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Database: UniProt/TrEMBL
Entry: H5SXB6_LACLL
LinkDB: H5SXB6_LACLL
Original site: H5SXB6_LACLL 
ID   H5SXB6_LACLL            Unreviewed;       189 AA.
AC   H5SXB6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-SEP-2017, entry version 34.
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=yfiG {ECO:0000313|EMBL:BAL50480.1};
GN   Synonyms=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN   ORFNames=lilo_0479 {ECO:0000313|EMBL:BAL50480.1};
OS   Lactococcus lactis subsp. lactis IO-1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1046624 {ECO:0000313|EMBL:BAL50480.1, ECO:0000313|Proteomes:UP000008189};
RN   [1] {ECO:0000313|EMBL:BAL50480.1, ECO:0000313|Proteomes:UP000008189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IO-1 {ECO:0000313|EMBL:BAL50480.1,
RC   ECO:0000313|Proteomes:UP000008189};
RX   PubMed=22461545; DOI=10.1128/JB.00074-12;
RA   Kato H., Shiwa Y., Oshima K., Machii M., Araya-kojima T., Zendo T.,
RA   Shimizu-kadota M., Hattori M., Sonomoto K., Yoshikawa H.;
RT   "Complete Genome Sequence of Lactococcus lactis IO-1, a Lactic Acid
RT   Bacterium That Utilizes Xylose and Produces High Levels of L-Lactic
RT   Acid.";
RL   J. Bacteriol. 194:2102-2103(2012).
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; AP012281; BAL50480.1; -; Genomic_DNA.
DR   RefSeq; WP_012897306.1; NC_020450.1.
DR   ProteinModelPortal; H5SXB6; -.
DR   EnsemblBacteria; BAL50480; BAL50480; lilo_0479.
DR   KEGG; lls:lilo_0479; -.
DR   PATRIC; fig|1046624.4.peg.506; -.
DR   KO; K00857; -.
DR   Proteomes; UP000008189; 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:UP000008189};
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:BAL50480.1};
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};
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   189 AA;  21413 MW;  FF51FB7110C406CD CRC64;
     MAQLYFKYGT MNSGKSIEIL KVAHNYEEQG KPVLLMTSSL DTRAGVGTVA SRIGMKAEAV
     AIDEEMSVFD YVNSLSAKPF CVLIDEAQFL NKKHVYDFAR VVDELNVPVM AFGLKNDFRN
     ELFEGSKYLL LLADKIEEIK TICWYCSKKA TMVIRTIDGK PVYEGEQLQI GGNETYIPVC
     RKHYFKPEI
//
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