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Database: UniProt/SWISS-PROT
Entry: KITH_BACFN
LinkDB: KITH_BACFN
Original site: KITH_BACFN 
ID   KITH_BACFN              Reviewed;         199 AA.
AC   Q5LHP5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   28-FEB-2018, entry version 71.
DE   RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; OrderedLocusNames=BF0583;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC
OS   9343).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G.,
RA   Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A.,
RA   Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N.,
RA   Line A., Lord A., Norbertczak H., Ormond D., Price C.,
RA   Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable
RT   gene expression.";
RL   Science 307:1463-1465(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; CR626927; CAH06335.1; -; Genomic_DNA.
DR   RefSeq; WP_010992105.1; NC_003228.3.
DR   ProteinModelPortal; Q5LHP5; -.
DR   SMR; Q5LHP5; -.
DR   STRING; 272559.BF0583; -.
DR   EnsemblBacteria; CAH06335; CAH06335; BF9343_0556.
DR   KEGG; bfs:BF9343_0556; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   Proteomes; UP000006731; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    199       Thymidine kinase.
FT                                /FTId=PRO_0000174957.
FT   NP_BIND      23     30       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      95     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       152    152       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       155    155       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       184    184       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       187    187       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   199 AA;  22221 MW;  210A59503FBB63FA CRC64;
     MVLFSEDHIQ ETRRRGRIEV ICGSMFSGKT EELIRRMKRA KFARQRVEIF KPAIDTRYSE
     GDVVSHDSNS ISSTPIDSSA SILLFTSEID VVGIDEAQFF DSGLIDVCNQ LANNGVRVII
     AGLDMDFKGI PFGPMPALCA IADEVSKVHA ICVKCGQLAS FSHRTVKNDK QVLLGETAQY
     EPLCRECYQR ALQEDREKS
//
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