ID   KITH_BACAN              Reviewed;         194 AA.
AC   Q81JX0; Q6HQH0; Q6KJU4;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 133.
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=BA_5573, GBAA_5573, BAS5179;
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   DEOXYTHYMIDINE, AND SUBUNIT.
RX   PubMed=17288553; DOI=10.1111/j.1742-4658.2006.05617.x;
RA   Kosinska U., Carnrot C., Sandrini M.P., Clausen A.R., Wang L., Piskur J.,
RA   Eriksson S., Eklund H.;
RT   "Structural studies of thymidine kinases from Bacillus anthracis and
RT   Bacillus cereus provide insights into quaternary structure and
RT   conformational changes upon substrate binding.";
RL   FEBS J. 274:727-737(2007).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00124};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124,
CC       ECO:0000269|PubMed:17288553}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00124}.
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DR   EMBL; AE016879; AAP29216.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT34716.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT57468.1; -; Genomic_DNA.
DR   RefSeq; NP_847730.1; NC_003997.3.
DR   RefSeq; WP_000280866.1; NZ_WXXJ01000038.1.
DR   RefSeq; YP_031418.1; NC_005945.1.
DR   PDB; 2J9R; X-ray; 2.70 A; A=1-194.
DR   PDBsum; 2J9R; -.
DR   AlphaFoldDB; Q81JX0; -.
DR   SMR; Q81JX0; -.
DR   IntAct; Q81JX0; 5.
DR   STRING; 261594.GBAA_5573; -.
DR   DNASU; 1085264; -.
DR   GeneID; 45025160; -.
DR   KEGG; ban:BA_5573; -.
DR   KEGG; bar:GBAA_5573; -.
DR   KEGG; bat:BAS5179; -.
DR   PATRIC; fig|198094.11.peg.5532; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_0_9; -.
DR   OMA; EAYEPRC; -.
DR   OrthoDB; 9781579at2; -.
DR   BioCyc; MetaCyc:MONOMER-17898; -.
DR   EvolutionaryTrace; Q81JX0; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..194
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000174953"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         88..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         120
FT                   /ligand="substrate"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         170..174
FT                   /ligand="substrate"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   HELIX           21..34
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   HELIX           97..106
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   HELIX           128..134
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          154..159
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   STRAND          179..182
FT                   /evidence="ECO:0007829|PDB:2J9R"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:2J9R"
SQ   SEQUENCE   194 AA;  21642 MW;  D2A9B182355D9D13 CRC64;
     MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG
     LKVKAVPVSA SKDIFKHITE EMDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF
     RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS PASRTQRLID GEPAAFDDPI ILVGASESYE
     PRCRHCHAVP TKQR
//