KITH_BACAN
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 03-AUG-2022, entry version 128.
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; Firmicutes; 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; 260799.BAS5179; -.
DR DNASU; 1085264; -.
DR EnsemblBacteria; AAP29216; AAP29216; BA_5573.
DR EnsemblBacteria; AAT34716; AAT34716; GBAA_5573.
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; GWLELIC; -.
DR BioCyc; MetaCyc:MON-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; 3.40.50.300; -; 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; 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 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
