| Tag | Content |
|---|
| CPLM ID | CPLM-009218 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Guanylate kinase |
Protein Synonyms/Alias | GMP kinase |
Gene Name | gmk |
Gene Synonyms/Alias | spoR; b3648; JW3623 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 26 | SLIQALLKTQPLYDT | acetylation | [1] | | 63 | FVNHDEFKEMISRDA | acetylation | [1] | | 128 | IFILPPSKIELDRRL | acetylation | [1] | | 148 | DSEEVIAKRMAQAVA | acetylation | [1] | | 203 | RHDALISKLLAD*** | 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 | Essential for recycling GMP and indirectly, cGMP. |
Sequence Annotation | DOMAIN 4 184 Guanylate kinase-like.
NP_BIND 11 18 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 | 207 AA |
Protein Sequence | MAQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSVSHT TRQPRPGEVH GEHYFFVNHD 60
EFKEMISRDA FLEHAEVFGN YYGTSREAIE QVLATGVDVF LDIDWQGAQQ IRQKMPHARS 120
IFILPPSKIE LDRRLRGRGQ DSEEVIAKRM AQAVAEMSHY AEYDYLIVND DFDTALTDLK 180
TIIRAERLRM SRQKQRHDAL ISKLLAD 207 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004385; F:guanylate kinase activity; IDA:EcoCyc. GO:0042802; F:identical protein binding; IDA:EcoCyc. GO:0006163; P:purine nucleotide metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |