ID   SURE_SALTY              Reviewed;         253 AA.
AC   P66881; Q8XFG4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=STM2927;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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; AE008833; AAL21807.1; -; Genomic_DNA.
DR   RefSeq; NP_461848.1; -.
DR   PDB; 2V4N; X-ray; 1.70 A; A=1-253.
DR   PDB; 2V4O; X-ray; 2.71 A; A/B/C/D=1-253.
DR   PDBsum; 2V4N; -.
DR   PDBsum; 2V4O; -.
DR   GeneID; 1254450; -.
DR   GenomeReviews; AE006468_GR; STM2927.
DR   KEGG; stm:STM2927; -.
DR   HOGENOM; P66881; -.
DR   OMA; P66881; NLNIPPC.
DR   BioCyc; STYP99287:STM2927-MON; -.
DR   BRENDA; 3.1.3.5; 2.
DR   BRENDA; 3.1.3.6; 2.
DR   BRENDA; 3.6.1.11; 2.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN         1    253       Multifunctional protein surE.
FT                                /FTId=PRO_0000111839.
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;  26980 MW;  A8C4DD6EE42372F8 CRC64;
     MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFDNGD
     IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
     LAVSLNGYQH YDTAAAVTCA LLRGLSREPL RTGRILNVNV PDLPLAQVKG IRVTRCGSRH
     PADKVIPQED PRGNTLYWIG PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV
     SDWLDSVGVG TQW
//