| Tag | Content |
|---|
| CPLM ID | CPLM-002911 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cytidylate kinase |
Protein Synonyms/Alias | CK; Cytidine monophosphate kinase; CMP kinase; Protein MssA; p25 |
Gene Name | cmk |
Gene Synonyms/Alias | mssA; ycaF; ycaG; b0910; JW0893 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 165 | RMLQLQEKGFSVNFE | acetylation | [1] | | 179 | ERLLAEIKERDDRDR | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. |
Sequence Annotation | NP_BIND 12 20 ATP (By similarity). |
Keyword | 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 227 AA |
Protein Sequence | MTAIAPVITI DGPSGAGKGT LCKAMAEALQ WHLLDSGAIY RVLALAALHH HVDVASEDAL 60
VPLASHLDVR FVSTNGNLEV ILEGEDVSGE IRTQEVANAA SQVAAFPRVR EALLRRQRAF 120
RELPGLIADG RDMGTVVFPD APVKIFLDAS SEERAHRRML QLQEKGFSVN FERLLAEIKE 180
RDDRDRNRAV APLVPAADAL VLDSTTLSIE QVIEKALQYA RQKLALA 227 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0004127; F:cytidylate kinase activity; IEA:HAMAP. GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |