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Database: UniProt
Entry: K0JNR9_SACES
LinkDB: K0JNR9_SACES
Original site: K0JNR9_SACES 
ID   K0JNR9_SACES            Unreviewed;       688 AA.
AC   K0JNR9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   16-OCT-2019, entry version 40.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   OrderedLocusNames=BN6_03330 {ECO:0000313|EMBL:CCH27665.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 /
OS   NBRC 15066 / NRRL 15764).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH27665.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH27665.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; HE804045; CCH27665.1; -; Genomic_DNA.
DR   STRING; 1179773.BN6_03330; -.
DR   EnsemblBacteria; CCH27665; CCH27665; BN6_03330.
DR   KEGG; sesp:BN6_03330; -.
DR   PATRIC; fig|1179773.3.peg.340; -.
DR   KO; K00943; -.
DR   OMA; RFTEAPD; -.
DR   BioCyc; SESP1179773:BN6_RS01630-MONOMER; -.
DR   Proteomes; UP000006281; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   InterPro; IPR010290; TM_effector.
DR   Pfam; PF05977; MFS_3; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006281};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     50     72       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     84    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    178    204       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    216    237       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    275    297       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    309    329       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    341    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    365    388       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    400    425       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    445    461       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       38    468       MFS. {ECO:0000259|PROSITE:PS50850}.
FT   REGION        1     33       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   688 AA;  72670 MW;  589EE1A549F9F611 CRC64;
     MRSGRRGTPG YPGPPARTAG VSTIQDGGGT AASTGHRIRS VLAIRPFRRL WGVTYLCSVG
     DWLSLLALTG LVSKLTQSYQ WESFALSLVV LTQLLPGILF APLGGVLADR FDRRKIMVVC
     DLLRGGLFIS IALVGTAWWL FIANFLVGCC AMLWIPAKDS AVPNLLRRPD QVETANQLGL
     VMTYGIAVIS GAGLYSLISG IPGYLHLQST DIEFRIATIA VMVNGALYVT SAVLVAVRIP
     ELSGRVNAVR AAEGEREGFF AMLRDGLRFA GRTPLVRGLV IGMIGAFAAA GAVIGTAKLY
     ALSLLGGDST FGLLFVAVFA GLAVGMAIAP RMARRLSYDR LFGVTIVLAG TSLVLVALAP
     HLWIALIAVA LVGGCAGMAF LTGLTIVGSK VEDAMRGRTV ALLQSLLKVV LFAASATAPL
     LVSVVQQPDI TLFGHEMQVD GTRPVLFGAA VIAVVLGLIA YRQMDDRRTE PILSDLLAAL
     RGRSRQGAGV LIAVEGESRA DTSAQARRLA DALRAAGHRV LLAADPDLDE QRLRNLLSTA
     DLAGVRAHAL VAAAVRADVV EREVRPALDS GSLVVMERYV DSPLAHFSAA GSVPPREMEG
     LVDWATGRLR PDVTVLLDRT PVEGSASVDA VEHHWRVQRL LTEMAAADPS RYLVVDGEGT
     VDEVAGRVRA AVLPLLAGAS AQPVADNS
//
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