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}.
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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
//
