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P0A840

- SURE_ECOLI

UniProt

P0A840 - SURE_ECOLI

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Protein

5'/3'-nucleotidase SurE

Gene
surE, ygbC, b2744, JW2714
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.UniRule annotation

Cofactori

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+.1 Publication

Enzyme regulationi

Inhibited by various ribo- or deoxyribonucleoside 5'-triphosphates but is insensitive to nucleoside diphosphates.UniRule annotation

Kineticsi

  1. KM=0.32 mM for 5'-AMP1 Publication
  2. KM=0.26 mM for 5'-GMP
  3. KM=0.28 mM for 5'-dGMP
  4. KM=0.10 mM for 3'-AMP
  5. KM=0.37 mM for 3'-CMP
  6. KM=2.49 mM for pNPP
  7. 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 dependencei

Optimum pH is 7.0-7.2 for nucleotidase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Divalent metal cation By similarity
Metal bindingi9 – 91Divalent metal cation By similarity
Metal bindingi39 – 391Divalent metal cation By similarity
Metal bindingi92 – 921Divalent metal cation By similarity

GO - Molecular functioni

  1. 3'-nucleotidase activity Source: EcoCyc
  2. 5'-nucleotidase activity Source: EcoCyc
  3. exopolyphosphatase activity Source: EcoCyc
  4. manganese ion binding Source: EcoCyc
  5. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. UMP catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Cobalt, Magnesium, Manganese, Metal-binding, Nickel, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG11817-MONOMER.
ECOL316407:JW2714-MONOMER.
MetaCyc:EG11817-MONOMER.
BRENDAi3.1.3.5. 2026.
SABIO-RKP0A840.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:surE
Synonyms:ygbC
Ordered Locus Names:b2744, JW2714
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11817. surE.

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2532535'/3'-nucleotidase SurEUniRule annotationPRO_0000111809Add
BLAST

Proteomic databases

PaxDbiP0A840.
PRIDEiP0A840.

Expressioni

Gene expression databases

GenevestigatoriP0A840.

Interactioni

Subunit structurei

Monomer and homooligomer in solution. The oligomeric complex consists of at least four subunits.1 Publication

Protein-protein interaction databases

DIPiDIP-47982N.
IntActiP0A840. 3 interactions.
STRINGi511145.b2744.

Structurei

3D structure databases

ProteinModelPortaliP0A840.
SMRiP0A840. Positions 1-253.

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.

Phylogenomic databases

eggNOGiCOG0496.
HOGENOMiHOG000122500.
KOiK03787.
OMAiVCDLIPK.
OrthoDBiEOG68WR45.
PhylomeDBiP0A840.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A840-1 [UniParc]FASTAAdd to Basket

« Hide

MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS    50
LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD 100
VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL 150
RTGRILNINV PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG 200
PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG 250
TQW 253
Length:253
Mass (Da):26,900
Last modified:June 7, 2005 - v1
Checksum:i33A7CD0AEE13C3DB
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiI69732.
RefSeqiNP_417224.1. NC_000913.3.
YP_490953.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75786; AAC75786; b2744.
BAE76821; BAE76821; BAE76821.
GeneIDi12933283.
947211.
KEGGiecj:Y75_p2682.
eco:b2744.
PATRICi32120894. VBIEscCol129921_2839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi I69732.
RefSeqi NP_417224.1. NC_000913.3.
YP_490953.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A840.
SMRi P0A840. Positions 1-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47982N.
IntActi P0A840. 3 interactions.
STRINGi 511145.b2744.

Proteomic databases

PaxDbi P0A840.
PRIDEi P0A840.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75786 ; AAC75786 ; b2744 .
BAE76821 ; BAE76821 ; BAE76821 .
GeneIDi 12933283.
947211.
KEGGi ecj:Y75_p2682.
eco:b2744.
PATRICi 32120894. VBIEscCol129921_2839.

Organism-specific databases

EchoBASEi EB1764.
EcoGenei EG11817. surE.

Phylogenomic databases

eggNOGi COG0496.
HOGENOMi HOG000122500.
KOi K03787.
OMAi VCDLIPK.
OrthoDBi EOG68WR45.
PhylomeDBi P0A840.

Enzyme and pathway databases

BioCyci EcoCyc:EG11817-MONOMER.
ECOL316407:JW2714-MONOMER.
MetaCyc:EG11817-MONOMER.
BRENDAi 3.1.3.5. 2026.
SABIO-RK P0A840.

Miscellaneous databases

PROi P0A840.

Gene expression databases

Genevestigatori P0A840.

Family and domain databases

Gene3Di 3.40.1210.10. 1 hit.
HAMAPi MF_00060. SurE.
InterProi IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view ]
Pfami PF01975. SurE. 1 hit.
[Graphical view ]
SUPFAMi SSF64167. SSF64167. 1 hit.
TIGRFAMsi TIGR00087. surE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSURE_ECOLI
AccessioniPrimary (citable) accession number: P0A840
Secondary accession number(s): P36664, Q2MA85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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