ID   J9W4U7_LENBU            Unreviewed;       221 AA.
AC   J9W4U7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124,
GN   ECO:0000313|EMBL:AFS00030.1};
GN   ORFNames=LBUCD034_0986 {ECO:0000313|EMBL:AFS00030.1};
OS   Lentilactobacillus buchneri subsp. silagei CD034.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus; Lentilactobacillus buchneri subsp. silagei.
OX   NCBI_TaxID=1071400 {ECO:0000313|EMBL:AFS00030.1, ECO:0000313|Proteomes:UP000007332};
RN   [1] {ECO:0000313|EMBL:AFS00030.1, ECO:0000313|Proteomes:UP000007332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD034 {ECO:0000313|EMBL:AFS00030.1,
RC   ECO:0000313|Proteomes:UP000007332};
RX   PubMed=22465289; DOI=10.1016/j.jbiotec.2012.03.007;
RA   Heinl S., Wibberg D., Eikmeyer F., Szczepanowski R., Blom J., Linke B.,
RA   Goesmann A., Grabherr R., Schwab H., Puhler A., Schluter A.;
RT   "Insights into the completely annotated genome of Lactobacillus buchneri
RT   CD034, a strain isolated from stable grass silage.";
RL   J. Biotechnol. 161:153-166(2012).
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:0000256|HAMAP-Rule:MF_00124,
CC         ECO:0000256|RuleBase:RU000544};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124,
CC       ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP003043; AFS00030.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9W4U7; -.
DR   STRING; 1071400.LBUCD034_0986; -.
DR   KEGG; lbn:LBUCD034_0986; -.
DR   PATRIC; fig|1071400.3.peg.940; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_2_2_9; -.
DR   Proteomes; UP000007332; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP-
KW   Rule:MF_00124};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Reference proteome {ECO:0000313|Proteomes:UP000007332};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE        117
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT                   ECO:0000256|PIRSR:PIRSR035805-1"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         116..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ   SEQUENCE   221 AA;  25829 MW;  1872649C9212D512 CRC64;
     MRVLANFLII IDFQNFFCIM EEKLLRKKVD ILAQLFYRYG AMNSGKTIEI IKVAHNYEEQ
     NKSVIIMTSA LDTREKQGMI ESRIGLERKA EPIREDTNVF DLVQELNPHA SCILIDEAQF
     LKKKHVMELA RIVDELNVPV MAFGLKNDFQ NNLFEGSKYL LLYADKIEEM KTICWFCGKK
     AIMNLRFHNG EPVYEGEQIQ MGGNESYYPV CRKHYYNPPI K
//