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P0A840

- SURE_ECOLI

UniProt

P0A840 - SURE_ECOLI

Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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.
    A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
    (Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.

    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.

    Kineticsi

    1. KM=0.32 mM for 5'-AMP1 Publication
    2. KM=0.26 mM for 5'-GMP1 Publication
    3. KM=0.28 mM for 5'-dGMP1 Publication
    4. KM=0.10 mM for 3'-AMP1 Publication
    5. KM=0.37 mM for 3'-CMP1 Publication
    6. KM=2.49 mM for pNPP1 Publication
    7. KM=0.02 mM for polyphosphate1 Publication

    Vmax=10.0 µmol/min/mg enzyme with 5'-AMP as substrate1 Publication

    Vmax=22.4 µmol/min/mg enzyme with 5'-GMP as substrate1 Publication

    Vmax=16.4 µmol/min/mg enzyme with 5'-dGMP as substrate1 Publication

    Vmax=20.1 µmol/min/mg enzyme with 3'-AMP as substrate1 Publication

    Vmax=12.1 µmol/min/mg enzyme with 3'-CMP as substrate1 Publication

    Vmax=7.24 µmol/min/mg enzyme with pNPP as substrate1 Publication

    Vmax=0.10 µmol/min/mg enzyme with polyphosphate as substrate1 Publication

    pH dependencei

    Optimum pH is 7.0-7.2 for nucleotidase activity.1 Publication

    Sites

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

    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 Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2532535'/3'-nucleotidase SurEPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SurE nucleotidase family.Curated

    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

    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: October 1, 2014
    This is version 76 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).Curated

    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