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Database: UniProt/TrEMBL
Entry: V5XS43_ENTMU
LinkDB: V5XS43_ENTMU
Original site: V5XS43_ENTMU 
ID   V5XS43_ENTMU            Unreviewed;       194 AA.
AC   V5XS43;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=tdk2 {ECO:0000313|EMBL:BAO07912.1};
GN   Synonyms=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN   ORFNames=EMQU_2355 {ECO:0000313|EMBL:BAO07912.1};
OS   Enterococcus mundtii QU 25.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1300150 {ECO:0000313|EMBL:BAO07912.1, ECO:0000313|Proteomes:UP000018580};
RN   [1] {ECO:0000313|Proteomes:UP000018580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QU25 {ECO:0000313|Proteomes:UP000018580};
RA   Shimizu-Kadota M., Shiwa Y., Sonomoto K., Yoshikawa H.;
RT   "Complete genome sequencing of Enterococcus mundtii QU25.";
RL   Submitted (MAR-2013) 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; AP013036; BAO07912.1; -; Genomic_DNA.
DR   RefSeq; WP_010736627.1; NC_022878.1.
DR   EnsemblBacteria; BAO07912; BAO07912; EMQU_2355.
DR   GeneID; 31548398; -.
DR   KEGG; emu:EMQU_2355; -.
DR   PATRIC; fig|1300150.4.peg.2334; -.
DR   KO; K00857; -.
DR   OrthoDB; POG091H0659; -.
DR   Proteomes; UP000018580; 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:UP000018580};
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:BAO07912.1};
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:UP000018580};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND       9     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND      85     88       ATP. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     86     86       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00124, ECO:0000256|PIRSR:PIRSR035805-
FT                                1}.
FT   METAL       143    143       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       180    180       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   194 AA;  22309 MW;  B720DD422DB044BC CRC64;
     MAQLFFKYGA MNSGKTIEIL KVAHNYEEQN KPVVLMTSGI DTRDGVGVVS SRIGLKREAI
     PIFETTDVFE VIQQMEHPPF CVLIDEAQFL TKEHVLAFTR IVDELNIPVM AFGLKNDFRN
     ELFEGSKYLL LYADKIEEMK TICWFCHKKA MMNLHYIDGT PVYEGDQVQI GGNEAYYPVC
     RKHYFHPLMI TEGD
//
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