ID   KTHY_STAAN              Reviewed;         205 AA.
AC   P65249; Q99WC1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=SA0440;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-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:0000255|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR   EMBL; BA000018; BAB41670.1; -; Genomic_DNA.
DR   PIR; C89814; C89814.
DR   RefSeq; WP_001272126.1; NC_002745.2.
DR   PDB; 4HDC; X-ray; 2.05 A; A/B=1-205.
DR   PDB; 4HEJ; X-ray; 2.00 A; A/B=1-205.
DR   PDBsum; 4HDC; -.
DR   PDBsum; 4HEJ; -.
DR   AlphaFoldDB; P65249; -.
DR   SMR; P65249; -.
DR   EnsemblBacteria; BAB41670; BAB41670; BAB41670.
DR   KEGG; sau:SA0440; -.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   OMA; VMTREPG; -.
DR   PRO; PR:P65249; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..205
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155340"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           42..52
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           59..76
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           78..83
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   TURN            101..105
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           135..144
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           154..173
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:4HEJ"
FT   HELIX           187..202
FT                   /evidence="ECO:0007829|PDB:4HEJ"
SQ   SEQUENCE   205 AA;  23425 MW;  71F9C96511FF3A5E CRC64;
     MSAFITFEGP EGSGKTTVIN EVYHRLVKDY DVIMTREPGG VPTGEEIRKI VLEGNDMDIR
     TEAMLFAASR REHLVLKVIP ALKEGKVVLC DRYIDSSLAY QGYARGIGVE EVRALNEFAI
     NGLYPDLTIY LNVSAEVGRE RIIKNSRDQN RLDQEDLKFH EKVIEGYQEI IHNESQRFKS
     VNADQPLENV VEDTYQTIIK YLEKI