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Database: UniProt/TrEMBL
Entry: A0A143AF33_9LACO
LinkDB: A0A143AF33_9LACO
Original site: A0A143AF33_9LACO 
ID   A0A143AF33_9LACO        Unreviewed;       196 AA.
AC   A0A143AF33;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
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=ADU72_1729 {ECO:0000313|EMBL:AMV67654.1};
OS   Pediococcus damnosus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=51663 {ECO:0000313|EMBL:AMV67654.1, ECO:0000313|Proteomes:UP000076244};
RN   [1] {ECO:0000313|EMBL:AMV67654.1, ECO:0000313|Proteomes:UP000076244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMW 2.1535 {ECO:0000313|EMBL:AMV67654.1,
RC   ECO:0000313|Proteomes:UP000076244};
RX   PubMed=27028007;
RA   Behr J., Geissler A.J., Schmid J., Zehe A., Vogel R.F.;
RT   "The Identification of Novel Diagnostic Marker Genes for the Detection
RT   of Beer Spoiling Pediococcus damnosus Strains Using the BlAst
RT   Diagnostic Gene findEr.";
RL   PLoS ONE 11:E0152747-E0152747(2016).
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; CP012288; AMV67654.1; -; Genomic_DNA.
DR   RefSeq; WP_046872230.1; NZ_JQBD01000025.1.
DR   EnsemblBacteria; AMV67654; AMV67654; ADU72_1729.
DR   KEGG; pdm:ADU72_1729; -.
DR   PATRIC; fig|51663.52.peg.718; -.
DR   KO; K00857; -.
DR   Proteomes; UP000076244; 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:UP000076244};
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:AMV67654.1};
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:AMV67654.1};
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   196 AA;  22671 MW;  46F39581D7BC0763 CRC64;
     MAQLFFHYGA MNSGKSIEIL KVAHNYEEQH KSVVLMTSGI DTRKKVGEIA SRIGLHRTAE
     PIFDDTDIYK RVLELNPNAA CLLIDEAQFL KKHHILELAK VVDDLNIPVM TFGLKNDFRN
     ELFEGSKYLL IYADKIEEMK TICWFCKHKA IMNLRFANGK PVYEGEQVQI GGNEAYYPVC
     RRHYFNPPLD EMRESK
//
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