| Tag | Content |
|---|
| CPLM ID | CPLM-003076 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoenolpyruvate synthase regulatory protein |
Protein Synonyms/Alias | PEP synthase regulatory protein; PSRP; Pyruvate, water dikinase regulatory protein |
Gene Name | ppsR |
Gene Synonyms/Alias | ydiA; b1703; JW1693 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 125 | LNPNNLNKYDARIAA | acetylation | [1] | | 198 | LVLPASLKPLQHKLF | 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 | Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. |
Sequence Annotation | NP_BIND 157 164 ATP (Potential). |
Keyword | ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 277 AA |
Protein Sequence | MDNAVDRHVF YISDGTAITA EVLGHAVMSQ FPVTISSITL PFVENESRAR AVKDQIDAIY 60
HQTGVRPLVF YSIVLPEIRA IILQSEGFCQ DIVQALVAPL QQEMKLDPTP IAHRTHGLNP 120
NNLNKYDARI AAIDYTLAHD DGISLRNLDQ AQVILLGVSR CGKTPTSLYL AMQFGIRAAN 180
YPFIADDMDN LVLPASLKPL QHKLFGLTID PERLAAIREE RRENSRYASL RQCRMEVAEV 240
EALYRKNQIP WINSTNYSVE EIATKILDIM GLSRRMY 277 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:HAMAP. GO:0030234; F:enzyme regulator activity; IDA:EcoCyc. GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. GO:0051338; P:regulation of transferase activity; IDA:EcoCyc. |
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