ID SURE_ECOLI Reviewed; 253 AA. AC P0A840; P36664; Q2MA85; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=5'/3'-nucleotidase SurE {ECO:0000305}; DE EC=3.1.3.5 {ECO:0000269|PubMed:15489502}; DE EC=3.1.3.6 {ECO:0000269|PubMed:15489502}; DE AltName: Full=Exopolyphosphatase; DE EC=3.6.1.11 {ECO:0000269|PubMed:15489502}; DE AltName: Full=Nucleoside monophosphate phosphohydrolase; DE AltName: Full=Stationary-phase survival protein SurE; GN Name=surE; Synonyms=ygbC; OrderedLocusNames=b2744, JW2714; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MP180; RX PubMed=7928962; DOI=10.1128/jb.176.19.6015-6022.1994; RA Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S.; RT "A new gene involved in stationary-phase survival located at 59 minutes on RT the Escherichia coli chromosome."; RL J. Bacteriol. 176:6015-6022(1994). RN [2] RP SEQUENCE REVISION. RA Ichikawa J.K.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL RP PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=15489502; DOI=10.1074/jbc.m411023200; RA Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., RA Savchenko A., Yakunin A.F.; RT "General enzymatic screens identify three new nucleotidases in Escherichia RT coli. Biochemical characterization of SurE, YfbR, and YjjG."; RL J. Biol. Chem. 279:54687-54694(2004). CC -!- FUNCTION: Nucleotidase with a broad substrate specificity as it can CC dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates CC and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP CC (PubMed:15489502). Also hydrolyzes polyphosphate (exopolyphosphatase CC activity) with the preference for short-chain-length substrates (P20- CC 25) (PubMed:15489502). Might be involved in the regulation of dNTP and CC NTP pools, and in the turnover of 3'-mononucleotides produced by CC numerous intracellular RNases (T1, T2, and F) during the degradation of CC various RNAs (PubMed:15489502). Also plays a significant physiological CC role in stress-response and is required for the survival of E.coli in CC stationary growth phase (PubMed:15489502). CC {ECO:0000269|PubMed:15489502, ECO:0000303|PubMed:15489502}. 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:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6; CC Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, CC ChEBI:CHEBI:43474; EC=3.6.1.11; CC Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; CC Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; CC Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:27898, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60880; Evidence={ECO:0000269|PubMed:15489502}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:27894, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60875; Evidence={ECO:0000269|PubMed:15489502}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15489502}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:15489502}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000269|PubMed:15489502}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15489502}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15489502}; CC Note=Binds 1 divalent metal cation per subunit. Highest nucleotidase CC activity with Mn(2+), followed by Co(2+), Ni(2+) and Mg(2+). Highest CC exopolyphosphatase activity with Mg(2+), followed by Co(2+) and Zn(2+). CC {ECO:0000269|PubMed:15489502}; CC -!- ACTIVITY REGULATION: Inhibited by various ribo- or deoxyribonucleoside CC 5'-triphosphates but is insensitive to nucleoside diphosphates. CC {ECO:0000269|PubMed:15489502}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.32 mM for 5'-AMP {ECO:0000269|PubMed:15489502}; CC KM=0.26 mM for 5'-GMP {ECO:0000269|PubMed:15489502}; CC KM=0.28 mM for 5'-dGMP {ECO:0000269|PubMed:15489502}; CC KM=0.1 mM for 3'-AMP {ECO:0000269|PubMed:15489502}; CC KM=0.37 mM for 3'-CMP {ECO:0000269|PubMed:15489502}; CC KM=2.49 mM for pNPP {ECO:0000269|PubMed:15489502}; CC KM=0.02 mM for polyphosphate {ECO:0000269|PubMed:15489502}; CC Vmax=10 umol/min/mg enzyme with 5'-AMP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=22.4 umol/min/mg enzyme with 5'-GMP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=16.4 umol/min/mg enzyme with 5'-dGMP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=20.1 umol/min/mg enzyme with 3'-AMP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=12.1 umol/min/mg enzyme with 3'-CMP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=7.24 umol/min/mg enzyme with pNPP as substrate CC {ECO:0000269|PubMed:15489502}; CC Vmax=0.1 umol/min/mg enzyme with polyphosphate as substrate CC {ECO:0000269|PubMed:15489502}; CC pH dependence: CC Optimum pH is 7.0-7.2 for nucleotidase activity. CC {ECO:0000269|PubMed:15489502}; CC -!- SUBUNIT: Monomer and homooligomer in solution. The oligomeric complex CC consists of at least four subunits. {ECO:0000269|PubMed:15489502}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. {ECO:0000305}. CC -!- CAUTION: Was originally annotated as an acid phosphatase (EC 3.1.3.2). CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA69254.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L07942; AAA79839.1; -; Genomic_DNA. DR EMBL; U29579; AAA69254.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC75786.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76821.1; -; Genomic_DNA. DR PIR; I69732; I69732. DR RefSeq; NP_417224.1; NC_000913.3. DR RefSeq; WP_001295182.1; NZ_SSZK01000017.1. DR AlphaFoldDB; P0A840; -. DR SMR; P0A840; -. DR BioGRID; 4262277; 12. DR DIP; DIP-47982N; -. DR IntAct; P0A840; 3. DR STRING; 511145.b2744; -. DR jPOST; P0A840; -. DR PaxDb; 511145-b2744; -. DR EnsemblBacteria; AAC75786; AAC75786; b2744. DR GeneID; 75205607; -. DR GeneID; 947211; -. DR KEGG; ecj:JW2714; -. DR KEGG; eco:b2744; -. DR PATRIC; fig|511145.12.peg.2839; -. DR EchoBASE; EB1764; -. DR eggNOG; COG0496; Bacteria. DR HOGENOM; CLU_045192_1_2_6; -. DR InParanoid; P0A840; -. DR OMA; DCVHIAL; -. DR OrthoDB; 9780815at2; -. DR PhylomeDB; P0A840; -. DR BioCyc; EcoCyc:EG11817-MONOMER; -. DR BioCyc; MetaCyc:EG11817-MONOMER; -. DR BRENDA; 3.1.3.5; 2026. DR BRENDA; 3.1.3.6; 2026. DR BRENDA; 3.6.1.11; 2026. DR SABIO-RK; P0A840; -. DR PRO; PR:P0A840; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008254; F:3'-nucleotidase activity; IDA:EcoCyc. DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:EcoCyc. DR GO; GO:0004309; F:exopolyphosphatase activity; IDA:EcoCyc. DR GO; GO:0050484; F:GMP 5'-nucleotidase activity; IEA:RHEA. DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046050; P:UMP catabolic process; IGI:EcoCyc. 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 NCBIfam; TIGR00087; surE; 1. 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. PE 1: Evidence at protein level; KW Cobalt; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nickel; KW Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1..253 FT /note="5'/3'-nucleotidase SurE" FT /id="PRO_0000111809" 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 92 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" 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 //