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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
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
//
