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Database: UniProt/SWISS-PROT
Entry: KITH_STRA3
LinkDB: KITH_STRA3
Original site: KITH_STRA3 
ID   KITH_STRA3              Reviewed;         189 AA.
AC   Q8E5C2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 100.
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=gbs1110;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC         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. {ECO:0000255|HAMAP-
CC       Rule:MF_00124}.
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DR   EMBL; AL766848; CAD46769.1; -; Genomic_DNA.
DR   RefSeq; WP_000068109.1; NC_004368.1.
DR   AlphaFoldDB; Q8E5C2; -.
DR   SMR; Q8E5C2; -.
DR   GeneID; 66886004; -.
DR   KEGG; san:gbs1110; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_2_2_9; -.
DR   OMA; GTMDCGK; -.
DR   Proteomes; UP000000823; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175026"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         85..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
SQ   SEQUENCE   189 AA;  21593 MW;  38BAAF6B62940D4A CRC64;
     MAQLYYKYGT MNSGKTIEIL KVAHNYEEQG KPVVIMTSAL DTRDEFGVVS SRIGMRREAV
     PISDDMDIFS YIQNLPQKPY CVLIDECQFL SKKNVYDLAR VVDDLDVPVM AFGLKNDFQN
     NLFEGSKHLL LLADKIDEIK TICQYCSKKA TMVLRTENGK PVYEGDQIQI GGNETYIPVC
     RKHYFNPDI
//
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