSU37060.
PATRIC18979446. VBIBacSub10457_3885.

Organism-specific databases

GenoListBSU37060. [Micado]

Phylogenomic databases

eggNOGCOG1435.
HOGENOMHOG000076390.
KOK00857.
OMADHISEST.
OrthoDBEOG69D3J2.
PhylomeDBQ03221.

Enzyme and pathway databases

BioCycBSUB:BSU37060-MONOMER.

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...

Entry information

Entry nameKITH_BACSU
AccessionPrimary (citable) accession number: Q03221
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 103 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList