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Protein

Spermidine N(1)-acetyltransferase

Gene

speG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the protection against polyamine toxicity by regulating their concentration (PubMed:7642535, PubMed:10986239). Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine (PubMed:8077207, PubMed:7052085, PubMed:6297970). It can also use polyamines such as spermine, but not putrescine (PubMed:7052085).5 Publications

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.2 Publications

Enzyme regulationi

Heat shock, alkaline shift, ethanol treatment and poor nutrient availability produce increased concentrations of monoacetylated spermidine (PubMed:2061318). Inhibited by alkaline phosphatase, N1,N(8)-bis(ethyl)spermidine (BESPD) and N1,N(12)-bis(ethyl)spermidine (BESPM) (PubMed:8077207, PubMed:6297970).3 Publications

Kineticsi

  1. KM=2 µM for AcCoA (in the presence of 3 mM spermidine at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=220 µM for spermine (in the presence of 10 µM AcCoA at pH 7.5 and 37 degrees Celsius)1 Publication
  3. KM=1290 µM for spermidine (in the presence of 10 µM AcCoA at pH 7.5 and 37 degrees Celsius)1 Publication

    Temperature dependencei

    The level of spermidine acetyltransferase activity increases at low temperature to prevent spermidine toxicity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi35 – 351Magnesium1 Publication
    Binding sitei43 – 431SubstrateBy similarity
    Metal bindingi76 – 761Magnesium1 Publication
    Sitei85 – 851Could be important for selectivity toward long polyaminesBy similarity

    GO - Molecular functioni

    • diamine N-acetyltransferase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    • N-terminal protein amino acid acetylation Source: GO_Central
    • polyamine catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:SPERMACTRAN-MONOMER.
    ECOL316407:JW1576-MONOMER.
    MetaCyc:SPERMACTRAN-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spermidine N(1)-acetyltransferase1 Publication (EC:2.3.1.572 Publications)
    Short name:
    SAT1 Publication
    Alternative name(s):
    Spermidine/spermine N(1)-acetyltransferase1 Publication
    Short name:
    SSAT1 Publication
    Gene namesi
    Name:speG
    Ordered Locus Names:b1584, JW1576
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12447. speG.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene accumulate spermidine at late stationnary phase and show a reduced cell viability due to a decrease in protein biosynthesis (PubMed:7642535). At 37 degrees Celsius, growth of mutant is normal in the presence of 0.5 or 1 mM spermidine. However, following a shift to 7 degrees Celsius, the addition of 0.5 or 1 mM spermidine results in inhibition of cellular growth or cell lysis, respectively. Furthermore, at 7 degrees Celsius, spermidine accumulation resulted in a decrease in total protein synthesis accompanied by an increase in the synthesis of the major cold shock proteins CspA, CspB, and CspG (PubMed:10986239).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 186185Spermidine N(1)-acetyltransferasePRO_0000074588Add
    BLAST

    Proteomic databases

    PaxDbiP0A951.

    Expressioni

    Inductioni

    Constitutively expressed throughout log and plateau phases of growth.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi4260234. 7 interactions.
    IntActiP0A951. 11 interactions.
    STRINGi511145.b1584.

    Structurei

    Secondary structure

    1
    186
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115Combined sources
    Helixi14 – 163Combined sources
    Helixi17 – 215Combined sources
    Beta strandi31 – 333Combined sources
    Beta strandi36 – 383Combined sources
    Helixi41 – 5010Combined sources
    Turni51 – 533Combined sources
    Beta strandi58 – 647Combined sources
    Beta strandi67 – 7812Combined sources
    Turni79 – 824Combined sources
    Beta strandi83 – 908Combined sources
    Helixi92 – 943Combined sources
    Helixi99 – 11315Combined sources
    Beta strandi118 – 1258Combined sources
    Helixi129 – 1379Combined sources
    Beta strandi141 – 15111Combined sources
    Beta strandi153 – 16513Combined sources
    Helixi166 – 1716Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4R9MX-ray2.90A/B/C1-186[»]
    ProteinModelPortaliP0A951.
    SMRiP0A951. Positions 5-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 167161N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 873Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the acetyltransferase family.Curated
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4108MK9. Bacteria.
    COG1670. LUCA.
    HOGENOMiHOG000078522.
    InParanoidiP0A951.
    KOiK00657.
    OMAiIISPEHQ.
    OrthoDBiEOG6D5G79.
    PhylomeDBiP0A951.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF13302. Acetyltransf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A951-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPSAHSVKLR PLEREDLRYV HQLDNNASVM RYWFEEPYEA FVELSDLYDK
    60 70 80 90 100
    HIHDQSERRF VVECDGEKAG LVELVEINHV HRRAEFQIII SPEYQGKGLA
    110 120 130 140 150
    TRAAKLAMDY GFTVLNLYKL YLIVDKENEK AIHIYRKLGF SVEGELMHEF
    160 170 180
    FINGQYRNAI RMCIFQHQYL AEHKTPGQTL LKPTAQ
    Length:186
    Mass (Da):21,887
    Last modified:January 23, 2007 - v2
    Checksum:i27297083B93B3752
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D25276 Genomic DNA. Translation: BAA04966.1.
    U00096 Genomic DNA. Translation: AAC74656.1.
    AP009048 Genomic DNA. Translation: BAA15286.1.
    PIRiA55345.
    RefSeqiNP_416101.1. NC_000913.3.
    WP_001138581.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74656; AAC74656; b1584.
    BAA15286; BAA15286; BAA15286.
    GeneIDi946117.
    KEGGiecj:JW1576.
    eco:b1584.
    PATRICi32118470. VBIEscCol129921_1655.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D25276 Genomic DNA. Translation: BAA04966.1.
    U00096 Genomic DNA. Translation: AAC74656.1.
    AP009048 Genomic DNA. Translation: BAA15286.1.
    PIRiA55345.
    RefSeqiNP_416101.1. NC_000913.3.
    WP_001138581.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4R9MX-ray2.90A/B/C1-186[»]
    ProteinModelPortaliP0A951.
    SMRiP0A951. Positions 5-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260234. 7 interactions.
    IntActiP0A951. 11 interactions.
    STRINGi511145.b1584.

    Proteomic databases

    PaxDbiP0A951.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74656; AAC74656; b1584.
    BAA15286; BAA15286; BAA15286.
    GeneIDi946117.
    KEGGiecj:JW1576.
    eco:b1584.
    PATRICi32118470. VBIEscCol129921_1655.

    Organism-specific databases

    EchoBASEiEB2341.
    EcoGeneiEG12447. speG.

    Phylogenomic databases

    eggNOGiENOG4108MK9. Bacteria.
    COG1670. LUCA.
    HOGENOMiHOG000078522.
    InParanoidiP0A951.
    KOiK00657.
    OMAiIISPEHQ.
    OrthoDBiEOG6D5G79.
    PhylomeDBiP0A951.

    Enzyme and pathway databases

    BioCyciEcoCyc:SPERMACTRAN-MONOMER.
    ECOL316407:JW1576-MONOMER.
    MetaCyc:SPERMACTRAN-MONOMER.

    Miscellaneous databases

    PROiP0A951.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF13302. Acetyltransf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Properties and structure of spermidine acetyltransferase in Escherichia coli."
      Fukuchi J., Kashiwagi K., Takio K., Igarashi K.
      J. Biol. Chem. 269:22581-22585(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "Occurrence and induction of spermidine-N1-acetyltransferase in Escherichia coli."
      Matsui I., Kamei M., Otani S., Morisawa S., Pegg A.E.
      Biochem. Biophys. Res. Commun. 106:1155-1160(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    6. "Inactivation of spermidine N1-acetyltransferase with alkaline phosphatase."
      Matsui I., Otani S., Kamei M., Morisawa S.
      FEBS Lett. 150:211-213(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    7. "Spermidine acetylation in response to a variety of stresses in Escherichia coli."
      Carper S.W., Willis D.G., Manning K.A., Gerner E.W.
      J. Biol. Chem. 266:12439-12441(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INDUCTION.
      Strain: K12.
    8. "Decrease in cell viability due to the accumulation of spermidine in spermidine acetyltransferase-deficient mutant of Escherichia coli."
      Fukuchi J., Kashiwagi K., Yamagishi M., Ishihama A., Igarashi K.
      J. Biol. Chem. 270:18831-18835(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
    9. "Spermidine acetyltransferase is required to prevent spermidine toxicity at low temperatures in Escherichia coli."
      Limsuwun K., Jones P.G.
      J. Bacteriol. 182:5373-5380(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
    10. "Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli."
      Niiyama M., Sugiyama S., Hirose M., Ishikawa S., Tomitori H., Higashi K., Yamashita T., Adachi H., Takano K., Murakami S., Murata M., Inoue T., Mori Y., Kashiwagi K., Matsumura H., Igarashi K.
      Acta Crystallogr. F 69:884-887(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT.
      Strain: K12.

    Entry informationi

    Entry nameiATDA_ECOLI
    AccessioniPrimary (citable) accession number: P0A951
    Secondary accession number(s): P37354
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: January 20, 2016
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Acetylation neutralizes the charge of the polyamine, which is then typically excreted from the cell.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.