Entry sw:SURE_SALPB

ID   SURE_SALPB              Reviewed;         253 AA.
AC   A9N2D0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   02-NOV-2016, entry version 54.
DE   RecName: Full=5'/3'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.6 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Exopolyphosphatase {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.6.1.11 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Nucleoside monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN   Name=surE {ECO:0000255|HAMAP-Rule:MF_00060};
GN   OrderedLocusNames=SPAB_03641;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA   Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate. {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate. {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O =
CC       (polyphosphate)(n-1) + phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00060}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00060};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- SIMILARITY: Belongs to the SurE nucleotidase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00060}.
DR   EMBL; CP000886; ABX68981.1; -; Genomic_DNA.
DR   RefSeq; WP_001221537.1; NC_010102.1.
DR   ProteinModelPortal; A9N2D0; -.
DR   EnsemblBacteria; ABX68981; ABX68981; SPAB_03641.
DR   KEGG; spq:SPAB_03641; -.
DR   PATRIC; 18534201; VBISalEnt120821_2942.
DR   HOGENOM; HOG000122500; -.
DR   KO; K03787; -.
DR   OMA; ANGFYYV; -.
DR   BioCyc; SENT28901:GH9O-3632-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1210.10; -; 1.
DR   HAMAP; MF_00060; SurE; 1.
DR   InterPro; IPR030048; SurE.
DR   InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR   Pfam; PF01975; SurE; 1.
DR   SUPFAM; SSF64167; SSF64167; 1.
DR   TIGRFAMs; TIGR00087; surE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    253       5'/3'-nucleotidase SurE.
FT                                /FTId=PRO_1000075039.
FT   METAL         8      8       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00060}.
FT   METAL         9      9       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00060}.
FT   METAL        39     39       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00060}.
FT   METAL        92     92       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         3    180       ipfam:SurE [T]
FT   MYHIT         1    249       ihamap:SurE [T]
SQ   SEQUENCE   253 AA;  26994 MW;  192BC381E4350844 CRC64;
     MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFDNGD
     IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
     LAVSLNGYQH YDTAAAVTCA LLRGLSREPL RTGRILNVNV PDLPLAQIKG IRVTRCGSRH
     PADKVIPQED PRGNTLYWIG PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV
     SDWLDSVGVG TQW
//