ID   SURE_LEPBP              Reviewed;         247 AA.
AC   B0SJM4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   04-NOV-2026, entry version 92.
DE   RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN   Name=surE {ECO:0000255|HAMAP-Rule:MF_00060};
GN   OrderedLocusNames=LEPBI_I0458;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Pseudomonadati; Spirochaetota; Leptospiria; Leptospirales;
OC   Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside
CC       5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000255|HAMAP-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. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; CP000786; ABZ96597.1; -; Genomic_DNA.
DR   RefSeq; WP_012387484.1; NC_010602.1.
DR   SMR; B0SJM4; -.
DR   STRING; 456481.LEPBI_I0458; -.
DR   KEGG; lbi:LEPBI_I0458; -.
DR   HOGENOM; CLU_045192_1_2_12; -.
DR   OMA; AAEHWGP; -.
DR   OrthoDB; 9780815at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS02230-MONOMER; -.
DR   Gene3D; 3.40.1210.10; Survival protein SurE-like phosphatase/nucleotidase; 1.
DR   HAMAP; MF_00060; SurE; 1.
DR   InterPro; IPR030048; SurE.
DR   InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR   InterPro; IPR036523; SurE-like_sf.
DR   PANTHER; PTHR30457; 5'-NUCLEOTIDASE SURE; 1.
DR   PANTHER; PTHR30457:SF12; 5'_3'-NUCLEOTIDASE SURE; 1.
DR   Pfam; PF01975; SurE; 1.
DR   SUPFAM; SSF64167; SurE-like; 1.
DR   NCBIfam; TIGR00087; surE; 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IEA:TreeGrafter.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000001847; Chromosome I.
DR   AlphaFoldDB; B0SJM4; -.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..247
FT                   /note="5'-nucleotidase SurE"
FT                   /id="PRO_1000092014"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         39
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         91
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
SQ   SEQUENCE   247 AA;  27391 MW;  9D9FCFF657EEE05A CRC64;
     MNLLITNDDG ISSAGIKALE RVLGKSYNTY LIAPLKERSV TSMALTVFQG MRVERINDNH
     YIADGFPVDC VNIGLYAEIF PKIDFVISGI NRGVNMGYDV HYSGTVGAAK HGALHGIPSL
     AVSSGRIDPE DGYEKEAELV LAFLEQYKSQ IQSGEIWNLN FPPEVSGTGT ISELVFTRLG
     RRRYSEKYEK KQIIEGVSEF QLNGSLLGHD EETGTDFEAY AQGKIPLTPI QLDLTEKNRL
     KELLTNR
//