ID   KCY2_BORBU              Reviewed;         180 AA.
AC   O51759;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Cytidylate kinase 2;
DE            Short=CK 2;
DE            EC=2.7.4.25;
DE   AltName: Full=Cytidine monophosphate kinase 2;
DE            Short=CMP kinase 2;
GN   Name=cmk2; OrderedLocusNames=BB_0819;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000783; AAC67164.1; -; Genomic_DNA.
DR   PIR; B70202; B70202.
DR   RefSeq; NP_212953.1; NC_001318.1.
DR   RefSeq; WP_010889829.1; NC_001318.1.
DR   AlphaFoldDB; O51759; -.
DR   SMR; O51759; -.
DR   STRING; 224326.BB_0819; -.
DR   PRIDE; O51759; -.
DR   EnsemblBacteria; AAC67164; AAC67164; BB_0819.
DR   KEGG; bbu:BB_0819; -.
DR   PATRIC; fig|224326.49.peg.1211; -.
DR   HOGENOM; CLU_079959_1_0_12; -.
DR   OMA; FIFRDMA; -.
DR   Proteomes; UP000001807; 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_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02173; cyt_kin_arch; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..180
FT                   /note="Cytidylate kinase 2"
FT                   /id="PRO_0000132028"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  21066 MW;  4CD956B6F8A5900B CRC64;
     MKIALSGKSG CGNTTVSGMI AKHYGLEFIN YTFHDIAREH NIPFSEFYEK EIIGRNDYYW
     DKYLDNRLSV LSRKNNTVLA SRLAIWISKS ADLKIYLYAK MEVRAERIMT REGGMYSDVL
     SSTFIRDEND KKRYLAIYNI DIDDYFSETD LVIDVTNINP NEVFELIRDE IDKRNLKKNS