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Database: UniProt/SWISS-PROT
Entry: KITH_STAAB
LinkDB: KITH_STAAB
Original site: KITH_STAAB 
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   07-JUN-2017, entry version 77.
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; Firmicutes; 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
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; AJ938182; CAI81692.1; -; Genomic_DNA.
DR   RefSeq; WP_000273356.1; NC_007622.1.
DR   ProteinModelPortal; Q2YUN4; -.
DR   SMR; Q2YUN4; -.
DR   EnsemblBacteria; CAI81692; CAI81692; SAB2003c.
DR   GeneID; 31214852; -.
DR   KEGG; sab:SAB2003c; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
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; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 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       Thymidine kinase.
FT                                /FTId=PRO_0000242806.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      88     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       148    148       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {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
//
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