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Database: UniProt/TrEMBL
Entry: A0A143HGM2_9BACL
LinkDB: A0A143HGM2_9BACL
Original site: A0A143HGM2_9BACL 
ID   A0A143HGM2_9BACL        Unreviewed;       197 AA.
AC   A0A143HGM2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Thymidine kinase {ECO:0000256|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU000544};
GN   Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN   ORFNames=ATY39_16785 {ECO:0000313|EMBL:AMX00888.1};
OS   Rummeliibacillus stabekisii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Rummeliibacillus.
OX   NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00888.1, ECO:0000313|Proteomes:UP000076021};
RN   [1] {ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {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|HAMAP-Rule:MF_00124, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP014806; AMX00888.1; -; Genomic_DNA.
DR   RefSeq; WP_066791731.1; NZ_CP014806.1.
DR   KEGG; rst:ATY39_16785; -.
DR   KO; K00857; -.
DR   Proteomes; UP000076021; 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   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 {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076021};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW   DNA synthesis {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544, ECO:0000313|EMBL:AMX00888.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076021};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND      15     22       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND      88     91       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00124, ECO:0000256|PIRSR:PIRSR035805-
FT                                1}.
FT   METAL       145    145       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       148    148       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   197 AA;  21751 MW;  91D4E8C375054953 CRC64;
     MYVMTQNGWI EVICGSMFSG KSEELIRRVR RAQFAKQKIV VFKPKIDNRY SEEAVVSHNG
     TTVIAYPISQ STDMWGYLSD DVDVVAIDEA QFFGEDIIAT VQQLANHGYR VILAGLDQDF
     KGVPFGPMPQ LMAIAEQVTK LQAVCSVCGS PASRTQRLIN GQPAKADDPV ILVGAAEAYE
     PRCRHHHVVP ASQTQVK
//
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