ID   KCY1_BORAP              Reviewed;         221 AA.
AC   Q0SP35; G0IQX3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Cytidylate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CK 1 {ECO:0000255|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238};
GN   Name=cmk1 {ECO:0000255|HAMAP-Rule:MF_00238};
GN   OrderedLocusNames=BAPKO_0130, BafPKo_0126;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP + ATP = CDP + ADP; 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=dCMP + ATP = dCDP + ADP; 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; CP000395; ABH01393.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69359.1; -; Genomic_DNA.
DR   RefSeq; WP_011600843.1; NC_008277.1.
DR   AlphaFoldDB; Q0SP35; -.
DR   SMR; Q0SP35; -.
DR   STRING; 29518.BLA32_03650; -.
DR   KEGG; baf:BAPKO_0130; -.
DR   KEGG; bafz:BafPKo_0126; -.
DR   PATRIC; fig|390236.22.peg.125; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_12; -.
DR   OrthoDB; 9807434at2; -.
DR   Proteomes; UP000005216; 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:UniProtKB-UniRule.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00017; cmk; 1.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..221
FT                   /note="Cytidylate kinase 1"
FT                   /id="PRO_1000048188"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   221 AA;  25513 MW;  A12685834C18A1BF CRC64;
     MIIAIDGPSA SGKSSIAREL SVKLGFKFIS SGYLYRIITL IAQRSFISGC DFISENRLLN
     LVLENDISFN DSSFLLNGEN VENQILNDKI DFQVSFYSSY IGIRNIVNKK LREVVKFSDD
     NYIIEGRDIT TIVFPESEFK IYLDASIKVR ALRRYKQRNG NETLEELERT LKIRDDVDKN
     KQYGKLELSK GVFYLDTSYK GLDDVCNIII EKFNLKKVRE R
//