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P0A3L9 (KITH_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:Z2015, ECs1740
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Phosphorylates both thymidine and deoxyuridine By similarity. HAMAP-Rule MF_00124

Catalytic activity

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

Enzyme regulation

Allosteric enzyme which is feedback inhibited by dTTP and activated by a number of dNDP and dNTP By similarity. 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 termAllosteric enzyme
Complete 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 – 205205Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174973

Regions

Nucleotide binding9 – 168ATP By similarity
Nucleotide binding87 – 904ATP By similarity

Sites

Active site881Proton acceptor Potential
Metal binding1451Zinc By similarity
Metal binding1471Zinc By similarity
Metal binding1821Zinc By similarity
Metal binding1851Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A3L9 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 533166D9E91D0E16

FASTA20523,399
        10         20         30         40         50         60 
MAQLYFYYSA MNAGKSTALL QSSYNYQERG MRTVVYTAEI DDRFGAGKVS SRIGLSSPAK 

        70         80         90        100        110        120 
LFNQNSSLFD EIRAEHEQQA IHCVLVDECQ FLTRQQVYEL SEVVDQLDIP VLCYGLRTDF 

       130        140        150        160        170        180 
RGELFIGSQY LLAWSDKLVE LKTICFCGRK ASMVLRLDQA GRPYNEGEQV VIGGNERYVS 

       190        200 
VCRKHYKEAL QVGSLTAIQE RHRHD 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157."
Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.
Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O157:H- / 184 / EHEC.
[2]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008676 Genomic DNA. Translation: BAA77748.1.
AE005174 Genomic DNA. Translation: AAG56095.1.
BA000007 Genomic DNA. Translation: BAB35163.1.
PIRC85704.
D90846.
RefSeqNP_287483.1. NC_002655.2.
NP_309767.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A3L9.
SMRP0A3L9. Positions 1-189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56095; AAG56095; Z2015.
BAB35163; BAB35163; BAB35163.
GeneID913112.
960490.
KEGGece:Z2015.
ecs:ECs1740.
PATRIC18352744. VBIEscCol44059_1595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1435.
HOGENOMHOG000076391.
KOK00857.
OMARTICHCG.
OrthoDBEOG69D3J2.
ProtClustDBPRK04296.

Enzyme and pathway databases

BioCycECOL386585:GJFA-1724-MONOMER.
ECOO157:TDK-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_ECO57
AccessionPrimary (citable) accession number: P0A3L9
Secondary accession number(s): Q9S5G7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: April 16, 2014
This is version 55 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