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Database: UniProt
Entry: Q5M0B8
LinkDB: Q5M0B8
Original site: Q5M0B8 
ID   KITH_STRT1              Reviewed;         196 AA.
AC   Q5M0B8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 75.
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}; OrderedLocusNames=str0751;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D.,
RA   Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D.,
RA   Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J.,
RA   Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy
RT   bacterium Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV62344.1; -; Genomic_DNA.
DR   RefSeq; WP_011227082.1; NC_006449.1.
DR   ProteinModelPortal; Q5M0B8; -.
DR   SMR; Q5M0B8; -.
DR   EnsemblBacteria; AAV62344; AAV62344; str0751.
DR   GeneID; 31939072; -.
DR   KEGG; stc:str0751; -.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; STHE299768:G1G42-770-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    196       Thymidine kinase.
FT                                /FTId=PRO_0000175038.
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   196 AA;  22706 MW;  AC5F1F8CE55F43F5 CRC64;
     MAQLYFRYGT MNSGKSIEIL KVAYNYEEQG KPVVLLTSRL DDRDEVGYIS SRIGMRRKAY
     PIGNDTDIFD YIDDISPRPY CVLIDEAQFL TRANVYDLAR IVDELDIPVM AFGLKNDFQN
     NLFEGSKYLL LLSDKIEEIK TICHYCSRKA TMVLRMEDGE PVYEGVQVQI GGHESYISVC
     RKHWFNPPRE RIVPLK
//
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