Tag | Content |
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CPLM ID | CPLM-003055 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 5'/3'-nucleotidase SurE |
Protein Synonyms/Alias | Exopolyphosphatase; Nucleoside monophosphate phosphohydrolase; Stationary-phase survival protein SurE |
Gene Name | surE |
Gene Synonyms/Alias | ygbC; b2744; JW2714 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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21 | PGIQTLAKALREFAD | acetylation | [1] | 169 | DLPLDQIKGIRVTRC | acetylation | [1] |
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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 | Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'- monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain- length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase. |
Sequence Annotation | METAL 8 8 Divalent metal cation (By similarity). METAL 9 9 Divalent metal cation (By similarity). METAL 39 39 Divalent metal cation (By similarity). METAL 92 92 Divalent metal cation (By similarity). |
Keyword | Cobalt; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nickel; Nucleotide-binding; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 253 AA |
Protein Sequence | MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD 60 IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA 120 LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH 180 PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV 240 SDWLNSVGVG TQW 253 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0008254; F:3'-nucleotidase activity; IDA:EcoCyc. GO:0008253; F:5'-nucleotidase activity; IDA:EcoCyc. GO:0004309; F:exopolyphosphatase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:HAMAP. GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. GO:0006464; P:cellular protein modification process; IMP:EcoCyc. |
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