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Database: UniProt/TrEMBL
Entry: F8DML2_LACRS
LinkDB: F8DML2_LACRS
Original site: F8DML2_LACRS 
ID   F8DML2_LACRS            Unreviewed;       191 AA.
AC   F8DML2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-SEP-2017, entry version 35.
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   ECO:0000313|EMBL:AEI57880.1};
GN   OrderedLocusNames=HMPREF0538_21671 {ECO:0000313|EMBL:AEI57880.1};
OS   Lactobacillus reuteri (strain ATCC 55730 / SD2112).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=491077 {ECO:0000313|EMBL:AEI57880.1, ECO:0000313|Proteomes:UP000001924};
RN   [1] {ECO:0000313|Proteomes:UP000001924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55730 / SD2112 {ECO:0000313|Proteomes:UP000001924};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G.,
RA   Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W.,
RA   Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J.,
RA   Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D.,
RA   Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A.,
RA   Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L.,
RA   Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.,
RA   Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RT   "The complete genome of Lactobacillus reuteri ATCC 55730 / SD2112.";
RL   Submitted (JUN-2011) 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; CP002844; AEI57880.1; -; Genomic_DNA.
DR   RefSeq; WP_003667548.1; NC_015697.1.
DR   ProteinModelPortal; F8DML2; -.
DR   EnsemblBacteria; AEI57880; AEI57880; HMPREF0538_21671.
DR   GeneID; 5188855; -.
DR   KEGG; lru:HMPREF0538_21671; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; POG091H0659; -.
DR   Proteomes; UP000001924; 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:UP000001924};
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:AEI57880.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00124,
KW   ECO:0000256|RuleBase:RU000544, ECO:0000313|EMBL:AEI57880.1};
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   191 AA;  22171 MW;  56A1541E23FACF45 CRC64;
     MAQLFFKYGA MNSGKSIDIL KVAHNYEEQG KPVVLMTSGV DDRSGRGIIA SRIGLERKVK
     PIMDDTNIYD YVNKMDRKIY CVLIDEAQFL KKEHVLQLIK IVDELNIPVM AFGLKNDFRN
     ELFEGSKYLL IYADKIEEMK TICWFCPHKA TMNLRIHNGK PVYEGEQVQI GGNESYYPVC
     RKHYFHPQLK Q
//
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