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Database: UniProt
Entry: Q81JX0
LinkDB: Q81JX0
Original site: Q81JX0 
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   13-FEB-2019, entry version 113.
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.,
RA   Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D.,
RA   Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F.,
RA   Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C.,
RA   Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O.,
RA   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
RT   closely 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.,
RA   Piskur J., 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(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
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_QPKQ01000006.1.
DR   RefSeq; YP_031418.1; NC_005945.1.
DR   PDB; 2J9R; X-ray; 2.70 A; A=1-194.
DR   PDBsum; 2J9R; -.
DR   ProteinModelPortal; 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   EnsemblBacteria; AAT57468; AAT57468; BAS5179.
DR   GeneID; 1085264; -.
DR   GeneID; 2851937; -.
DR   KEGG; ban:BA_5573; -.
DR   KEGG; bar:GBAA_5573; -.
DR   KEGG; bat:BAS5179; -.
DR   PATRIC; fig|198094.11.peg.5532; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   BioCyc; ANTHRA:TDK-MONOMER; -.
DR   BioCyc; BANT260799:BAS5179-MONOMER; -.
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   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; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    194       Thymidine kinase.
FT                                /FTId=PRO_0000174953.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      88     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   REGION      170    174       Substrate binding.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc.
FT   METAL       148    148       Zinc.
FT   METAL       183    183       Zinc.
FT   METAL       186    186       Zinc.
FT   BINDING     120    120       Substrate; via amide nitrogen.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
FT   STRAND        9     14       {ECO:0000244|PDB:2J9R}.
FT   HELIX        21     34       {ECO:0000244|PDB:2J9R}.
FT   STRAND       39     43       {ECO:0000244|PDB:2J9R}.
FT   STRAND       65     67       {ECO:0000244|PDB:2J9R}.
FT   HELIX        71     77       {ECO:0000244|PDB:2J9R}.
FT   STRAND       84     87       {ECO:0000244|PDB:2J9R}.
FT   HELIX        90     92       {ECO:0000244|PDB:2J9R}.
FT   HELIX        97    106       {ECO:0000244|PDB:2J9R}.
FT   STRAND      110    115       {ECO:0000244|PDB:2J9R}.
FT   HELIX       128    134       {ECO:0000244|PDB:2J9R}.
FT   STRAND      136    140       {ECO:0000244|PDB:2J9R}.
FT   TURN        146    148       {ECO:0000244|PDB:2J9R}.
FT   STRAND      149    151       {ECO:0000244|PDB:2J9R}.
FT   STRAND      154    159       {ECO:0000244|PDB:2J9R}.
FT   TURN        176    178       {ECO:0000244|PDB:2J9R}.
FT   STRAND      179    182       {ECO:0000244|PDB:2J9R}.
FT   TURN        184    186       {ECO:0000244|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
//
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