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P0A840 (SURE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'/3'-nucleotidase SurE

EC=3.1.3.5
EC=3.1.3.6
Alternative name(s):
Exopolyphosphatase
EC=3.6.1.11
Nucleoside monophosphate phosphohydrolase
Stationary-phase survival protein SurE
Gene names
Name:surE
Synonyms:ygbC
Ordered Locus Names:b2744, JW2714
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase. Ref.5

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060

A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. HAMAP-Rule MF_00060

Cofactor

Binds 1 divalent metal cation per subunit. Highest nucleotidase activity with Mn2+, followed by Co2+, Ni2+ and Mg2+. Highest exopolyphosphatase activity with Mg2+, followed by Co2+ and Zn2+. Ref.5

Enzyme regulation

Inhibited by various ribo- or deoxyribonucleoside 5'-triphosphates but is insensitive to nucleoside diphosphates. HAMAP-Rule MF_00060

Subunit structure

Monomer and homooligomer in solution. The oligomeric complex consists of at least four subunits. Ref.5

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00060.

Sequence similarities

Belongs to the SurE nucleotidase family.

Caution

Was originally annotated as an acid phosphatase (EC 3.1.3.2).

Biophysicochemical properties

Kinetic parameters:

KM=0.32 mM for 5'-AMP Ref.5

KM=0.26 mM for 5'-GMP

KM=0.28 mM for 5'-dGMP

KM=0.10 mM for 3'-AMP

KM=0.37 mM for 3'-CMP

KM=2.49 mM for pNPP

KM=0.02 mM for polyphosphate

Vmax=10.0 µmol/min/mg enzyme with 5'-AMP as substrate

Vmax=22.4 µmol/min/mg enzyme with 5'-GMP as substrate

Vmax=16.4 µmol/min/mg enzyme with 5'-dGMP as substrate

Vmax=20.1 µmol/min/mg enzyme with 3'-AMP as substrate

Vmax=12.1 µmol/min/mg enzyme with 3'-CMP as substrate

Vmax=7.24 µmol/min/mg enzyme with pNPP as substrate

Vmax=0.10 µmol/min/mg enzyme with polyphosphate as substrate

pH dependence:

Optimum pH is 7.0-7.2 for nucleotidase activity.

Sequence caution

The sequence AAA69254.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2532535'/3'-nucleotidase SurE HAMAP-Rule MF_00060
PRO_0000111809

Sites

Metal binding81Divalent metal cation By similarity
Metal binding91Divalent metal cation By similarity
Metal binding391Divalent metal cation By similarity
Metal binding921Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A840 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 33A7CD0AEE13C3DB

FASTA25326,900
        10         20         30         40         50         60 
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD 

        70         80         90        100        110        120 
IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA 

       130        140        150        160        170        180 
LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH 

       190        200        210        220        230        240 
PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV 

       250 
SDWLNSVGVG TQW 

« Hide

References

« Hide 'large scale' references
[1]"A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome."
Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S.
J. Bacteriol. 176:6015-6022(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MP180.
[2]Ichikawa J.K.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG."
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., Savchenko A., Yakunin A.F.
J. Biol. Chem. 279:54687-54694(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07942 Genomic DNA. Translation: AAA79839.1.
U29579 Genomic DNA. Translation: AAA69254.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75786.1.
AP009048 Genomic DNA. Translation: BAE76821.1.
PIRI69732.
RefSeqNP_417224.1. NC_000913.3.
YP_490953.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A840.
SMRP0A840. Positions 1-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47982N.
IntActP0A840. 3 interactions.
STRING511145.b2744.

Proteomic databases

PaxDbP0A840.
PRIDEP0A840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75786; AAC75786; b2744.
BAE76821; BAE76821; BAE76821.
GeneID12933283.
947211.
KEGGecj:Y75_p2682.
eco:b2744.
PATRIC32120894. VBIEscCol129921_2839.

Organism-specific databases

EchoBASEEB1764.
EcoGeneEG11817. surE.

Phylogenomic databases

eggNOGCOG0496.
HOGENOMHOG000122500.
KOK03787.
OMADCVHIAL.
OrthoDBEOG68WR45.
PhylomeDBP0A840.
ProtClustDBPRK00346.

Enzyme and pathway databases

BioCycEcoCyc:EG11817-MONOMER.
ECOL316407:JW2714-MONOMER.
MetaCyc:EG11817-MONOMER.
BRENDA3.1.3.5. 2026.
SABIO-RKP0A840.

Gene expression databases

GenevestigatorP0A840.

Family and domain databases

Gene3D3.40.1210.10. 1 hit.
HAMAPMF_00060. SurE.
InterProIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMSSF64167. SSF64167. 1 hit.
TIGRFAMsTIGR00087. surE. 1 hit.
ProtoNetSearch...

Other

PROP0A840.

Entry information

Entry nameSURE_ECOLI
AccessionPrimary (citable) accession number: P0A840
Secondary accession number(s): P36664, Q2MA85
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene