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Database: UniProt
Entry: P0A3L9
LinkDB: P0A3L9
Original site: P0A3L9 
ID   KITH_ECO57              Reviewed;         205 AA.
AC   P0A3L9; Q9S5G7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   13-FEB-2019, entry version 86.
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=Z2015, ECs1740;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O157:H- / 184 / EHEC;
RX   PubMed=10222209; DOI=10.1006/mpat.1998.0253;
RA   Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
RT   "Analysis of the genes responsible for the O-antigen synthesis in
RT   enterohaemorrhagic Escherichia coli O157.";
RL   Microb. Pathog. 26:235-247(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Phosphorylates both thymidine and deoxyuridine.
CC       {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Allosteric enzyme which is feedback inhibited
CC       by dTTP and activated by a number of dNDP and dNTP. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
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; AB008676; BAA77748.1; -; Genomic_DNA.
DR   EMBL; AE005174; AAG56095.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35163.1; -; Genomic_DNA.
DR   PIR; C85704; C85704.
DR   PIR; D90846; D90846.
DR   RefSeq; NP_309767.1; NC_002695.1.
DR   RefSeq; WP_000068079.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; P0A3L9; -.
DR   STRING; 155864.Z2015; -.
DR   PRIDE; P0A3L9; -.
DR   EnsemblBacteria; AAG56095; AAG56095; Z2015.
DR   EnsemblBacteria; BAB35163; BAB35163; BAB35163.
DR   GeneID; 913112; -.
DR   KEGG; ece:Z2015; -.
DR   KEGG; ecs:ECs1740; -.
DR   PATRIC; fig|386585.9.peg.1841; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   BioCyc; ECOO157:TDK-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    205       Thymidine kinase.
FT                                /FTId=PRO_0000174973.
FT   NP_BIND       9     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      87     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     88     88       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       182    182       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       185    185       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   205 AA;  23399 MW;  533166D9E91D0E16 CRC64;
     MAQLYFYYSA MNAGKSTALL QSSYNYQERG MRTVVYTAEI DDRFGAGKVS SRIGLSSPAK
     LFNQNSSLFD EIRAEHEQQA IHCVLVDECQ FLTRQQVYEL SEVVDQLDIP VLCYGLRTDF
     RGELFIGSQY LLAWSDKLVE LKTICFCGRK ASMVLRLDQA GRPYNEGEQV VIGGNERYVS
     VCRKHYKEAL QVGSLTAIQE RHRHD
//
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