CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
21PGIQTLAKALREFADacetylation[1]
169DLPLDQIKGIRVTRCacetylation[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
 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. 
Interpro
 IPR002828; SurE-like_Pase/nucleotidase. 
Pfam
 PF01975; SurE 
SMART
  
PROSITE
  
PRINTS