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Database: UniProt/SWISS-PROT
Entry: KITH_STRGC
LinkDB: KITH_STRGC
Original site: KITH_STRGC 
ID   KITH_STRGC              Reviewed;         191 AA.
AC   P47848; A8AXD2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   23-MAY-2018, entry version 102.
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=SGO_1155;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1
OS   / DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8598265; DOI=10.1111/j.1574-6968.1996.tb07973.x;
RA   McNab R.;
RT   "Cloning and sequence analysis of thymidine kinase from the oral
RT   bacterium Streptococcus gordonii.";
RL   FEMS Microbiol. Lett. 135:103-110(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in
RT   response to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {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; L40415; AAB02289.1; -; Genomic_DNA.
DR   EMBL; CP000725; ABV10749.1; -; Genomic_DNA.
DR   RefSeq; WP_008808654.1; NC_009785.1.
DR   ProteinModelPortal; P47848; -.
DR   SMR; P47848; -.
DR   STRING; 467705.SGO_1155; -.
DR   PRIDE; P47848; -.
DR   EnsemblBacteria; ABV10749; ABV10749; SGO_1155.
DR   GeneID; 25051793; -.
DR   KEGG; sgo:SGO_1155; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; POG091H0659; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
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; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    191       Thymidine kinase.
FT                                /FTId=PRO_0000175030.
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   191 AA;  21842 MW;  3F3EB8E3C5035283 CRC64;
     MAQLYYKYGT MNSGKTIEIL KVAHNYEEQG KGVVIMTSAV DTRDGVGYVS SRIGMKRQAM
     AIEDDTDILG YIKNLPEKPY CILIDEAQFL KRHHVYDLAR VVDELDVPVM AFGLKNDFRN
     ELFEGSKHLL LLADKIEEIK TICQYCSRKA TMVLRTDHGK PVYDGEQIQI GGNETYIPVC
     RKHYFKPDIN N
//
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