KCY_ECOLI
ID KCY_ECOLI Reviewed; 227 AA.
AC P0A6I0; 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 138.
DE RecName: Full=Cytidylate kinase;
DE Short=CK;
DE EC=2.7.4.25;
DE AltName: Full=Cytidine monophosphate kinase;
DE Short=CMP kinase;
DE AltName: Full=Protein MssA;
DE AltName: Full=p25;
GN Name=cmk; Synonyms=mssA, ycaF, ycaG; OrderedLocusNames=b0910, JW0893;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6384724; DOI=10.1007/bf00334105;
RA Pedersen S., Skouv J., Kajitani M., Ishihama A.;
RT "Transcriptional organization of the rpsA operon of Escherichia coli.";
RL Mol. Gen. Genet. 196:135-140(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JS6.5;
RX PubMed=6281725; DOI=10.1093/nar/10.6.1857;
RA Schnier J., Isono K.;
RT "The DNA sequence of the gene rpsA of Escherichia coli coding for ribosomal
RT protein S1.";
RL Nucleic Acids Res. 10:1857-1865(1982).
RN [6]
RP FUNCTION.
RX PubMed=8190075; DOI=10.1007/bf00283870;
RA Yamanaka K., Ogura T., Koonin E.V., Niki H., Hiraga S.;
RT "Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia
RT coli.";
RL Mol. Gen. Genet. 243:9-16(1994).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7836281; DOI=10.1128/jb.177.3.517-523.1995;
RA Fricke J., Neuhard J., Kelln R.A., Pedersen S.;
RT "The cmk gene encoding cytidine monophosphate kinase is located in the rpsA
RT operon and is required for normal replication rate in Escherichia coli.";
RL J. Bacteriol. 177:517-523(1995).
RN [8]
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=9126287; DOI=10.1006/abbi.1997.9888;
RA Schultz C.P., Ylisastigui-Pons L., Serina L., Sakamoto H., Mantsch H.H.,
RA Neuhard J., Barzu O., Gilles A.M.;
RT "Structural and catalytic properties of CMP kinase from Bacillus subtilis:
RT a comparative analysis with the homologous enzyme from Escherichia coli.";
RL Arch. Biochem. Biophys. 340:144-153(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=9862805; DOI=10.1016/s0969-2126(98)00150-6;
RA Briozzo P., Golinelli-Pimpaneau B., Gilles A.M., Gaucher J.F.,
RA Burlacu-Miron S., Sakamoto H., Janin J., Barzu O.;
RT "Structures of Escherichia coli CMP kinase alone and in complex with CDP: a
RT new fold of the nucleoside monophosphate binding domain and insights into
RT cytosine nucleotide specificity.";
RL Structure 6:1517-1527(1998).
CC -!- FUNCTION: ATP, dATP, and GTP are equally effective as phosphate donors.
CC CMP and dCMP are the best phosphate acceptors.
CC {ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:8190075}.
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 Evidence={ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:9126287};
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 Evidence={ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:9126287};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X00785; CAA25360.1; -; Genomic_DNA.
DR EMBL; X82933; CAA58107.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73996.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35645.1; -; Genomic_DNA.
DR EMBL; V00352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A04448; QQEC31.
DR PIR; E64830; E64830.
DR RefSeq; NP_415430.1; NC_000913.3.
DR RefSeq; WP_000125016.1; NZ_STEB01000006.1.
DR PDB; 1CKE; X-ray; 1.75 A; A=1-227.
DR PDB; 1KDO; X-ray; 1.90 A; A/B=1-227.
DR PDB; 1KDP; X-ray; 2.30 A; A/B=1-227.
DR PDB; 1KDR; X-ray; 2.25 A; A/B=1-227.
DR PDB; 1KDT; X-ray; 1.95 A; A/B=1-227.
DR PDB; 2CMK; X-ray; 2.00 A; A=1-227.
DR PDB; 2FEM; X-ray; 1.90 A; A=1-227.
DR PDB; 2FEO; X-ray; 2.80 A; A=1-227.
DR PDBsum; 1CKE; -.
DR PDBsum; 1KDO; -.
DR PDBsum; 1KDP; -.
DR PDBsum; 1KDR; -.
DR PDBsum; 1KDT; -.
DR PDBsum; 2CMK; -.
DR PDBsum; 2FEM; -.
DR PDBsum; 2FEO; -.
DR AlphaFoldDB; P0A6I0; -.
DR SMR; P0A6I0; -.
DR BioGRID; 4260009; 269.
DR BioGRID; 849909; 3.
DR IntAct; P0A6I0; 6.
DR STRING; 511145.b0910; -.
DR DrugBank; DB02883; 2',3'-Dideoxycytidine-5'-Monophosphate.
DR DrugBank; DB02456; Aracytidine 5'-monophosphate.
DR DrugBank; DB04555; Cytidine-5'-Diphosphate.
DR DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR jPOST; P0A6I0; -.
DR PaxDb; P0A6I0; -.
DR PRIDE; P0A6I0; -.
DR EnsemblBacteria; AAC73996; AAC73996; b0910.
DR EnsemblBacteria; BAA35645; BAA35645; BAA35645.
DR GeneID; 66670814; -.
DR GeneID; 945535; -.
DR KEGG; ecj:JW0893; -.
DR KEGG; eco:b0910; -.
DR PATRIC; fig|1411691.4.peg.1366; -.
DR EchoBASE; EB1244; -.
DR eggNOG; COG0283; Bacteria.
DR HOGENOM; CLU_079959_0_2_6; -.
DR InParanoid; P0A6I0; -.
DR OMA; RAITWWM; -.
DR PhylomeDB; P0A6I0; -.
DR BioCyc; EcoCyc:CMPKI-MON; -.
DR BioCyc; MetaCyc:CMPKI-MON; -.
DR BRENDA; 2.7.4.25; 2026.
DR SABIO-RK; P0A6I0; -.
DR EvolutionaryTrace; P0A6I0; -.
DR PRO; PR:P0A6I0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; IDA:EcoCyc.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
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 Reference proteome; Transferase.
FT CHAIN 1..227
FT /note="Cytidylate kinase"
FT /id="PRO_0000131913"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 164
FT /note="E -> V (in Ref. 1; CAA25360)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1CKE"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1KDO"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1CKE"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1CKE"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:1CKE"
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
