ID A0A0D6A4R4_9LACO Unreviewed; 199 AA.
AC A0A0D6A4R4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=GJR85_02935 {ECO:0000313|EMBL:QGV04424.1}, LA749_05410
GN {ECO:0000313|EMBL:QFG51464.1}, LBAT_1066
GN {ECO:0000313|EMBL:BAQ57455.1};
OS Lactobacillus acetotolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ57455.1, ECO:0000313|Proteomes:UP000035709};
RN [1] {ECO:0000313|EMBL:BAQ57455.1, ECO:0000313|Proteomes:UP000035709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ57455.1,
RC ECO:0000313|Proteomes:UP000035709};
RA Toh H., Morita H., Fujita N.;
RT "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QFG51464.1, ECO:0000313|Proteomes:UP000325393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LA749 {ECO:0000313|EMBL:QFG51464.1,
RC ECO:0000313|Proteomes:UP000325393};
RA Kim K.;
RT "Genome sequencing of Lactobacillus acetotolerans.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QGV04424.1, ECO:0000313|Proteomes:UP000427729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN247 {ECO:0000313|EMBL:QGV04424.1,
RC ECO:0000313|Proteomes:UP000427729};
RA Luan C.;
RT "Complete genome sequence and characteristic analysis of beer-spoilage
RT bacterium Lactobacillus acetotolerans cn247.";
RL Submitted (DEC-2019) 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; AP014808; BAQ57455.1; -; Genomic_DNA.
DR EMBL; CP044496; QFG51464.1; -; Genomic_DNA.
DR EMBL; CP046528; QGV04424.1; -; Genomic_DNA.
DR RefSeq; WP_056970386.1; NZ_WNWN01000021.1.
DR STRING; 1600.LBAT_1066; -.
DR GeneID; 78212422; -.
DR KEGG; lae:LBAT_1066; -.
DR PATRIC; fig|1600.4.peg.1090; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000035709; Chromosome.
DR Proteomes; UP000325393; Chromosome.
DR Proteomes; UP000427729; 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:UP000035709};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT ACT_SITE 94
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 93..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ SEQUENCE 199 AA; 22605 MW; 497753CD7625BE19 CRC64;
MAQLFFRYGA MSSGKTIEIL KVAHNYEAQG RKIALMTSGI DNRNGVGTVA SRIGLHRKAI
PVDAKLNLFD YISNKNKKDE AEGNGKLVCV LIDEAQFLKK HHVLECARIV DDLKIPVMTF
GLKNDFQNHL FEGSENLLIY ADKIEEMKTI CHFCGHKATM NLRINNKQPV YEGEQVQIGG
DESYYPVCRF HYFHPGQNR
//