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Protein

Cytidylate kinase

Gene

cmk

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.2 Publications

Catalytic activityi

ATP + (d)CMP = ADP + (d)CDP.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 209ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • cytidylate kinase activity Source: EcoCyc

GO - Biological processi

  • nucleobase-containing small molecule interconversion Source: EcoCyc
  • nucleotide phosphorylation Source: GOC
  • pyrimidine nucleotide metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CMPKI-MONOMER.
ECOL316407:JW0893-MONOMER.
MetaCyc:CMPKI-MONOMER.
BRENDAi2.7.4.25. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidylate kinase (EC:2.7.4.25)
Short name:
CK
Alternative name(s):
Cytidine monophosphate kinase
Short name:
CMP kinase
Protein MssA
p25
Gene namesi
Name:cmk
Synonyms:mssA, ycaF, ycaG
Ordered Locus Names:b0910, JW0893
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11265. cmk.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Cytidylate kinasePRO_0000131913Add
BLAST

Proteomic databases

EPDiP0A6I0.
PaxDbiP0A6I0.
PRIDEiP0A6I0.

Interactioni

Protein-protein interaction databases

BioGridi4260009. 256 interactions.
IntActiP0A6I0. 6 interactions.
STRINGi511145.b0910.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi18 – 2912Combined sources
Beta strandi32 – 354Combined sources
Helixi36 – 5015Combined sources
Helixi57 – 659Combined sources
Beta strandi69 – 746Combined sources
Beta strandi77 – 826Combined sources
Helixi88 – 914Combined sources
Helixi94 – 10310Combined sources
Helixi107 – 11812Combined sources
Beta strandi126 – 1327Combined sources
Helixi133 – 1375Combined sources
Beta strandi142 – 1487Combined sources
Helixi151 – 16515Combined sources
Helixi171 – 1788Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi200 – 2034Combined sources
Turni204 – 2063Combined sources
Helixi209 – 22416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CKEX-ray1.75A1-227[»]
1KDOX-ray1.90A/B1-227[»]
1KDPX-ray2.30A/B1-227[»]
1KDRX-ray2.25A/B1-227[»]
1KDTX-ray1.95A/B1-227[»]
2CMKX-ray2.00A1-227[»]
2FEMX-ray1.90A1-227[»]
2FEOX-ray2.80A1-227[»]
ProteinModelPortaliP0A6I0.
SMRiP0A6I0. Positions 3-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6I0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CAT. Bacteria.
COG0283. LUCA.
HOGENOMiHOG000242849.
InParanoidiP0A6I0.
KOiK00945.
OMAiLKIFMTA.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP0A6I0.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00238. Cytidyl_kinase_type1.
InterProiIPR003136. Cytidylate_kin.
IPR011994. Cytidylate_kinase_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02224. Cytidylate_kin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00017. cmk. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAIAPVITI DGPSGAGKGT LCKAMAEALQ WHLLDSGAIY RVLALAALHH
60 70 80 90 100
HVDVASEDAL VPLASHLDVR FVSTNGNLEV ILEGEDVSGE IRTQEVANAA
110 120 130 140 150
SQVAAFPRVR EALLRRQRAF RELPGLIADG RDMGTVVFPD APVKIFLDAS
160 170 180 190 200
SEERAHRRML QLQEKGFSVN FERLLAEIKE RDDRDRNRAV APLVPAADAL
210 220
VLDSTTLSIE QVIEKALQYA RQKLALA
Length:227
Mass (Da):24,746
Last modified:March 29, 2005 - v1
Checksum:iB1578B6B06966776
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641E → V in CAA25360 (PubMed:6384724).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00785 Genomic DNA. Translation: CAA25360.1.
X82933 Genomic DNA. Translation: CAA58107.1.
U00096 Genomic DNA. Translation: AAC73996.1.
AP009048 Genomic DNA. Translation: BAA35645.1.
V00352 Genomic DNA. No translation available.
PIRiA04448. QQEC31.
E64830.
RefSeqiNP_415430.1. NC_000913.3.
WP_000125016.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73996; AAC73996; b0910.
BAA35645; BAA35645; BAA35645.
GeneIDi945535.
KEGGiecj:JW0893.
eco:b0910.
PATRICi32117033. VBIEscCol129921_0941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00785 Genomic DNA. Translation: CAA25360.1.
X82933 Genomic DNA. Translation: CAA58107.1.
U00096 Genomic DNA. Translation: AAC73996.1.
AP009048 Genomic DNA. Translation: BAA35645.1.
V00352 Genomic DNA. No translation available.
PIRiA04448. QQEC31.
E64830.
RefSeqiNP_415430.1. NC_000913.3.
WP_000125016.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CKEX-ray1.75A1-227[»]
1KDOX-ray1.90A/B1-227[»]
1KDPX-ray2.30A/B1-227[»]
1KDRX-ray2.25A/B1-227[»]
1KDTX-ray1.95A/B1-227[»]
2CMKX-ray2.00A1-227[»]
2FEMX-ray1.90A1-227[»]
2FEOX-ray2.80A1-227[»]
ProteinModelPortaliP0A6I0.
SMRiP0A6I0. Positions 3-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260009. 256 interactions.
IntActiP0A6I0. 6 interactions.
STRINGi511145.b0910.

Proteomic databases

EPDiP0A6I0.
PaxDbiP0A6I0.
PRIDEiP0A6I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73996; AAC73996; b0910.
BAA35645; BAA35645; BAA35645.
GeneIDi945535.
KEGGiecj:JW0893.
eco:b0910.
PATRICi32117033. VBIEscCol129921_0941.

Organism-specific databases

EchoBASEiEB1244.
EcoGeneiEG11265. cmk.

Phylogenomic databases

eggNOGiENOG4105CAT. Bacteria.
COG0283. LUCA.
HOGENOMiHOG000242849.
InParanoidiP0A6I0.
KOiK00945.
OMAiLKIFMTA.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP0A6I0.

Enzyme and pathway databases

BioCyciEcoCyc:CMPKI-MONOMER.
ECOL316407:JW0893-MONOMER.
MetaCyc:CMPKI-MONOMER.
BRENDAi2.7.4.25. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6I0.
PROiP0A6I0.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00238. Cytidyl_kinase_type1.
InterProiIPR003136. Cytidylate_kin.
IPR011994. Cytidylate_kinase_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02224. Cytidylate_kin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00017. cmk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional organization of the rpsA operon of Escherichia coli."
    Pedersen S., Skouv J., Kajitani M., Ishihama A.
    Mol. Gen. Genet. 196:135-140(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The DNA sequence of the gene rpsA of Escherichia coli coding for ribosomal protein S1."
    Schnier J., Isono K.
    Nucleic Acids Res. 10:1857-1865(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / JS6.5.
  6. "Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli."
    Yamanaka K., Ogura T., Koonin E.V., Niki H., Hiraga S.
    Mol. Gen. Genet. 243:9-16(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli."
    Fricke J., Neuhard J., Kelln R.A., Pedersen S.
    J. Bacteriol. 177:517-523(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli."
    Schultz C.P., Ylisastigui-Pons L., Serina L., Sakamoto H., Mantsch H.H., Neuhard J., Barzu O., Gilles A.M.
    Arch. Biochem. Biophys. 340:144-153(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.
  9. "Structures of Escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity."
    Briozzo P., Golinelli-Pimpaneau B., Gilles A.M., Gaucher J.F., Burlacu-Miron S., Sakamoto H., Janin J., Barzu O.
    Structure 6:1517-1527(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiKCY_ECOLI
AccessioniPrimary (citable) accession number: P0A6I0
Secondary accession number(s): P03823, P23863, P78263
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 13, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.