ID   KITH_BACNA              Reviewed;         195 AA.
AC   O52951;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-MAY-2023, entry version 86.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=tdk;
OS   Bacillus subtilis subsp. natto.
OG   Plasmid pLS32.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM 1163;
RX   PubMed=9490016; DOI=10.1016/s0014-5793(98)00015-5;
RA   Tanaka T., Ogura M.;
RT   "A novel Bacillus natto plasmid pLS32 capable of replication in Bacillus
RT   subtilis.";
RL   FEBS Lett. 422:243-246(1998).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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; D49467; BAA24875.1; -; Genomic_DNA.
DR   RefSeq; WP_013603338.1; NC_015149.1.
DR   RefSeq; YP_004243650.1; NC_015149.1.
DR   AlphaFoldDB; O52951; -.
DR   SMR; O52951; -.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Plasmid; Transferase; Zinc.
FT   CHAIN           1..195
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175057"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   195 AA;  22221 MW;  1ABFA791B1A56B23 CRC64;
     MDITFNTGLM GSGKSKKLID DYLIDPKEKV ALSVSLTEDT FSRGKIESRD GRSLRSINLN
     RDQFKQNISL LEIIIFMTNT QTIYIDESQF LPKETVEKFV SLSESYHVPI HFYGLDLTFT
     GELFDSSSHL LTILPSENIN RISRGCEASK CSKIAQYNAR IVDGKVSRSG ETFVEEKSYY
     LALCSDHYYN DEKII
//