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Database: UniProt
Entry: A0A2A5S9Y1_9LACT
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ID   A0A2A5S9Y1_9LACT        Unreviewed;       189 AA.
AC   A0A2A5S9Y1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ORFNames=D9N18_09485 {ECO:0000313|EMBL:MBW9331584.1}, GU335_01855
GN   {ECO:0000313|EMBL:QIW55425.1};
OS   Lactococcus raffinolactis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1366 {ECO:0000313|EMBL:MBW9331584.1, ECO:0000313|Proteomes:UP000709450};
RN   [1] {ECO:0000313|EMBL:MBW9331584.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3042 {ECO:0000313|EMBL:MBW9331584.1};
RA   Meslier V., Dridi B., Almeida M., Abraham A.-L., Pons N., Renault P.;
RT   "Lactococcus raffinolactis, an underestimated dairy Lactococci revealed by
RT   genomic and metagenomic analysis.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QIW55425.1, ECO:0000313|Proteomes:UP000501197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lr_19_4S {ECO:0000313|EMBL:QIW55425.1,
RC   ECO:0000313|Proteomes:UP000501197};
RA   Ybazeta G., Ross M., Brabant-Kirwan D., Saleh M., Dillon J.A., Splinter K.,
RA   Nokhbeh R.;
RT   "Whole genome sequences of Lactococcus raffinolactis strains isolated from
RT   sewage.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; RCHZ01000016; MBW9331584.1; -; Genomic_DNA.
DR   EMBL; CP050534; QIW55425.1; -; Genomic_DNA.
DR   RefSeq; WP_061775030.1; NZ_VBTC01000019.1.
DR   STRING; 1348633.GCA_001591765_01547; -.
DR   GeneID; 47267395; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000501197; Chromosome.
DR   Proteomes; UP000709450; Unassembled WGS sequence.
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT                   ECO:0000256|PIRSR:PIRSR035805-1"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         85..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ   SEQUENCE   189 AA;  21599 MW;  5C7E54EE08FDC963 CRC64;
     MAKLYFKYGT MNSGKSIEIL KVAHNYEEQG KPVVIMTSAL DNRDEIGVVS SRIGMREQAV
     PIDAALNVFD YVAKLPEKPY CILIDEAQFL SKKNIYDFAR VVDELNVPVM AFGLKNDFQN
     ELFEGSKYLL LLADKIEEIK TICWFCSKKA TMVLRTENNQ PVYEGSQIQI GGNESYLPVC
     RKHWFKPEL
//
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