Reviewed, UniProtKB/Swiss-Prot P0A6I0 (KCY_ECOLI)

Names and origin

Protein names

Recommended name:
    Cytidylate kinase
      Short name=CK
    EC=2.7.4.14
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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. HAMAP MF_00238
Subcellular location	Cytoplasm. HAMAP 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
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 MF_00238

PRO_0000131913

Regions

Nucleotide binding

12 – 20

9

ATP By similarity

Experimental info

Sequence conflict

164

1

E → V in CAA25360. Ref.1

Secondary structure

1

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227

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

18 – 29

12

Beta strand

32 – 35

4

Helix

36 – 50

15

Helix

57 – 65

9

Beta strand

69 – 74

6

Beta strand

77 – 82

6

Helix

88 – 91

4

Helix

94 – 103

10

Helix

107 – 118

12

Beta strand

126 – 132

7

Helix

133 – 137

5

Beta strand

142 – 148

7

Helix

151 – 165

15

Helix

171 – 178

8

Beta strand

200 – 203

4

Turn

204 – 206

3

Helix

209 – 224

16

Sequences

	Sequence		Length	Mass (Da)
	P0A6I0-1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: B1578B6B06966776	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

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: 6384724] [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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [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: 9278503] [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: 16738553] [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: 6281725] [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: 8190075] [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: 7836281] [Abstract] Cited for: FUNCTION.
[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: 9126287] [Abstract] Cited for: 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: 9862805] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_001540.1.
NP_415430.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A6I0.

Genome annotation databases

GeneID

945535.

GenomeReviews

Gene locus JW0893 in contig AP009048_GR.
Gene locus b0910 in contig U00096_GR.

KEGG

ecj:JW0893.
eco:b0910.

Organism-specific databases

EchoBASE

EB1244.

EcoGene

EG11265. cmk.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6I0.

OMA

GLLYRAV.

Enzyme and pathway databases

BioCyc

EcoCyc:CMPKI-MON.
MetaCyc:CMPKI-MON.

BRENDA

2.7.4.14. 246.

Gene expression databases

Genevestigator

P0A6I0.

Family and domain databases

HAMAP

MF_00238.
[Tree]

InterPro

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

PANTHER

PTHR21299:SF2. Cytidylate_kin. 1 hit.

Pfam

PF02224. Cytidylate_kin. 1 hit.
[Graphical view]

ProDom

PD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00017. cmk. 1 hit.

ProtoNet

Search...

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:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)