ID KITH_STAAB Reviewed; 199 AA. AC Q2YUN4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; GN OrderedLocusNames=SAB2003c; OS Staphylococcus aureus (strain bovine RF122 / ET3-1). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=273036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bovine RF122 / ET3-1; RX PubMed=17971880; DOI=10.1371/journal.pone.0001120; RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.; RT "Molecular correlates of host specialization in Staphylococcus aureus."; RL PLoS ONE 2:E1120-E1120(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00124}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00124}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ938182; CAI81692.1; -; Genomic_DNA. DR RefSeq; WP_000273356.1; NC_007622.1. DR AlphaFoldDB; Q2YUN4; -. DR SMR; Q2YUN4; -. DR KEGG; sab:SAB2003c; -. DR HOGENOM; CLU_064400_3_0_9; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; THYMIDINE KINASE; 1. DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Transferase; Zinc. FT CHAIN 1..199 FT /note="Thymidine kinase" FT /id="PRO_0000242806" FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 15..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 88..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" SQ SEQUENCE 199 AA; 22214 MW; C1EC76B7C5645909 CRC64; MYETYHSGWI ECITGSMFSG KSEELIRRLR RGIYAKQKVV VFKPAIDDRY HKEKVVSHNG NAIEAINISK ASEIMTHDLT NVDVIGIDEV QFFDDEIVSI VEKLSADGHR VIVAGLDMDF RGEPFEPMPK LMAVSEQVTK LQAVCAVCGS SSSRTQRLIN GKPAKIDDPI ILVGANESYE PRCRAHHIVA PSDNNKEEL //