ID   KCY_STAAW               Reviewed;         219 AA.
AC   P63807; Q99U12;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=MW1366;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00238};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00238}.
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DR   EMBL; BA000033; BAB95231.1; -; Genomic_DNA.
DR   RefSeq; WP_000644391.1; NC_003923.1.
DR   PDB; 2H92; X-ray; 2.30 A; A/B/C=1-219.
DR   PDBsum; 2H92; -.
DR   AlphaFoldDB; P63807; -.
DR   SMR; P63807; -.
DR   EnsemblBacteria; BAB95231; BAB95231; BAB95231.
DR   KEGG; sam:MW1366; -.
DR   HOGENOM; CLU_079959_0_2_9; -.
DR   OMA; RAITWWM; -.
DR   EvolutionaryTrace; P63807; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..219
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_0000131977"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           34..47
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           54..59
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           102..116
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           146..159
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           166..182
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:2H92"
FT   HELIX           204..216
FT                   /evidence="ECO:0007829|PDB:2H92"
SQ   SEQUENCE   219 AA;  24595 MW;  5C4671129BFDFE46 CRC64;
     MKAINIALDG PAAAGKSTIA KRVASELSMI YVDTGAMYRA LTYKYLKLNK TEDFAKLVDQ
     TTLDLTYKAD KGQCVILDNE DVTDFLRNND VTQHVSYVAS KEPVRSFAVK KQKELAAEKG
     IVMDGRDIGT VVLPDADLKV YMIASVEERA ERRYKDNQLR GIESNFEDLK RDIEARDQYD
     MNREISPLRK ADDAVTLDTT GKSIEEVTDE ILAMVSQIK