ID   KTHY_TREPA              Reviewed;         208 AA.
AC   O83373;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=TP_0354;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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;
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC   -!- CAUTION: Could be inactive due to a defective ATP-binding site.
CC       {ECO:0000305}.
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DR   EMBL; AE000520; AAC65341.1; -; Genomic_DNA.
DR   PIR; H71333; H71333.
DR   RefSeq; WP_010881802.1; NC_021490.2.
DR   AlphaFoldDB; O83373; -.
DR   SMR; O83373; -.
DR   IntAct; O83373; 11.
DR   STRING; 243276.TPANIC_0354; -.
DR   PRIDE; O83373; -.
DR   EnsemblBacteria; AAC65341; AAC65341; TP_0354.
DR   GeneID; 57878884; -.
DR   KEGG; tpa:TP_0354; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_1_3_12; -.
DR   OMA; QMAYLFA; -.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000000811; Chromosome.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Putative thymidylate kinase"
FT                   /id="PRO_0000155363"
FT   REGION          12..19
FT                   /note="Defective ATP-binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   208 AA;  23948 MW;  E0186BAF9949896D CRC64;
     MNILHNFVVF EGIDGTGTST QLRALERHFQ ARKDMVFTQE PTGGEIGTLI RDVLQKRVIM
     SSKALGLLFA ADRHEHLEGA GGINDCLAEG KIVLCDRYVF SSLVYQGMAV SGSFAYELNK
     EFPLPEVVFY FDAPIEVCVE RITARGLQTE LYEYTSFQEK ARKGYETIFR KCRHLYPAMK
     VIEIDAREEI EVVHERILHH LREYRRLK