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Database: UniProt
Entry: Q8XFQ8
LinkDB: Q8XFQ8
Original site: Q8XFQ8 
ID   KITH_SALTI              Reviewed;         205 AA.
AC   Q8XFQ8; Q7AN37;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, 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=STY1301, t1661;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; AL513382; CAD08383.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69287.1; -; Genomic_DNA.
DR   RefSeq; NP_455750.1; NC_003198.1.
DR   RefSeq; WP_000068097.1; NZ_UFRG01000003.1.
DR   ProteinModelPortal; Q8XFQ8; -.
DR   SMR; Q8XFQ8; -.
DR   STRING; 220341.STY1301; -.
DR   EnsemblBacteria; AAO69287; AAO69287; t1661.
DR   EnsemblBacteria; CAD08383; CAD08383; CAD08383.
DR   GeneID; 1247702; -.
DR   KEGG; stt:t1661; -.
DR   KEGG; sty:STY1301; -.
DR   PATRIC; fig|220341.7.peg.1307; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   BRENDA; 2.7.1.21; 5557.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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   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; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    205       Thymidine kinase.
FT                                /FTId=PRO_0000175013.
FT   NP_BIND       9     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      87     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     88     88       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       182    182       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       185    185       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   205 AA;  23405 MW;  89F01D1D1D568DE9 CRC64;
     MAQLYFYYSA MNAGKSTALL QSSYNYQERG MRTVVYTAEI DDRFGAGKVS SRIGLSSPAK
     LFNQNTSLFE EIRAESARQT IHCVLVDESQ FLTRQQVYQL SEVVDKLDIP VLCYGLRTDF
     RGELFVGSQY LLAWSDKLVE LKTICFCGRK ASMVLRLDQD GRPYNEGEQV VIGGNERYVS
     VCRKHYKDAL EEGSLTAIQE RHRHI
//
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