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Database: UniProt/TrEMBL
Entry: M4KJB1_LACPN
LinkDB: M4KJB1_LACPN
Original site: M4KJB1_LACPN 
ID   M4KJB1_LACPN            Unreviewed;       195 AA.
AC   M4KJB1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 23.
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:AGE39887.1};
GN   ORFNames=zj316_2348 {ECO:0000313|EMBL:AGE39887.1};
OS   Lactobacillus plantarum ZJ316.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1284663 {ECO:0000313|EMBL:AGE39887.1, ECO:0000313|Proteomes:UP000011825};
RN   [1] {ECO:0000313|EMBL:AGE39887.1, ECO:0000313|Proteomes:UP000011825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZJ316 {ECO:0000313|EMBL:AGE39887.1};
RX   PubMed=23516215;
RA   Li X., Gu Q., Lou X., Zhang X., Song D., Shen L., Zhao Y.;
RT   "Complete genome sequence of the probiotic Lactobacillus plantarum
RT   strain ZJ316.";
RL   Genome Announc. 1:E0009413-E0009413(2013).
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; CP004082; AGE39887.1; -; Genomic_DNA.
DR   ProteinModelPortal; M4KJB1; -.
DR   EnsemblBacteria; AGE39887; AGE39887; zj316_2348.
DR   KEGG; lpt:zj316_2348; -.
DR   PATRIC; fig|1284663.3.peg.2319; -.
DR   KO; K00857; -.
DR   Proteomes; UP000011825; 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:UP000011825};
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};
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:AGE39887.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   NP_BIND      12     19       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       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   METAL       149    149       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   195 AA;  22503 MW;  B9C38C274B61D507 CRC64;
     MSRLAQLFFR YGAMNSGKTI EILKVAHNYE EQDKSVIILT SGLDNRDGVG YVASRIGLKR
     EATPVFDDTN IFEIVKQTNP DAACVLIDEA QFLKKHHVLE LADIVDELKI PVMTFGLKND
     FRNELFEGSK YLLLYADKIE EMKTICWFCR KKAIMNLRFH DGQPVYEGEQ VQIGGNEAYY
     PVCRHHYFYP PKLTK
//
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