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Database: UniProt
Entry: Q8P126
LinkDB: Q8P126
Original site: Q8P126 
ID   KITH_STRP8              Reviewed;         189 AA.
AC   Q8P126;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=spyM18_1100;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA   Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA   Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18
RT   group A Streptococcus strains associated with acute rheumatic fever
RT   outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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   -!- 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; AE009949; AAL97722.1; -; Genomic_DNA.
DR   RefSeq; WP_002989802.1; NC_003485.1.
DR   ProteinModelPortal; Q8P126; -.
DR   SMR; Q8P126; -.
DR   EnsemblBacteria; AAL97722; AAL97722; spyM18_1100.
DR   KEGG; spm:spyM18_1100; -.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; SPYO186103:G1FZQ-979-MONOMER; -.
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   ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    189       Thymidine kinase.
FT                                /FTId=PRO_0000175037.
FT   NP_BIND       9     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      85     88       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     86     86       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       143    143       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       180    180       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   189 AA;  21547 MW;  BF895E3F609B821E CRC64;
     MAQLYYKYGT MNSGKTIEIL KVAHNYEEQG KPVVIMTSAL DTRDGFGIVS SRIGMRREAI
     PISNDMDIFT FIAQLEEKPY CVLIDESQFL SKQNVYDLAR VVDELNVPVM AFGLKNDFQN
     NLFEGSKHLL LLADKIDEIK TICQYCSKKA TMVLRTENGK PVYEGDQIQI GGNETYIPVC
     RKHYFNPEI
//
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