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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)DescriptionActionsGraphical viewLength
    Metal bindingi35Magnesium1 Publication1
    Binding sitei43SubstrateBy similarity1
    Metal bindingi76Magnesium1 Publication1
    Sitei85Could be important for selectivity toward long polyaminesBy similarity1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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 stationary 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)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000745882 – 186Spermidine N(1)-acetyltransferaseAdd BLAST185

    Proteomic databases

    PaxDbiP0A951.
    PRIDEiP0A951.

    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 interactors.
    IntActiP0A951. 11 interactors.
    STRINGi511145.b1584.

    Structurei

    Secondary structure

    1186
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 11Combined sources5
    Helixi14 – 16Combined sources3
    Helixi17 – 21Combined sources5
    Beta strandi31 – 33Combined sources3
    Beta strandi36 – 38Combined sources3
    Helixi41 – 50Combined sources10
    Turni51 – 53Combined sources3
    Beta strandi58 – 64Combined sources7
    Beta strandi67 – 78Combined sources12
    Turni79 – 82Combined sources4
    Beta strandi83 – 90Combined sources8
    Helixi92 – 94Combined sources3
    Helixi99 – 113Combined sources15
    Beta strandi118 – 125Combined sources8
    Helixi129 – 137Combined sources9
    Beta strandi141 – 151Combined sources11
    Beta strandi153 – 165Combined sources13
    Helixi166 – 171Combined sources6

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini7 – 167N-acetyltransferasePROSITE-ProRule annotationAdd BLAST161

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni85 – 87Substrate bindingBy similarity3

    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.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4R9MX-ray2.90A/B/C1-186[»]
    ProteinModelPortaliP0A951.
    SMRiP0A951.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260234. 7 interactors.
    IntActiP0A951. 11 interactors.
    STRINGi511145.b1584.

    Proteomic databases

    PaxDbiP0A951.
    PRIDEiP0A951.

    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.
    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...

    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: November 2, 2016
    This is version 92 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.