Cytidylate kinase - Escherichia coli (strain K12)

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P0A6I0 (KCY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytidylate kinase
Short name=CK
EC=2.7.4.25

Alternative name(s):
Cytidine monophosphate kinase
Short name=CMP kinase
Protein MssA
p25

Gene names

Name:	cmk
Synonyms:	mssA, ycaF, ycaG
Ordered Locus Names:	b0910, JW0893

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Ref.6 Ref.7
Catalytic activity	ATP + (d)CMP = ADP + (d)CDP. Ref.7 Ref.8
Subcellular location	Cytoplasm HAMAP-Rule MF_00238.
Sequence similarities	Belongs to the cytidylate kinase family. Type 1 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pyrimidine nucleotide metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP cytidylate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

Cytidylate kinase HAMAP-Rule MF_00238

PRO_0000131913

Regions

Nucleotide binding

12 – 20

ATP By similarity

Experimental info

Sequence conflict

164

E → V in CAA25360. Ref.1

Secondary structure

227

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6I0 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: B1578B6B06966776
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FASTA

227

24,746

        10         20         30         40         50         60 
MTAIAPVITI DGPSGAGKGT LCKAMAEALQ WHLLDSGAIY RVLALAALHH HVDVASEDAL 

        70         80         90        100        110        120 
VPLASHLDVR FVSTNGNLEV ILEGEDVSGE IRTQEVANAA SQVAAFPRVR EALLRRQRAF 

       130        140        150        160        170        180 
RELPGLIADG RDMGTVVFPD APVKIFLDAS SEERAHRRML QLQEKGFSVN FERLLAEIKE 

       190        200        210        220 
RDDRDRNRAV APLVPAADAL VLDSTTLSIE QVIEKALQYA RQKLALA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

QQEC31. A04448.
E64830.

RefSeq

NP_415430.1. NC_000913.2.
YP_489182.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CKE	X-ray	1.75	A	1-227	[»]
1KDO	X-ray	1.90	A/B	1-227	[»]
1KDP	X-ray	2.30	A/B	1-227	[»]
1KDR	X-ray	2.25	A/B	1-227	[»]
1KDT	X-ray	1.95	A/B	1-227	[»]
2CMK	X-ray	2.00	A	1-227	[»]
2FEM	X-ray	1.90	A	1-227	[»]
2FEO	X-ray	2.80	A	1-227	[»]

ProteinModelPortal

P0A6I0.

SMR

P0A6I0. Positions 3-225.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6I0. 3 interactions.

STRING

511145.b0910.

Proteomic databases

PaxDb

P0A6I0.

PRIDE

P0A6I0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73996; AAC73996; b0910.
BAA35645; BAA35645; BAA35645.

GeneID

12931015.
945535.

KEGG

ecj:Y75_p0882.
eco:b0910.

PATRIC

32117033. VBIEscCol129921_0941.

Organism-specific databases

EchoBASE

EB1244.

EcoGene

EG11265. cmk.

Phylogenomic databases

eggNOG

COG0283.

HOGENOM

HOG000242849.

K00945.

OMA

HIDTGAM.

ProtClustDB

PRK00023.

Enzyme and pathway databases

BioCyc

EcoCyc:CMPKI-MONOMER.
ECOL316407:JW0893-MONOMER.
MetaCyc:CMPKI-MONOMER.

BRENDA

2.7.4.14. 2026.

Gene expression databases

Genevestigator

P0A6I0.

Family and domain databases

HAMAP

MF_00238. Cytidyl_kinase_type1.

InterPro

IPR003136. Cytidylate_kin.
IPR011994. Cytidylate_kinase_dom.
[Graphical view]

PANTHER

PTHR21299:SF2. PTHR21299:SF2. 1 hit.

Pfam

PF02224. Cytidylate_kin. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00017. cmk. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6I0.

Entry information

Entry name

KCY_ECOLI

Accession

Primary (citable) accession number: P0A6I0
Secondary accession number(s): P03823, P23863, P78263

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents