SURE_ECOLI
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 03-AUG-2022, entry version 121.
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; Proteobacteria; 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=0.10 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=10.0 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=0.10 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};
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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; P0A840; -.
DR PRIDE; P0A840; -.
DR EnsemblBacteria; AAC75786; AAC75786; b2744.
DR EnsemblBacteria; BAE76821; BAE76821; BAE76821.
DR GeneID; 67413964; -.
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 PhylomeDB; P0A840; -.
DR BioCyc; EcoCyc:EG11817-MON; -.
DR BioCyc; MetaCyc:EG11817-MON; -.
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; IBA:GO_Central.
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 InterPro; IPR036523; SurE-like_sf.
DR PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 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
