ID   KTHY_STAA1              Reviewed;         205 AA.
AC   A7WYM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SAHV_0479;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF77362.1; -; Genomic_DNA.
DR   RefSeq; WP_001272126.1; NZ_CTYB01000022.1.
DR   PDB; 4XWA; X-ray; 1.89 A; A/B=1-205.
DR   PDBsum; 4XWA; -.
DR   AlphaFoldDB; A7WYM2; -.
DR   SMR; A7WYM2; -.
DR   KEGG; saw:SAHV_0479; -.
DR   HOGENOM; CLU_049131_0_2_9; -.
DR   OMA; VMTREPG; -.
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_1000023286"
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:4XWA"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           42..52
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           59..76
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           78..83
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   TURN            101..105
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           135..144
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           154..173
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:4XWA"
FT   HELIX           187..202
FT                   /evidence="ECO:0007829|PDB:4XWA"
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