ID   KCY_ECOL6               Reviewed;         227 AA.
AC   P0A6I1; P03823; P23863; P78263;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytidylate kinase;
DE            Short=CK;
DE            EC=2.7.4.25;
DE   AltName: Full=Cytidine monophosphate kinase;
DE            Short=CMP kinase;
GN   Name=cmk; Synonyms=mssA; OrderedLocusNames=c1048;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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;
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN79518.1; -; Genomic_DNA.
DR   RefSeq; WP_000125016.1; NC_004431.1.
DR   AlphaFoldDB; P0A6I1; -.
DR   SMR; P0A6I1; -.
DR   STRING; 199310.c1048; -.
DR   EnsemblBacteria; AAN79518; AAN79518; c1048.
DR   GeneID; 66670814; -.
DR   KEGG; ecc:c1048; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_6; -.
DR   OMA; RAITWWM; -.
DR   BioCyc; ECOL199310:C1048-MON; -.
DR   Proteomes; UP000001410; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..227
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_0000131914"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  24746 MW;  B1578B6B06966776 CRC64;
     MTAIAPVITI DGPSGAGKGT LCKAMAEALQ WHLLDSGAIY RVLALAALHH HVDVASEDAL
     VPLASHLDVR FVSTNGNLEV ILEGEDVSGE IRTQEVANAA SQVAAFPRVR EALLRRQRAF
     RELPGLIADG RDMGTVVFPD APVKIFLDAS SEERAHRRML QLQEKGFSVN FERLLAEIKE
     RDDRDRNRAV APLVPAADAL VLDSTTLSIE QVIEKALQYA RQKLALA