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Q0H0G9 (Q0H0G9_STAAU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Thymidine kinase RuleBase RU000544 HAMAP-Rule MF_00124

EC=2.7.1.21 RuleBase RU000544 HAMAP-Rule MF_00124
Gene names
Name:tdk HAMAP-Rule MF_00124 EMBL ABD37699.1
ORF Names:X998_2098 EMBL AHW68308.1
OrganismStaphylococcus aureus EMBL ABD37699.1
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. SAAS SAAS020634 RuleBase RU000544 HAMAP-Rule MF_00124

Subunit structure

Homotetramer By similarity. SAAS SAAS020634 HAMAP-Rule MF_00124

Subcellular location

Cytoplasm By similarity SAAS SAAS020634 HAMAP-Rule MF_00124.

Sequence similarities

Belongs to the thymidine kinase family. RuleBase RU004165 HAMAP-Rule MF_00124

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding15 – 228ATP By similarity HAMAP-Rule MF_00124
Nucleotide binding88 – 914ATP By similarity HAMAP-Rule MF_00124

Sites

Active site891Proton acceptor By similarity HAMAP-Rule MF_00124
Metal binding1451Zinc PDB 3E2I
Metal binding1451Zinc By similarity HAMAP-Rule MF_00124
Metal binding1481Zinc PDB 3E2I
Metal binding1481Zinc By similarity HAMAP-Rule MF_00124
Metal binding1831Zinc PDB 3E2I
Metal binding1831Zinc By similarity HAMAP-Rule MF_00124
Metal binding1861Zinc By similarity HAMAP-Rule MF_00124
Metal binding1861Zinc; via pros nitrogen PDB 3E2I

Sequences

Sequence LengthMass (Da)Tools
Q0H0G9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C1EC76B7C5645909

FASTA19922,214
        10         20         30         40         50         60 
MYETYHSGWI ECITGSMFSG KSEELIRRLR RGIYAKQKVV VFKPAIDDRY HKEKVVSHNG 

        70         80         90        100        110        120 
NAIEAINISK ASEIMTHDLT NVDVIGIDEV QFFDDEIVSI VEKLSADGHR VIVAGLDMDF 

       130        140        150        160        170        180 
RGEPFEPMPK LMAVSEQVTK LQAVCAVCGS SSSRTQRLIN GKPAKIDDPI ILVGANESYE 

       190 
PRCRAHHIVA PSDNNKEEL 

« Hide

References

[1]"Bacterial deoxyribonucleoside kinases."
Sandrini M.P.B., Clausen A.R., Piskur J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DVI CCM 885 EMBL ABD37699.1.
[2]"Deoxyribonucleoside kinases activate nucleoside antibiotics in severely pathogenic bacteria."
Sandrini M.P., Shannon O., Clausen A.R., Bjorck L., Piskur J.
Antimicrob. Agents Chemother. 51:2726-2732(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DVI CCM 885 EMBL ABD37699.1.
[3]"Nucleoside analogues are activated by bacterial deoxyribonucleoside kinases in a species-specific manner."
Sandrini M.P., Clausen A.R., On S.L., Aarestrup F.M., Munch-Petersen B., Piskur J.
J. Antimicrob. Chemother. 60:510-520(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DVI CCM 885 EMBL ABD37699.1.
[4]"Crystal structure of Thymidine Kinase from S. aureus."
Lam R., Johns K., Battaile K.P., Romanov V., Lam K., Pai E.F., Chirgadze N.Y.
Submitted (AUG-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH ZINC.
[5]"Genome sequence of Staphylococcus aureus NRS 100."
Sichtig H., Utter B., Tallon L.J., Deshong S.Lisa., Sengamalay N., Nagaraj S., McCracken C.L., Daugherty S.
Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NRS 100 EMBL AHW68308.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ384605 Genomic DNA. Translation: ABD37699.1.
CP007539 Genomic DNA. Translation: AHW68308.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E2IX-ray2.01A1-199[»]
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ0H0G9.
ChEMBLCHEMBL5323.

Proteomic databases

PRIDEQ0H0G9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceQ0H0G9.

Entry information

Entry nameQ0H0G9_STAAU
AccessionPrimary (citable) accession number: Q0H0G9
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)