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Database: UniProt/SWISS-PROT
Entry: KITH_BACSK
LinkDB: KITH_BACSK
Original site: KITH_BACSK 
ID   KITH_BACSK              Reviewed;         192 AA.
AC   Q5WB52;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   07-JUN-2017, entry version 74.
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}; OrderedLocusNames=ABC3877;
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD66408.1; -; Genomic_DNA.
DR   RefSeq; WP_011248711.1; NC_006582.1.
DR   ProteinModelPortal; Q5WB52; -.
DR   SMR; Q5WB52; -.
DR   STRING; 66692.ABC3877; -.
DR   EnsemblBacteria; BAD66408; BAD66408; ABC3877.
DR   KEGG; bcl:ABC3877; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; POG091H0659; -.
DR   Proteomes; UP000001168; Chromosome.
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; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    192       Thymidine kinase.
FT                                /FTId=PRO_0000174962.
FT   NP_BIND       9     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      85     88       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     86     86       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       143    143       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       181    181       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       184    184       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   192 AA;  22179 MW;  79E1F963B3AFC378 CRC64;
     MAQLFFKYGA MNSGKSIEIL KVANNYEEQK KPVLIFTSGM DTRDEVGYVS SRVGLRRRAV
     PIFDDTNIFD YVESCRQKPY CVLIDEVQFL TKAHVLQLAN IVDTLDIPVM GFGLKNDFRN
     ELFEGSKYML LYADKIEEMK TICWFCHKKA IMNLRVDEQG KPIYDGEQIQ IGGNETYYPV
     CRKCHQHPPL TV
//
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