ID   KITH_MYCPE              Reviewed;         220 AA.
AC   Q8EU99;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   07-JAN-2015, entry version 69.
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=MYPE10320;
OS   Mycoplasma penetrans (strain HF-2).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an
RT   intracellular bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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}.
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DR   EMBL; BA000026; BAC44817.1; -; Genomic_DNA.
DR   RefSeq; NP_758413.1; NC_004432.1.
DR   ProteinModelPortal; Q8EU99; -.
DR   STRING; 272633.MYPE10320; -.
DR   EnsemblBacteria; BAC44817; BAC44817; BAC44817.
DR   GeneID; 1041069; -.
DR   KEGG; mpe:MYPE10320; -.
DR   PATRIC; 20021252; VBIMycPen56664_1056.
DR   eggNOG; COG1435; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; VITGPMY; -.
DR   OrthoDB; EOG69D3J2; -.
DR   BioCyc; MPEN272633:GJBP-1059-MONOMER; -.
DR   Proteomes; UP000002522; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
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   InterPro; IPR020634; Thymidine_kinase_subgr.
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; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    220       Thymidine kinase.
FT                                /FTId=PRO_0000174998.
FT   NP_BIND      18     25       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      93     96       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     94     94       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       150    150       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       153    153       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       188    188       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       191    191       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   220 AA;  25184 MW;  47CFA4901E74737F CRC64;
     MKNNAFGKEK GWIELIYGPM FAGKSEELLR KLKRLDYADV IYQVFKPKID TRTKNKIMSR
     DGRNMDSFEF DNPYEIFDKL LSLEVNPHVV AIDEAQFADE SIVDVCQALA DSGYIVYVSA
     LDKNFKNEPF MVTAKIACIA EYVEKLSAIC TDCGAPGTAT QRIINDKPSN YDEPVVQIGN
     YETYTVKCRH HHKIPGKPFP EEIKKFKSDL RNLLKNKENK
//