ID   SURE_ECOL5              Reviewed;         253 AA.
AC   Q0TEB4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Multifunctional protein surE;
DE   Includes:
DE     RecName: Full=5'/3'-nucleotidase;
DE              EC=3.1.3.5;
DE              EC=3.1.3.6;
DE     AltName: Full=Nucleoside monophosphate phosphohydrolase;
DE   Includes:
DE     RecName: Full=Exopolyphosphatase;
DE              EC=3.6.1.11;
GN   Name=surE; OrderedLocusNames=ECP_2726;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Nucleotidase with a broad substrate specificity as it
CC       can dephosphorylate various ribo- and deoxyribonucleoside 5'-
CC       monophosphates and ribonucleoside 3'-monophosphates with highest
CC       affinity to 3'-AMP. Also hydrolyzes polyphosphate
CC       (exopolyphosphatase activity) with the preference for short-chain-
CC       length substrates (P20-25). Might be involved in the regulation of
CC       dNTP and NTP pools, and in the turnover of 3'-mononucleotides
CC       produced by numerous intracellular RNases (T1, T2, and F) during
CC       the degradation of various RNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O =
CC       (polyphosphate)(n-1) + phosphate.
CC   -!- COFACTOR: Binds 1 divalent metal cation per subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the surE nucleotidase family.
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DR   EMBL; CP000247; ABG70715.1; -; Genomic_DNA.
DR   RefSeq; YP_670616.1; -.
DR   GeneID; 4189998; -.
DR   GenomeReviews; CP000247_GR; ECP_2726.
DR   KEGG; ecp:ECP_2726; -.
DR   HOGENOM; Q0TEB4; -.
DR   OMA; Q0TEB4; SINIPIK.
DR   BioCyc; ECOL362663:ECP_2726-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IEA:EC.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:HAMAP.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00060; -; 1.
DR   InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR   Gene3D; G3DSA:3.40.1210.10; SurE-like_Pase/nucleotidase; 1.
DR   Pfam; PF01975; SurE; 1.
DR   ProDom; PD005378; SurE; 1.
DR   TIGRFAMs; TIGR00087; surE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN         1    253       Multifunctional protein surE.
FT                                /FTId=PRO_1000007728.
FT   METAL         8      8       Divalent metal cation (By similarity).
FT   METAL         9      9       Divalent metal cation (By similarity).
FT   METAL        39     39       Divalent metal cation (By similarity).
FT   METAL        92     92       Divalent metal cation (By similarity).
SQ   SEQUENCE   253 AA;  26900 MW;  33A7CD0AEE13C3DB CRC64;
     MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD
     IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
     LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH
     PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV
     SDWLNSVGVG TQW
//