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P0AE72

- MAZE_ECOLI

UniProt

P0AE72 - MAZE_ECOLI

Protein

Antitoxin MazE

Gene

mazE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Antitoxin component of a toxin-antitoxin (TA) module. Labile antitoxin that binds to the MazF mRNA interferase toxin and neutralizes its endoribonuclease activity. Is considered to be an 'addiction' molecule as the cell will die in its absence. The endoribonuclease activity (MazF, a toxin) is inhibited by the labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium the overexpression of MazF leads to programmed cell death. Cell growth and viability are not affected when MazF and MazE are coexpressed. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their transcription.
    Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation, while MazE-MazF is also implicated in cell death in liquid media.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10571-MONOMER.
    ECOL316407:JW2754-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antitoxin MazE
    Gene namesi
    Name:mazE
    Synonyms:chpAI, chpR
    Ordered Locus Names:b2783, JW2754
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10571. mazE.

    Pathology & Biotechi

    Disruption phenotypei

    Decreased sensitivity to dramatic intracellular increases of ppGpp. Double mazE-mazF deletions survive high temperature, various DNA-damaging agents and H2O2 exposure better than wild-type cells. They produce more P1 phage than wild-type cells, while introduction of lysogens into a growing non-lysogenic deletion culture is lethal. Double mazE-mazF deletions show reduced biofilm formation, and survive antibiotic treatment in log phase better than wild-type cells.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81R → A: Binds poorly to DNA. 1 Publication
    Mutagenesisi16 – 161R → A: Does not bind to DNA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 8282Antitoxin MazEPRO_0000089649Add
    BLAST

    Post-translational modificationi

    Degraded by the ClpPA protease during steady state growth and possibly by the Lon protease during amino acid starvation.

    Expressioni

    Inductioni

    Expressed in exponentially growing cells. Induction has been reported to occur after amino acid starvation in a ppGpp-independent fashion and to be Lon protease-dependent (PubMed:12972253), but also to not occur after amino acid starvation and to be regulated by ppGpp (PubMed:8650219). MazE alone and in combination with MazF, represses transcription of the mazE-mazF operon. Fis activates transcription. Part of the relA-mazE-mazF-mazG operon, there is also a second mazE-mazF specific promoter which is negatively autoregulated.3 Publications

    Gene expression databases

    GenevestigatoriP0AE72.

    Interactioni

    Subunit structurei

    Forms a heterohexamer composed of alternating toxin and antitoxin homodimers MazF(2)-MazE(2)-MazF2.3 Publications

    Protein-protein interaction databases

    IntActiP0AE72. 10 interactions.
    STRINGi511145.b2783.

    Structurei

    Secondary structure

    1
    82
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Beta strandi12 – 154
    Helixi19 – 246
    Helixi55 – 606
    Turni64 – 663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MVFX-ray1.65D/E1-82[»]
    1UB4X-ray1.70C1-82[»]
    ProteinModelPortaliP0AE72.
    SMRiP0AE72. Positions 2-76.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AE72.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 5145AbrB-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PemI family.Curated
    Contains 1 AbrB-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG2336.
    HOGENOMiHOG000289070.
    KOiK07172.
    OMAiPENRHEE.
    OrthoDBiEOG6Z3KS9.
    PhylomeDBiP0AE72.

    Family and domain databases

    InterProiIPR007159. AbrB-like_dom.
    [Graphical view]
    PfamiPF04014. Antitoxin-MazE. 1 hit.
    [Graphical view]
    SMARTiSM00966. SpoVT_AbrB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AE72-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIHSSVKRWG NSPAVRIPAT LMQALNLNID DEVKIDLVDG KLIIEPVRKE   50
    PVFTLAELVN DITPENLHEN IDWGEPKDKE VW 82
    Length:82
    Mass (Da):9,356
    Last modified:December 6, 2005 - v1
    Checksum:iCD452A9AA4FB362E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16450 Genomic DNA. Translation: BAA41177.1.
    J04039 Unassigned DNA. Translation: AAA03238.1.
    U29580 Genomic DNA. Translation: AAA69293.1.
    U00096 Genomic DNA. Translation: AAC75825.1.
    AP009048 Genomic DNA. Translation: BAE76857.1.
    PIRiB31996. BVECZE.
    RefSeqiNP_417263.1. NC_000913.3.
    YP_490991.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75825; AAC75825; b2783.
    BAE76857; BAE76857; BAE76857.
    GeneIDi12933307.
    947245.
    KEGGiecj:Y75_p2720.
    eco:b2783.
    PATRICi32120982. VBIEscCol129921_2883.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16450 Genomic DNA. Translation: BAA41177.1 .
    J04039 Unassigned DNA. Translation: AAA03238.1 .
    U29580 Genomic DNA. Translation: AAA69293.1 .
    U00096 Genomic DNA. Translation: AAC75825.1 .
    AP009048 Genomic DNA. Translation: BAE76857.1 .
    PIRi B31996. BVECZE.
    RefSeqi NP_417263.1. NC_000913.3.
    YP_490991.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MVF X-ray 1.65 D/E 1-82 [» ]
    1UB4 X-ray 1.70 C 1-82 [» ]
    ProteinModelPortali P0AE72.
    SMRi P0AE72. Positions 2-76.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0AE72. 10 interactions.
    STRINGi 511145.b2783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75825 ; AAC75825 ; b2783 .
    BAE76857 ; BAE76857 ; BAE76857 .
    GeneIDi 12933307.
    947245.
    KEGGi ecj:Y75_p2720.
    eco:b2783.
    PATRICi 32120982. VBIEscCol129921_2883.

    Organism-specific databases

    EchoBASEi EB0566.
    EcoGenei EG10571. mazE.

    Phylogenomic databases

    eggNOGi COG2336.
    HOGENOMi HOG000289070.
    KOi K07172.
    OMAi PENRHEE.
    OrthoDBi EOG6Z3KS9.
    PhylomeDBi P0AE72.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10571-MONOMER.
    ECOL316407:JW2754-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AE72.
    PROi P0AE72.

    Gene expression databases

    Genevestigatori P0AE72.

    Family and domain databases

    InterProi IPR007159. AbrB-like_dom.
    [Graphical view ]
    Pfami PF04014. Antitoxin-MazE. 1 hit.
    [Graphical view ]
    SMARTi SM00966. SpoVT_AbrB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence and characterization of the relA gene of Escherichia coli."
      Metzger S., Dror I.B., Aizenman E., Schreiber G., Toone M., Friesen J.D., Cashel M., Glaser G.
      J. Biol. Chem. 263:15699-15704(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
      Strain: K12.
    2. "chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100."
      Masuda Y., Miyakawa K., Nishimura Y., Ohtsubo E.
      J. Bacteriol. 175:6850-6856(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / MC1000 / ATCC 39531.
    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. "An Escherichia coli chromosomal 'addiction module' regulated by guanosine 3',5'-bispyrophosphate: a model for programmed bacterial cell death."
      Aizenman E., Engelberg-Kulka H., Glaser G.
      Proc. Natl. Acad. Sci. U.S.A. 93:6059-6063(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CLEAVAGE BY THE CLPPA PROTEASE, INTERACTION WITH MAZF, INDUCTION, OPERON STRUCTURE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    6. "The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome."
      Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G.
      J. Biol. Chem. 276:5975-5984(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTION REGULATION, DNA-BINDING, SUBUNIT.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins."
      Pedersen K., Christensen S.K., Gerdes K.
      Mol. Microbiol. 45:501-510(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ANTITOXIN.
      Strain: K12.
    8. "Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA."
      Christensen S.K., Pedersen K., Hansen F.G., Gerdes K.
      J. Mol. Biol. 332:809-819(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, POSSIBLE CLEAVAGE BY THE LON PROTEASE, DISRUPTION PHENOTYPE.
      Strain: K12 / MG1655 / ATCC 47076.
    9. "MazF-mediated cell death in Escherichia coli: a point of no return."
      Amitai S., Yassin Y., Engelberg-Kulka H.
      J. Bacteriol. 186:8295-8300(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN PROGRAMMED CELL DEATH.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    10. "MazG -- a regulator of programmed cell death in Escherichia coli."
      Gross M., Marianovsky I., Glaser G.
      Mol. Microbiol. 59:590-601(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, OPERON STRUCTURE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation."
      Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.
      PLoS ONE 4:E6785-E6785(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL DEATH, FUNCTION IN BIOFILM FORMATION, DISRUPTION PHENOTYPE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    12. "mRNA interferases, sequence-specific endoribonucleases from the toxin-antitoxin systems."
      Yamaguchi Y., Inouye M.
      Prog. Mol. Biol. Transl. Sci. 85:467-500(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH AN ANTIBODY FRAGMENT, DNA-BINDING, MUTAGENESIS OF ARG-8 AND ARG-16.
    14. "Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition."
      Kamada K., Hanaoka F., Burley S.K.
      Mol. Cell 11:875-884(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiMAZE_ECOLI
    AccessioniPrimary (citable) accession number: P0AE72
    Secondary accession number(s): P18534, Q2MA49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 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

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    External Data

    Dasty 3